Influenza Infection (Homo sapiens)

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3058, 59507, 32573014633, 16, 17, 2425, 35, 37, 482145, 68436, 56, 60, 659, 23, 38, 4630306133, 4330191, 26, 42, 693212, 13, 42, 697111663, 17, 44, 64328, 15, 65726, 67, 7041, 52, 7314341410, 49, 52, 535728, 40315, 14, 2955227, 37, 39, 51, 6420, 5222, 6754Gycosylated NA Tetramer Cleaved Trimeric palmitylated HA NPLipid Raft Gycosylated NA Tetramer vRNA vRNP destined for Export Gycosylated NA Tetramer vRNP destined for Export Glycosylated, palmitylated and folded HA trimerLipid Raft Complex palmitylated M2 Tetramer endocytic vesicle membraneGycosylated NA Tetramer TFIIF Elongated vRNA-mRNA Complex Ribonucleoprotein Trimeric palmitylated HA RNP ComplexKaryopherin alpha vRNA palmitylated M2 Tetramer Cleaved Trimeric palmitylated HA Influenza A Viral Envelope With An Inter-Membrane Spanning HA2 M2 Tetramer Glycosylated, palmitylated and folded HA trimer vRNPM1 for Export Glycosylated, palmitylated and folded HA trimer Viral Proteins Segment 4 RNP RNA Polymerase II holoenzyme complex Viral Polymerase vRNPM1NEP Ribonucleoprotein vRNA Ran GTPaseGTP cytosolRNPKaryopherin alphaKaryopherin beta complex vRNA Gycosylated NA Tetramer Glycosylated and folded HA trimer Viral Polymerase vRNPM1NEP vRNA TFIIF Crm1Ran GTPaseGDP vRNA Ribonucleoprotein vRNA Segment 3 RNP Gycosylated NA Tetramer Influenza A Viral Envelope Fused With The Endocytic Vesicle Membrane By An Inter-Membrane Spanning HA2 Ribonucleoprotein Viral Polymerase vRNP Influenza A Viral Envelope vRNPM1NEPNP vRNA capped, methylated pre-mRNACBC Complex Initiated cRNA-vRNA Complex Nup107 Complex Membrane Spanning Cleaved Trimeric palmitylated HA RNA Polymerase II vRNA Nuclear Pore Complex vRNA Gycosylated NA TetramerLipid Raft Influenza A Viral Envelope with a fusion competent HA2 Influenza A Viral Envelope U1 snRNP snRNP Sm core complex Membrane Spanning Cleaved Trimeric palmitylated HA Gycosylated NA Tetramer Ribonucleoprotein Glycosylated NA Tetramer Membrane Spanning Cleaved Trimeric palmitylated HA Gycosylated NA Tetramer Acidified Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore Gycosylated NA Tetramer Clathrin Gycosylated NA TetramerLipid Raft RNP ComplexKaryopherin alpha Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore RNP ComplexKaryopherin alpha Segment 1 RNP Fusion Competent Cleaved Trimeric palmitylated HA Viral Polymerase Post Fusion Cleaved Trimeric palmitylated HA Influenza A Viral Envelope Inserted Into The Endocytic Vesicle Membrane RNPKaryopherin alphaKaryopherin beta complex RNP pre-assembly complex vRNA Ribonucleoprotein Membrane enveloped Influenza Virion RNP complex Segment 2 RNP Glycosylated, palmitylated and folded HA trimerLipid Raft Complex Influenza A Viral Particle Glycosylated and folded HA trimer Golgi membraneRNA Polymerase II Nup62 Complex vRNPM1 for Export palmitylated M2 Tetramer RNA polymerase II Segment 5 RNP Glycosylated NA Tetramer palmitylated M2 Tetramer cRNP Ribonucleoprotein Glycosylated NA Tetramer vRNP Export Complex cRNP Ribonucleoprotein M2 Tetramer M2 Tetramer Glycosylated, palmitylated and folded HA trimer vRNA Cap Binding Complex Glycosylated, palmitylated and folded HA trimer Elongating viral mRNA Ribonucleoprotein Cleaved HA Influenza A Viral Particle M2 Tetramer Cleaved HA Influenza A Viral Particle Cleaved Trimeric palmitylated HA Spliceosomal E Complex RNA Polymerase II holoenzyme complex Glycosylated NA Tetramer palmitylated M2 Tetramer Ribonucleoprotein vRNA palmitylated M2 Tetramer 80S ribosome Influenza A Viral Particle With A Fusion Competent HA2 vRNA Ribonucleoprotein vRNPM1 for Export palmitylated M2 Tetramer vRNA Sialic Acid Bound Influenza A Viral Particle Initiated vRNA Transcription Complex Ribonucleoprotein Gycosylated NA Tetramer palmitylated M2 Tetramer vRNA Transcription Complex vRNA Segment 6 RNP vRNA Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane Initiated vRNA-cRNA Complex Influenza A Viral Envelope Fused With The Endocytic Vesicle Membrane By An Inter-Membrane Spanning HA2 vRNP destined for Export 40S ribosomal complex Sialic Acid Bound Influenza A Viral Particle vRNA Glycosylated, palmitylated and folded HA trimer Ribonucleoprotein Influenza A Viral Envelope palmitylated M2 Tetramer Gycosylated NA Tetramer vRNA Viral Polymerase palmitylated M2 Tetramer Influenza A Viral Particle Glycosylated and folded HA trimer Segment 7 RNP Influenza A Viral Envelope Intracellular assembly complex vRNP destined for Export palmitylated M2 Tetramer vRNA endoplasmic reticulum membraneNPLipid Raft Viral Polymerase palmitylated M2 Tetramer Segment 8 RNP vRNA Gycosylated NA Tetramer 60S ribosomal complex Cleaved Trimeric palmitylated HA Glycosylated NA Tetramer nucleoplasmHA folded, glycosylated, and palmitylated PB2 M1 mRNA PB2 PB2 Glycosylated, palmitylated and folded HA trimerM2 NP Genomic RNA Segment 1 Genomic RNA Segment 6 Genomic RNA Segment 7 SA RPS4Y1NEP/NS2PB1 Genomic RNA Segment 3 HA folded, glycosylated, and palmitylated GTF2F1POLR2C Genomic RNA Segment 8 SEH1L-2 PA Genomic RNA Segment 2 HA folded, glycosylated, and palmitylated Glycosylated NA M2 Genomic RNA Segment 3 HNRNPK Lipid RaftPOLR2E Initiated cRNA-vRNA ComplexCCAR1 Genomic RNA Segment 8 Genomic RNA Segment 1 PB2 NP Genomic RNA Segment 8 NP Genomic RNA Segment 6 Genomic RNA Segment 8 RNPKaryopherin alphaKaryopherin beta complexPOLR2L RPS14 M1 PA viral mRNARPS29 M1 M2 M1Genomic RNA Segment 7 PB1 NP Genomic RNA Segment 8 Genomic RNA Segment 6 2xMe-SNRPB RNPS1 POLR2J Genomic RNA Segment 4 RPL13Genomic RNA Segment 5 PA Influenza A Viral ParticleHA1 Genomic RNA Segment 7 POLR2G NP PA HNRNPU HA1 Genomic RNA Segment 6 Genomic RNA Segment 6 NP U1 snRNA Genomic RNA Segment 4 Genomic RNA Segment 8 Sialic Acid Bound Influenza A Viral ParticleKPNB12xMe-SNRPD1 Genomic RNA Segment 8 PB1 PTBP1 NS1Ran GTPaseGTPRPS24 RPS20 NUP107 Genomic RNA Segment 8 RPS12 PA PB2 PB2 PB1PB1 Genomic RNA Segment 8 NP M2 Genomic RNA Segment 5 Influenza A Viral Envelope Inserted Into The Endocytic Vesicle MembranePA RPL39 RPL3LNP Segment 5 RNP18S rRNA NP PA HA2 Genomic RNA Segment 7 NEP/NS2 XPO1 PB2 NUP62 NEP/NS2 NUP133 Inter-Membrane Spanning HA2 NASRSF1 M2 Glycosylated NA Genomic RNA Segment 1 NUP85 Genomic RNA Segment 8 Genomic RNA Segment 1 Genomic RNA Segment 1 M1 vRNA Transcription ComplexRAN POLR2A SRSF7 KPNA1 HA1 Genomic RNA Segment 6 POLR2J SRSF9 POM121 vRNP Export ComplexGenomic RNA Segment 7 M1 SNRNP70 NUP98-5 RPLP1NP mRNA Glycosylated, palmitylated and folded HA trimerLipid Raft ComplexInfluenza A Viral ParticlePCBP2 RNPKaryopherin alphaKaryopherin beta complexPB2 NEP/NS2 XPO1M2 mRNAPB2 Genomic RNA Segment 7 Genomic RNA Segment 4 Genomic RNA Segment 6 Genomic RNA Segment 4 POLR2G RPS27AGenomic RNA Segment 3 Acidified Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open PoreSegment 1 RNPPA NUP210 Glycosylated NA TetramerSNRPD2 palmitylated M2 NCBP2 Glycosylated and folded HA trimerGenomic RNA Segment 8 Genomic RNA Segment 5 Genomic RNA Segment 1 M1 PB1 POLR2DPB1 M1 PA Genomic RNA Segment 3 Gycosylated NA TetramerPB1 PA Genomic RNA Segment 1 M1 Genomic RNA Segment 2 M2 NP HA folded, glycosylated, and palmitylated M2 RPL7 RPL34 palmitylated M2 Genomic RNA Segment 6 PA HA2 Genomic RNA Segment 4 Glycosylated NA POLR2K PB1 viral mRNAPB2 NP M1 RPL18A Influenza cRNA AAAS PB1 RPS3A vRNPM1NEPHA2 Genomic RNA Segment 1 PB1 RPL26 Genomic RNA Segment 2 M2 mRNA Glycosylated NA NUP37 Genomic RNA Segment 3 NP HA2 PA NA RPL22 SNRPA RPS17 RPL19 Genomic RNA Segment 7 Genomic RNA Segment 2 Genomic RNA Segment 7 NEP/NS2NUPL2 HSPA1AGenomic RNA Segment 4 Genomic RNA Segment 1 NP Mature intronless transcript derived mRNA with m7G cap removedNP Genomic RNA Segment 1 M1 Genomic RNA Segment 6 Gycosylated NA TetramerLipid RaftNP RPL30HNRNPFGenomic RNA Segment 4 Genomic RNA Segment 5 UBA52palmitylated M2 Genomic RNA Segment 7 HAGenomic RNA Segment 2 RNP ComplexKaryopherin alphaRPS18 PiInfluenza A Viral Particle Docked At The Endocytic Vesicle MembraneGenomic RNA Segment 7 HSP90AA1PB1 Genomic RNA Segment 6 KPNB1 M1 NEP/NS2 POLR2E H+KPNB1 Genomic RNA Segment 2 NS2 mRNA M1 PB2Genomic RNA Segment 1 Genomic RNA Segment 8 28S rRNA Aminoacyl-tRNAGenomic RNA Segment 3 Genomic RNA Segment 4 PB1 GTP Initiated vRNA-cRNA ComplexGenomic RNA Segment 5 NEP/NS2 NP RANBP2 PA Genomic RNA Segment 2 RPLP2 NUP35 Genomic RNA Segment 5 PA M1 NUP155 Segment 6 RNPNEP/NS2 palmitylated M2 M1 Genomic RNA Segment 7 SRRM1 PA PB1-F2POLR2H Glycosylated NARPS21 Genomic RNA Segment 7 NUPL1-2 M1 RPL10 PA Genomic RNA Segment 5 Genomic RNA Segment 2 NUP88 PB1 POLR2H Genomic RNA Segment 8 HA1 PB2 PA Genomic RNA Segment 3 PB2 POLR2I POLR2FRPL38 Genomic RNA Segment 2 Glycosylated NA NUP205HA1 PB2 Segment 4 RNPNUP153 Genomic RNA Segment 6 Genomic RNA Segment 2 NEP/NS2 RNA Polymerase II CANXNS2 mRNAGenomic RNA Segment 3 Genomic RNA Segment 8 Genomic RNA Segment 6 NP GTF2F2HNRNPD Genomic RNA Segment 5 PA PA NP NA mRNA Genomic RNA Segment 1 Genomic RNA Segment 7 PB2 Genomic RNA Segment 4 U2AF1 M1 POLR2L NP Genomic RNA Segment 4 POLR2FHA2 PB2 NUP50 NUP214 Genomic RNA Segment 3 NP RPS6 Genomic RNA Segment 8 RPS9 Genomic RNA Segment 4 NUP43 Segment 2 RNPNP RPL9 RPS7 Genomic RNA Segment 1 RPL36 Genomic RNA Segment 8 RPL4 PB2 RPL35A SNRPG RPL3 HNRNPC Genomic RNA Segment 8 Genomic RNA Segment 4 Genomic RNA Segment 6 Genomic RNA Segment 4 M1Genomic RNA Segment 5 Genomic RNA Segment 5 Genomic RNA Segment 7 Genomic RNA Segment 5 YBX1 NP PA M1 mRNAGenomic RNA Segment 5 DNAJC3NPLipid RaftGenomic RNA Segment 5 Genomic RNA Segment 3 Genomic RNA Segment 2 NUP188RPS10 Genomic RNA Segment 4 KPNA1 RPS15 Host Derived Lipid Bilayer Membrane Rich In Sphingolipids And CholesterolGenomic RNA Segment 6 Genomic RNA Segment 1 RPL41 Genomic RNA Segment 1 Genomic RNA Segment 3 PA PB1 Genomic RNA Segment 2 Genomic RNA Segment 1 PA HNRNPL palmitylated M2 TetramerNPPA RPS16 HNRNPH1Genomic RNA Segment 7 Genomic RNA Segment 6 Genomic RNA Segment 6 SRSF2 Spliceosomal E ComplexGenomic RNA Segment 7 Genomic RNA Segment 5 NEP/NS2 Genomic RNA Segment 8 NP PB2 palmitylated M2 NPNP RPL12 PB2 RPS2Elongated vRNA-mRNA ComplexRPL23 PB2 Genomic RNA Segment 5 Genomic RNA Segment 8 GTF2F1RPL31 RPL21 PANEP/NS2 Genomic RNA Segment 3 RPL37A M2 TetramerGlycosylated NA PB2 RPS13Genomic RNA Segment 4 NP PAGenomic RNA Segment 3 M1 NP RPL11 Segment 3 RNPDHX9 Genomic RNA Segment 2 Genomic RNA Segment 3 Genomic RNA Segment 2 Genomic RNA Segment 2 NEP/NS2 POLR2DNP Genomic RNA Segment 3 NA Ribonucleoprotein PB1 Genomic RNA Segment 7 HNRNPUL1 FAU Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open PoreGenomic RNA Segment 4 Glycosylated NA GTF2F2SRSF6 NEP/NS2 Genomic RNA Segment 4 RNP pre-assembly complexGenomic RNA Segment 3 5.8S rRNA vRNPM1 for ExportNP RPL26L1Genomic RNA Segment 7 HNRNPA1 Glycosylated, palmitylated and folded HA trimerRAE1 RPL8 NEP/NS2Genomic RNA Segment 3 HA1 Genomic RNA Segment 2 Glycosylated NA Segment 7 RNPRPLP0 NEP/NS2 Genomic RNA Segment 1 NEP/NS2 M1 XPO1 Intracellular assembly complexPB1 Genomic RNA Segment 2 Genomic RNA Segment 8 RPL18 M2 RPS5NEP/NS2 HA1 RPS3 NP 7-methylguanosine cap CALRInter-Membrane Spanning HA2 P1 mRNA Genomic RNA Segment 4 NP NP Influenza A Viral Particle With A Fusion Competent HA2Genomic RNA Segment 3 SRSF5 RPL36A Genomic RNA Segment 8 Genomic RNA Segment 8 Genomic RNA Segment 7 PB1 RPL10A Genomic RNA Segment 2 PB2 NEP/NS2 vRNA RBM5 NP Genomic RNA Segment 1 Genomic RNA Segment 6 ALYREF Glycosylated NA Gycosylated NA TetramerLipid RaftGlycosylated NA TetramerGenomic RNA Segment 1 Genomic RNA Segment 2 POLR2K Genomic RNA Segment 4 NS1 mRNA PB2 PB1 Genomic RNA Segment 2 Genomic RNA Segment 1 PB1 NS1 mRNASRSF3 SUGP1 HNRNPA0 NEP/NS2 Genomic RNA Segment 6 2xMe-SNRPD3 IPO5Genomic RNA Segment 4 M1 NP Genomic RNA Segment 7 Genomic RNA Segment 2 PB1 PB1 M1 Genomic RNA Segment 7 PA cRNPRPL27A Genomic RNA Segment 1 Genomic RNA Segment 4 RPL13A NFX.1 PB2 RPS28 p-S5-POLR2A PB1 Segment 8 RNPGenomic RNA Segment 3 Genomic RNA Segment 2 PB1 PB2 HNRNPA3 Genomic RNA Segment 3 RPL35 M1 PB2 PB2 RPL23A RPL14 Genomic RNA Segment 4 H+TPR PB2 RPS4X Genomic RNA Segment 7 PB2 Genomic RNA Segment 5 RPL37 NP PB1 NA RPS15A Genomic RNA Segment 3 Genomic RNA Segment 8 GRSF1M2PB1 SA Genomic RNA Segment 7 Genomic RNA Segment 1 RPL24 PA PB1 RPL28 PB1 Glycosylated and folded HARBMXM2 RPS27 Genomic RNA Segment 1 RPS11 RPL5 Genomic RNA Segment 2 Glycosylated and folded HA PB2 PB2 NP80S ribosomeRAN POLR2B RPS26 CD2BP2 M2 PA RPL27PB1 mRNAGenomic RNA Segment 4 Ribonucleoprotein Genomic RNA Segment 4 Genomic RNA Segment 2 CLTA U2AF2 RPL15KPNA1Genomic RNA Segment 3 Genomic RNA Segment 8 Genomic RNA Segment 6 PA Genomic RNA Segment 6 NEP/NS2 PA mRNA PB1 PB2 PB2 Genomic RNA Segment 3 FUS Glycosylated NA HNRNPA2B1 PB2 PA Genomic RNA Segment 8 HA folded, glycosylated, and palmitylated HNRNPH2 Glycosylated, palmitylated and folded HA trimerLipid Raft ComplexHNRNPR RPS23 Genomic RNA Segment 8 ClathrinGenomic RNA Segment 7 Genomic RNA Segment 6 SNRPE Crm1Ran GTPaseGDPRPL32 NEP/NS2 Glycosylated NA Genomic RNA Segment 8 NPLipid RaftGenomic RNA Segment 2 NUP54 NP Inter-Membrane Spanning HA2 PA vRNPM1NEPNPHNRNPM RPS19 NEP/NS2 PA Genomic RNA Segment 3 HA1 NAvRNP destined for ExportPB1 M1 Initiated vRNA Transcription ComplexNA M1 Genomic RNA Segment 1 PCBP1 PB1 Genomic RNA Segment 6 Cleaved HA Influenza A Viral Particlepalmitylated M2 NEP/NS2 5S rRNA Genomic RNA Segment 5 Nup45 PB2 PB1 vRNPvRNA POLR2C M1KPNB1NP M1HA1 Genomic RNA Segment 5 GDP Genomic RNA Segment 7 NP SNRPF SARPS25 NS1 Genomic RNA Segment 5 HA folded and glycosylated M1 NP HA folded and glycosylated Inter-Membrane Spanning HA2 NP SMC1A Sialic Acid Bound Influenza A Viral ParticlePB1 Genomic RNA Segment 5 Genomic RNA Segment 5 PB1 POLR2I Genomic RNA Segment 8 PB1RPL29 Glycosylated NA TetramerGenomic RNA Segment 1 Genomic RNA Segment 5 palmitylated M2 RPL7A RPSA PB1 Mature intronless transcript derived mRNAGlycosylated and folded HA trimerpalmitylated M2 TetramerHA folded, glycosylated, and palmitylated Genomic RNA Segment 3 Genomic RNA Segment 2 NUP160 Genomic RNA Segment 4 Genomic RNA Segment 1 Genomic RNA Segment 6 Genomic RNA Segment 7 M1 KPNA1NS2 mRNAPB2 PB2Genomic RNA Segment 5 Genomic RNA Segment 4 Genomic RNA Segment 5 RPL17 Genomic RNA Segment 4 PB1 Genomic RNA Segment 6 NTPGenomic RNA Segment 3 Genomic RNA Segment 5 NUP93 Glycosylated NA NEP/NS2 NEP/NS2 HA mRNA NEP/NS2 Genomic RNA Segment 1 Genomic RNA Segment 2 Genomic RNA Segment 5 Glycosylated and folded HA trimerPB1 Nuclear Pore Complex Genomic RNA Segment 6 H+ PB2 Genomic RNA Segment 5 SAM2 mRNANA RPS8PA Viral ProteinsPA PA M2 TetramerNP Viral PolymeraseGenomic RNA Segment 3 PA Genomic RNA Segment 4 KPNA1 PA POLR2B M2 TetramerGenomic RNA Segment 6 NCBP1 PA Genomic RNA Segment 7 Genomic RNA Segment 6 RPL6 18, 47, 62


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Wikipathways-description 
The virus particle initially associates with a human host cell by binding to sialic acid-containing receptors on the host cell surface. The bound virus is endocytosed by one of four distinct mechanisms. The low endosomal pH sets in motion a number of steps that lead to viral membrane fusion mediated by the viral hemagglutinin (HA) protein, and the eventual release of the uncoated viral ribonucleoprotein complex into the cytosol of the host cell. The ribonucleoprotein complex is transported through the nuclear pore into the nucleus. Once in the nucleus, the incoming negative-sense viral RNA (vRNA) is transcribed into messenger RNA (mRNA) by a primer-dependent mechanism. Replication occurs via a two step process. A full-length complementary RNA (cRNA), a positive-sense copy of the vRNA, is first made and this in turn is used as a template to produce more vRNA. The viral proteins are expressed and processed and eventually assemble with vRNAs at budding sites within the host cell membrane. The viral protein complexes and ribonucleoproteins are assembled into viral particles and bud from the host cell, enveloped in the host cell's membrane.

This release contains a framework for the further annotation of the viral life-cycle.

Original Pathway at Reactome: http://www.reactome.org/PathwayBrowser/#DB=gk_current&FOCUS_SPECIES_ID=48887&FOCUS_PATHWAY_ID=168255

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Bibliography

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  59. Yasuda J, Nakada S, Kato A, Toyoda T, Ishihama A.; ''Molecular assembly of influenza virus: association of the NS2 protein with virion matrix.''; PubMed Europe PMC Scholia
  60. Sugrue RJ, Belshe RB, Hay AJ.; ''Palmitoylation of the influenza A virus M2 protein.''; PubMed Europe PMC Scholia
  61. Chen W, Calvo PA, Malide D, Gibbs J, Schubert U, Bacik I, Basta S, O'Neill R, Schickli J, Palese P, Henklein P, Bennink JR, Yewdell JW.; ''A novel influenza A virus mitochondrial protein that induces cell death.''; PubMed Europe PMC Scholia
  62. Luo C, Nobusawa E, Nakajima K.; ''An analysis of the role of neuraminidase in the receptor-binding activity of influenza B virus: the inhibitory effect of Zanamivir on haemadsorption.''; PubMed Europe PMC Scholia
  63. Marjuki H, Alam MI, Ehrhardt C, Wagner R, Planz O, Klenk HD, Ludwig S, Pleschka S.; ''Membrane accumulation of influenza A virus hemagglutinin triggers nuclear export of the viral genome via protein kinase Calpha-mediated activation of ERK signaling.''; PubMed Europe PMC Scholia
  64. Suntharalingam M, Wente SR.; ''Peering through the pore: nuclear pore complex structure, assembly, and function.''; PubMed Europe PMC Scholia
  65. Li ML, Rao P, Krug RM.; ''The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits.''; PubMed Europe PMC Scholia
  66. Melén K, Kinnunen L, Fagerlund R, Ikonen N, Twu KY, Krug RM, Julkunen I.; ''Nuclear and nucleolar targeting of influenza A virus NS1 protein: striking differences between different virus subtypes.''; PubMed Europe PMC Scholia
  67. Palese P, Compans RW.; ''Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): mechanism of action.''; PubMed Europe PMC Scholia
  68. Nilsson J, Askjaer P, Kjems J.; ''A role for the basic patch and the C terminus of RanGTP in regulating the dynamic interactions with importin beta, CRM1 and RanBP1.''; PubMed Europe PMC Scholia
  69. Li N, Ren A, Wang X, Fan X, Zhao Y, Gao GF, Cleary P, Wang B.; ''Influenza viral neuraminidase primes bacterial coinfection through TGF-β-mediated expression of host cell receptors.''; PubMed Europe PMC Scholia
  70. Kosinski J, Mosalaganti S, von Appen A, Teimer R, DiGuilio AL, Wan W, Bui KH, Hagen WJ, Briggs JA, Glavy JS, Hurt E, Beck M.; ''Molecular architecture of the inner ring scaffold of the human nuclear pore complex.''; PubMed Europe PMC Scholia
  71. DONALD HB, ISAACS A.; ''Counts of influenza virus particles.''; PubMed Europe PMC Scholia
  72. Chanturiya AN, Basañez G, Schubert U, Henklein P, Yewdell JW, Zimmerberg J.; ''PB1-F2, an influenza A virus-encoded proapoptotic mitochondrial protein, creates variably sized pores in planar lipid membranes.''; PubMed Europe PMC Scholia
  73. Stegmann T, Morselt HW, Scholma J, Wilschut J.; ''Fusion of influenza virus in an intracellular acidic compartment measured by fluorescence dequenching.''; PubMed Europe PMC Scholia
  74. Veit M, Klenk HD, Kendal A, Rott R.; ''The M2 protein of influenza A virus is acylated.''; PubMed Europe PMC Scholia
  75. Enami M, Sharma G, Benham C, Palese P.; ''An influenza virus containing nine different RNA segments.''; PubMed Europe PMC Scholia
  76. Braam J, Ulmanen I, Krug RM.; ''Molecular model of a eucaryotic transcription complex: functions and movements of influenza P proteins during capped RNA-primed transcription.''; PubMed Europe PMC Scholia
  77. Neumann G, Brownlee GG, Fodor E, Kawaoka Y.; ''Orthomyxovirus replication, transcription, and polyadenylation.''; PubMed Europe PMC Scholia
  78. Garman E, Laver G.; ''Controlling influenza by inhibiting the virus's neuraminidase.''; PubMed Europe PMC Scholia
  79. Ward AC, Castelli LA, Lucantoni AC, White JF, Azad AA, Macreadie IG.; ''Expression and analysis of the NS2 protein of influenza A virus.''; PubMed Europe PMC Scholia
  80. Martin K, Helenius A.; ''Transport of incoming influenza virus nucleocapsids into the nucleus.''; PubMed Europe PMC Scholia
  81. Perez DR, Donis RO.; ''Functional analysis of PA binding by influenza a virus PB1: effects on polymerase activity and viral infectivity.''; PubMed Europe PMC Scholia
  82. Nemeroff ME, Barabino SM, Li Y, Keller W, Krug RM.; ''Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs.''; PubMed Europe PMC Scholia
  83. Watanabe K, Takizawa N, Katoh M, Hoshida K, Kobayashi N, Nagata K.; ''Inhibition of nuclear export of ribonucleoprotein complexes of influenza virus by leptomycin B.''; PubMed Europe PMC Scholia
  84. Vreede FT, Brownlee GG.; ''Influenza virion-derived viral ribonucleoproteins synthesize both mRNA and cRNA in vitro.''; PubMed Europe PMC Scholia
  85. Plotch SJ, Bouloy M, Ulmanen I, Krug RM.; ''A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription.''; PubMed Europe PMC Scholia
  86. Amorim MJ, Read EK, Dalton RM, Medcalf L, Digard P.; ''Nuclear export of influenza A virus mRNAs requires ongoing RNA polymerase II activity.''; PubMed Europe PMC Scholia
  87. Zhang J, Lamb RA.; ''Characterization of the membrane association of the influenza virus matrix protein in living cells.''; PubMed Europe PMC Scholia
  88. González S, Zürcher T, Ortín J.; ''Identification of two separate domains in the influenza virus PB1 protein involved in the interaction with the PB2 and PA subunits: a model for the viral RNA polymerase structure.''; PubMed Europe PMC Scholia
  89. Petosa C, Schoehn G, Askjaer P, Bauer U, Moulin M, Steuerwald U, Soler-López M, Baudin F, Mattaj IW, Müller CW.; ''Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex.''; PubMed Europe PMC Scholia
  90. Carrasco M, Amorim MJ, Digard P.; ''Lipid raft-dependent targeting of the influenza A virus nucleoprotein to the apical plasma membrane.''; PubMed Europe PMC Scholia
  91. Mikulásová A, Varecková E, Fodor E.; ''Transcription and replication of the influenza a virus genome.''; PubMed Europe PMC Scholia
  92. Nakagawa Y, Oda K, Nakada S.; ''The PB1 subunit alone can catalyze cRNA synthesis, and the PA subunit in addition to the PB1 subunit is required for viral RNA synthesis in replication of the influenza virus genome.''; PubMed Europe PMC Scholia
  93. Veit M, Kretzschmar E, Kuroda K, Garten W, Schmidt MF, Klenk HD, Rott R.; ''Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin.''; PubMed Europe PMC Scholia
  94. Palese P, Tobita K, Ueda M, Compans RW.; ''Characterization of temperature sensitive influenza virus mutants defective in neuraminidase.''; PubMed Europe PMC Scholia
  95. Pritlove DC, Fodor E, Seong BL, Brownlee GG.; ''In vitro transcription and polymerase binding studies of the termini of influenza A virus cRNA: evidence for a cRNA panhandle.''; PubMed Europe PMC Scholia
  96. Schmitt AP, Lamb RA.; ''Escaping from the cell: assembly and budding of negative-strand RNA viruses.''; PubMed Europe PMC Scholia
  97. Salom D, Hill BR, Lear JD, DeGrado WF.; ''pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus.''; PubMed Europe PMC Scholia
  98. Deng T, Vreede FT, Brownlee GG.; ''Different de novo initiation strategies are used by influenza virus RNA polymerase on its cRNA and viral RNA promoters during viral RNA replication.''; PubMed Europe PMC Scholia
  99. Boulo S, Akarsu H, Ruigrok RW, Baudin F.; ''Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes.''; PubMed Europe PMC Scholia
  100. De Marcos Lousa C, Trézéguet V, Dianoux AC, Brandolin G, Lauquin GJ.; ''The human mitochondrial ADP/ATP carriers: kinetic properties and biogenesis of wild-type and mutant proteins in the yeast S. cerevisiae.''; PubMed Europe PMC Scholia
  101. Lamb RA, Lai CJ, Choppin PW.; ''Sequences of mRNAs derived from genome RNA segment 7 of influenza virus: colinear and interrupted mRNAs code for overlapping proteins.''; PubMed Europe PMC Scholia
  102. Tatu U, Hammond C, Helenius A.; ''Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment.''; PubMed Europe PMC Scholia
  103. Zheng H, Lee HA, Palese P, García-Sastre A.; ''Influenza A virus RNA polymerase has the ability to stutter at the polyadenylation site of a viral RNA template during RNA replication.''; PubMed Europe PMC Scholia
  104. Baudin F, Petit I, Weissenhorn W, Ruigrok RW.; ''In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein.''; PubMed Europe PMC Scholia
  105. Fortes P, Beloso A, Ortín J.; ''Influenza virus NS1 protein inhibits pre-mRNA splicing and blocks mRNA nucleocytoplasmic transport.''; PubMed Europe PMC Scholia
  106. Chen Z, Krug RM.; ''Selective nuclear export of viral mRNAs in influenza-virus-infected cells.''; PubMed Europe PMC Scholia
  107. Donelan NR, Basler CF, García-Sastre A.; ''A recombinant influenza A virus expressing an RNA-binding-defective NS1 protein induces high levels of beta interferon and is attenuated in mice.''; PubMed Europe PMC Scholia
  108. Mayer D, Molawi K, Martínez-Sobrido L, Ghanem A, Thomas S, Baginsky S, Grossmann J, García-Sastre A, Schwemmle M.; ''Identification of cellular interaction partners of the influenza virus ribonucleoprotein complex and polymerase complex using proteomic-based approaches.''; PubMed Europe PMC Scholia
  109. Fodor E, Pritlove DC, Brownlee GG.; ''The influenza virus panhandle is involved in the initiation of transcription.''; PubMed Europe PMC Scholia
  110. Bortz E, Westera L, Maamary J, Steel J, Albrecht RA, Manicassamy B, Chase G, Martínez-Sobrido L, Schwemmle M, García-Sastre A.; ''Host- and strain-specific regulation of influenza virus polymerase activity by interacting cellular proteins.''; PubMed Europe PMC Scholia
  111. Morris SJ, Price GE, Barnett JM, Hiscox SA, Smith H, Sweet C.; ''Role of neuraminidase in influenza virus-induced apoptosis.''; PubMed Europe PMC Scholia
  112. Takeda M, Leser GP, Russell CJ, Lamb RA.; ''Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion.''; PubMed Europe PMC Scholia
  113. Veit M, Schmidt MF.; ''Timing of palmitoylation of influenza virus hemagglutinin.''; PubMed Europe PMC Scholia
  114. Son KN, Liang Z, Lipton HL.; ''Double-Stranded RNA Is Detected by Immunofluorescence Analysis in RNA and DNA Virus Infections, Including Those by Negative-Stranded RNA Viruses.''; PubMed Europe PMC Scholia
  115. Gething MJ, McCammon K, Sambrook J.; ''Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
115105view18:57, 25 January 2021EgonwRemoved an empty reference.
114625view16:08, 25 January 2021ReactomeTeamReactome version 75
113585view08:08, 3 November 2020EgonwRemoved the empty reference (we now know this is a book that the convertor cannot handle).
113073view11:13, 2 November 2020ReactomeTeamReactome version 74
112844view05:16, 12 October 2020EgonwRemoved an empty (and unused) reference
112308view15:22, 9 October 2020ReactomeTeamReactome version 73
101951view12:13, 20 November 2018EgonwRemoved an empty reference.
101207view11:10, 1 November 2018ReactomeTeamreactome version 66
100745view20:35, 31 October 2018ReactomeTeamreactome version 65
100289view19:12, 31 October 2018ReactomeTeamreactome version 64
99835view15:56, 31 October 2018ReactomeTeamreactome version 63
99392view14:33, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99088view12:39, 31 October 2018ReactomeTeamreactome version 62
94058view13:54, 16 August 2017ReactomeTeamreactome version 61
93687view11:31, 9 August 2017ReactomeTeamreactome version 61
87172view19:26, 18 July 2016MkutmonOntology Term : 'infectious disease pathway' added !
86810view09:27, 11 July 2016ReactomeTeamreactome version 56
83087view09:57, 18 November 2015ReactomeTeamVersion54
81411view12:56, 21 August 2015ReactomeTeamVersion53
76880view08:15, 17 July 2014ReactomeTeamFixed remaining interactions
76585view11:56, 16 July 2014ReactomeTeamFixed remaining interactions
75918view09:57, 11 June 2014ReactomeTeamRe-fixing comment source
75618view10:48, 10 June 2014ReactomeTeamReactome 48 Update
74973view13:49, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74617view08:40, 30 April 2014ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
18S rRNA ProteinX03205 (EMBL)
28S rRNA ProteinM11167 (EMBL)
2xMe-SNRPB ProteinP14678 (Uniprot-TrEMBL)
2xMe-SNRPD1 ProteinP62314 (Uniprot-TrEMBL)
2xMe-SNRPD3 ProteinP62318 (Uniprot-TrEMBL)
5.8S rRNA ProteinJ01866 (EMBL)
5S rRNA ProteinV00589 (EMBL)
7-methylguanosine cap MetaboliteCHEBI:17825 (ChEBI)
80S ribosomeComplexREACT_4330 (Reactome)
AAAS ProteinQ9NRG9 (Uniprot-TrEMBL)
ALYREF ProteinQ86V81 (Uniprot-TrEMBL)
Acidified Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open PoreComplexREACT_9103 (Reactome)
Aminoacyl-tRNAMetaboliteREACT_4792 (Reactome)
CALRProteinP27797 (Uniprot-TrEMBL)
CANXProteinP27824 (Uniprot-TrEMBL)
CCAR1 ProteinQ8IX12 (Uniprot-TrEMBL)
CD2BP2 ProteinO95400 (Uniprot-TrEMBL)
CLTA ProteinP09496 (Uniprot-TrEMBL)
ClathrinComplexREACT_9338 (Reactome)
Cleaved HA Influenza A Viral ParticleComplexREACT_9239 (Reactome)
Crm1

Ran GTPase

GDP		ComplexREACT_6660 (Reactome)
DHX9 ProteinQ08211 (Uniprot-TrEMBL)
DNAJC3ProteinQ13217 (Uniprot-TrEMBL)
Elongated vRNA-mRNA ComplexComplexREACT_9568 (Reactome) Capped, synthesized RNA strand complementary to vRNA, plus viral polymerase and template vRNA (Plotch, 1977).
FAU ProteinP62861 (Uniprot-TrEMBL)
FUS ProteinP35637 (Uniprot-TrEMBL)
GDP MetaboliteCHEBI:17552 (ChEBI)
GRSF1ProteinQ12849 (Uniprot-TrEMBL)
GTF2F1ProteinP35269 (Uniprot-TrEMBL)
GTF2F2ProteinP13984 (Uniprot-TrEMBL)
GTP MetaboliteCHEBI:15996 (ChEBI)
Genomic RNA Segment 1 ProteinAF389115 (EMBL)
Genomic RNA Segment 2 ProteinAF389116 (EMBL)
Genomic RNA Segment 3 ProteinAF389117 (EMBL)
Genomic RNA Segment 4 ProteinAF389118 (EMBL)
Genomic RNA Segment 5 ProteinAF389119 (EMBL)
Genomic RNA Segment 6 ProteinAF389120 (EMBL)
Genomic RNA Segment 7 ProteinAF389121 (EMBL)
Genomic RNA Segment 8 ProteinAF389122 (EMBL)
Glycosylated NA ProteinP03468 (Uniprot-TrEMBL)
Glycosylated NA TetramerComplexREACT_10176 (Reactome)
Glycosylated NA TetramerComplexREACT_10567 (Reactome)
Glycosylated NA TetramerComplexREACT_10972 (Reactome)
Glycosylated NAProteinP03468 (Uniprot-TrEMBL)
Glycosylated and folded HA ProteinP03452 (Uniprot-TrEMBL)
Glycosylated and folded HA trimerComplexREACT_10412 (Reactome)
Glycosylated and folded HA trimerComplexREACT_10554 (Reactome)
Glycosylated and folded HA trimerComplexREACT_10717 (Reactome)
Glycosylated and folded HAProteinP03452 (Uniprot-TrEMBL)
Glycosylated, palmitylated and folded HA trimer Lipid Raft ComplexComplexREACT_10369 (Reactome)
Glycosylated, palmitylated and folded HA trimer Lipid Raft ComplexComplexREACT_10581 (Reactome)
Glycosylated, palmitylated and folded HA trimerComplexREACT_10197 (Reactome)
Glycosylated, palmitylated and folded HA trimerComplexREACT_10978 (Reactome)
Gycosylated NA Tetramer Lipid RaftComplexREACT_10662 (Reactome)
Gycosylated NA Tetramer Lipid RaftComplexREACT_10954 (Reactome)
Gycosylated NA TetramerComplexREACT_10841 (Reactome)
H+ MetaboliteCHEBI:15378 (ChEBI)
H+MetaboliteCHEBI:15378 (ChEBI)
HA folded and glycosylated ProteinP03452 (Uniprot-TrEMBL)
HA folded, glycosylated, and palmitylated ProteinP03452 (Uniprot-TrEMBL)
HA mRNA ProteinV01088 (EMBL)
HA1 ProteinP03452 (Uniprot-TrEMBL)
HA2 ProteinP03452 (Uniprot-TrEMBL)
HAProteinP03452 (Uniprot-TrEMBL)
HNRNPA0 ProteinQ13151 (Uniprot-TrEMBL)
HNRNPA1 ProteinP09651 (Uniprot-TrEMBL)
HNRNPA2B1 ProteinP22626 (Uniprot-TrEMBL)
HNRNPA3 ProteinP51991 (Uniprot-TrEMBL)
HNRNPC ProteinP07910 (Uniprot-TrEMBL)
HNRNPD ProteinQ14103 (Uniprot-TrEMBL)
HNRNPFProteinP52597 (Uniprot-TrEMBL)
HNRNPH1ProteinP31943 (Uniprot-TrEMBL)
HNRNPH2 ProteinP55795 (Uniprot-TrEMBL)
HNRNPK ProteinP61978 (Uniprot-TrEMBL)
HNRNPL ProteinP14866 (Uniprot-TrEMBL)
HNRNPM ProteinP52272 (Uniprot-TrEMBL)
HNRNPR ProteinO43390 (Uniprot-TrEMBL)
HNRNPU ProteinQ00839 (Uniprot-TrEMBL)
HNRNPUL1 ProteinQ9BUJ2 (Uniprot-TrEMBL)
HSP90AA1ProteinP07900 (Uniprot-TrEMBL)
HSPA1AProteinP08107 (Uniprot-TrEMBL)
Host Derived Lipid Bilayer Membrane Rich In Sphingolipids And CholesterolREACT_9200 (Reactome)
IPO5ProteinO00410 (Uniprot-TrEMBL)
Influenza A Viral Envelope Inserted Into The Endocytic Vesicle MembraneComplexREACT_9160 (Reactome)
Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open PoreComplexREACT_9315 (Reactome)
Influenza A Viral Particle Docked At The Endocytic Vesicle MembraneComplexREACT_9257 (Reactome)
Influenza A Viral Particle With A Fusion Competent HA2ComplexREACT_9163 (Reactome)
Influenza A Viral ParticleComplexREACT_10742 (Reactome)
Influenza A Viral ParticleComplexREACT_9077 (Reactome)
Influenza cRNA REACT_9879 (Reactome)
Initiated cRNA-vRNA ComplexComplexREACT_9672 (Reactome) cRNA bound by NP and trimeric polymerase, capable of vRNA synthesis from the cRNA template.
Initiated vRNA Transcription ComplexComplexREACT_9684 (Reactome) Viral RNA bound by polymerase PB1-PB2-PA subunits, primed by a 5' end cap cleaved from a host mRNA, and the second ribonucleotide (a G) complementary to a the vRNA second position (a C, Beaton, 1981; Krug, 1981; Li, 2001).
Initiated vRNA-cRNA ComplexComplexREACT_9685 (Reactome) vRNA bound by NP and trimeric polymerase, capable of complementary RNA synthesis.
Inter-Membrane Spanning HA2 ProteinP03452 (Uniprot-TrEMBL)
Intracellular assembly complexComplexREACT_10426 (Reactome)
KPNA1 ProteinP52294 (Uniprot-TrEMBL)
KPNA1ProteinP52294 (Uniprot-TrEMBL)
KPNB1 ProteinQ14974 (Uniprot-TrEMBL)
KPNB1ProteinQ14974 (Uniprot-TrEMBL)
Lipid RaftREACT_10385 (Reactome)
M1 ProteinP03485 (Uniprot-TrEMBL)
M1 mRNA ProteinAF389121 (EMBL)
M1 mRNARnaAF389121 (EMBL)
M1ProteinP03485 (Uniprot-TrEMBL)
M2 ProteinP06821 (Uniprot-TrEMBL)
M2 TetramerComplexREACT_10281 (Reactome)
M2 TetramerComplexREACT_10501 (Reactome)
M2 TetramerComplexREACT_10683 (Reactome)
M2 mRNA ProteinAF389121 (EMBL)
M2 mRNARnaAF389121 (EMBL)
M2ProteinP06821 (Uniprot-TrEMBL)
Mature intronless transcript derived mRNA with m7G cap removedREACT_9723 (Reactome) A mature mRNA that has been 3' cleaved, subsequently polyadenylated, and a m7G 5' cap. The m7G has been removed or snatched. This product was derived from an intronless transcript.
Mature intronless transcript derived mRNAREACT_4033 (Reactome) A mature mRNA that has been 3' cleaved, subsequently polyadenylated, and a m7G 5' cap. This product was derived from an intronless transcript.
NA ProteinP03468 (Uniprot-TrEMBL)
NA mRNA ProteinJ02146 (EMBL)
NAProteinP03468 (Uniprot-TrEMBL)
NCBP1 ProteinQ09161 (Uniprot-TrEMBL)
NCBP2 ProteinP52298 (Uniprot-TrEMBL)
NEP/NS2 ProteinP03508 (Uniprot-TrEMBL)
NEP/NS2ProteinP03508 (Uniprot-TrEMBL)
NFX.1 ProteinO43831 (Uniprot-TrEMBL)
NP Lipid RaftComplexREACT_10315 (Reactome)
NP Lipid RaftComplexREACT_10830 (Reactome)
NP ProteinP03466 (Uniprot-TrEMBL)
NP mRNA ProteinJ02147 (EMBL)
NPProteinP03466 (Uniprot-TrEMBL)
NS1 ProteinP03496 (Uniprot-TrEMBL)
NS1 mRNA ProteinJ02150 (EMBL)
NS1 mRNARnaJ02150 (EMBL)
NS1ProteinP03496 (Uniprot-TrEMBL)
NS2 mRNA ProteinJ02150 (EMBL)
NS2 mRNARnaJ02150 (EMBL)
NTPMetaboliteREACT_4491 (Reactome)
NUP107 ProteinP57740 (Uniprot-TrEMBL)
NUP133 ProteinQ8WUM0 (Uniprot-TrEMBL)
NUP153 ProteinP49790 (Uniprot-TrEMBL)
NUP155 ProteinO75694 (Uniprot-TrEMBL)
NUP160 ProteinQ12769 (Uniprot-TrEMBL)
NUP188ProteinQ5SRE5 (Uniprot-TrEMBL)
NUP205ProteinQ92621 (Uniprot-TrEMBL)
NUP210 ProteinQ8TEM1 (Uniprot-TrEMBL)
NUP214 ProteinP35658 (Uniprot-TrEMBL)
NUP35 ProteinQ8NFH5 (Uniprot-TrEMBL)
NUP37 ProteinQ8NFH4 (Uniprot-TrEMBL)
NUP43 ProteinQ8NFH3 (Uniprot-TrEMBL)
NUP50 ProteinQ9UKX7 (Uniprot-TrEMBL)
NUP54 ProteinQ7Z3B4 (Uniprot-TrEMBL)
NUP62 ProteinP37198 (Uniprot-TrEMBL)
NUP85 ProteinQ9BW27 (Uniprot-TrEMBL)
NUP88 ProteinQ99567 (Uniprot-TrEMBL)
NUP93 ProteinQ8N1F7 (Uniprot-TrEMBL)
NUP98-5 ProteinP52948-5 (Uniprot-TrEMBL)
NUPL1-2 ProteinQ9BVL2-1 (Uniprot-TrEMBL)
NUPL2 ProteinO15504 (Uniprot-TrEMBL)
Nuclear Pore Complex ComplexREACT_5542 (Reactome)
Nup45 ProteinQ9BVL2-2 (Uniprot-TrEMBL)
P1 mRNA ProteinJ02151 (EMBL)
PA ProteinP03433 (Uniprot-TrEMBL)
PA mRNA ProteinV01106 (EMBL)
PAProteinP03433 (Uniprot-TrEMBL)
PB1 ProteinP03431 (Uniprot-TrEMBL)
PB1 mRNARnaJ02151 (EMBL)
PB1-F2ProteinP0C0U1 (Uniprot-TrEMBL)
PB1ProteinP03431 (Uniprot-TrEMBL)
PB2 ProteinP03428 (Uniprot-TrEMBL)
PB2ProteinP03428 (Uniprot-TrEMBL)
PCBP1 ProteinQ15365 (Uniprot-TrEMBL)
PCBP2 ProteinQ15366 (Uniprot-TrEMBL)
POLR2A ProteinP24928 (Uniprot-TrEMBL)
POLR2B ProteinP30876 (Uniprot-TrEMBL)
POLR2C ProteinP19387 (Uniprot-TrEMBL)
POLR2DProteinO15514 (Uniprot-TrEMBL)
POLR2E ProteinP19388 (Uniprot-TrEMBL)
POLR2FProteinP61218 (Uniprot-TrEMBL)
POLR2G ProteinP62487 (Uniprot-TrEMBL)
POLR2H ProteinP52434 (Uniprot-TrEMBL)
POLR2I ProteinP36954 (Uniprot-TrEMBL)
POLR2J ProteinP52435 (Uniprot-TrEMBL)
POLR2K ProteinP53803 (Uniprot-TrEMBL)
POLR2L ProteinP62875 (Uniprot-TrEMBL)
POM121 ProteinQ96HA1 (Uniprot-TrEMBL)
PTBP1 ProteinP26599 (Uniprot-TrEMBL)
PiMetaboliteCHEBI:18367 (ChEBI)
RAE1 ProteinP78406 (Uniprot-TrEMBL)
RAN ProteinP62826 (Uniprot-TrEMBL)
RANBP2 ProteinP49792 (Uniprot-TrEMBL)
RBM5 ProteinP52756 (Uniprot-TrEMBL)
RBMXProteinP38159 (Uniprot-TrEMBL)
RNA Polymerase II ComplexREACT_3935 (Reactome)
RNP

Karyopherin alpha

Karyopherin beta complex		ComplexREACT_9158 (Reactome)
RNP

Karyopherin alpha

Karyopherin beta complex		ComplexREACT_9341 (Reactome)
RNP Complex Karyopherin alphaComplexREACT_9328 (Reactome)
RNP pre-assembly complexComplexREACT_11005 (Reactome)
RNPS1 ProteinQ15287 (Uniprot-TrEMBL)
RPL10 ProteinP27635 (Uniprot-TrEMBL)
RPL10A ProteinP62906 (Uniprot-TrEMBL)
RPL11 ProteinP62913 (Uniprot-TrEMBL)
RPL12 ProteinP30050 (Uniprot-TrEMBL)
RPL13A ProteinP40429 (Uniprot-TrEMBL)
RPL13ProteinP26373 (Uniprot-TrEMBL)
RPL14 ProteinP50914 (Uniprot-TrEMBL)
RPL15ProteinP61313 (Uniprot-TrEMBL)
RPL17 ProteinP18621 (Uniprot-TrEMBL)
RPL18 ProteinQ07020 (Uniprot-TrEMBL)
RPL18A ProteinQ02543 (Uniprot-TrEMBL)
RPL19 ProteinP84098 (Uniprot-TrEMBL)
RPL21 ProteinP46778 (Uniprot-TrEMBL)
RPL22 ProteinP35268 (Uniprot-TrEMBL)
RPL23 ProteinP62829 (Uniprot-TrEMBL)
RPL23A ProteinP62750 (Uniprot-TrEMBL)
RPL24 ProteinP83731 (Uniprot-TrEMBL)
RPL26 ProteinP61254 (Uniprot-TrEMBL)
RPL26L1ProteinQ9UNX3 (Uniprot-TrEMBL)
RPL27A ProteinP46776 (Uniprot-TrEMBL)
RPL27ProteinP61353 (Uniprot-TrEMBL)
RPL28 ProteinP46779 (Uniprot-TrEMBL)
RPL29 ProteinP47914 (Uniprot-TrEMBL)
RPL3 ProteinP39023 (Uniprot-TrEMBL)
RPL30ProteinP62888 (Uniprot-TrEMBL)
RPL31 ProteinP62899 (Uniprot-TrEMBL)
RPL32 ProteinP62910 (Uniprot-TrEMBL)
RPL34 ProteinP49207 (Uniprot-TrEMBL)
RPL35 ProteinP42766 (Uniprot-TrEMBL)
RPL35A ProteinP18077 (Uniprot-TrEMBL)
RPL36 ProteinQ9Y3U8 (Uniprot-TrEMBL)
RPL36A ProteinP83881 (Uniprot-TrEMBL)
RPL37 ProteinP61927 (Uniprot-TrEMBL)
RPL37A ProteinP61513 (Uniprot-TrEMBL)
RPL38 ProteinP63173 (Uniprot-TrEMBL)
RPL39 ProteinP62891 (Uniprot-TrEMBL)
RPL3LProteinQ92901 (Uniprot-TrEMBL)
RPL4 ProteinP36578 (Uniprot-TrEMBL)
RPL41 ProteinP62945 (Uniprot-TrEMBL)
RPL5 ProteinP46777 (Uniprot-TrEMBL)
RPL6 ProteinQ02878 (Uniprot-TrEMBL)
RPL7 ProteinP18124 (Uniprot-TrEMBL)
RPL7A ProteinP62424 (Uniprot-TrEMBL)
RPL8 ProteinP62917 (Uniprot-TrEMBL)
RPL9 ProteinP32969 (Uniprot-TrEMBL)
RPLP0 ProteinP05388 (Uniprot-TrEMBL)
RPLP1ProteinP05386 (Uniprot-TrEMBL)
RPLP2 ProteinP05387 (Uniprot-TrEMBL)
RPS10 ProteinP46783 (Uniprot-TrEMBL)
RPS11 ProteinP62280 (Uniprot-TrEMBL)
RPS12 ProteinP25398 (Uniprot-TrEMBL)
RPS13ProteinP62277 (Uniprot-TrEMBL)
RPS14 ProteinP62263 (Uniprot-TrEMBL)
RPS15 ProteinP62841 (Uniprot-TrEMBL)
RPS15A ProteinP62244 (Uniprot-TrEMBL)
RPS16 ProteinP62249 (Uniprot-TrEMBL)
RPS17 ProteinP08708 (Uniprot-TrEMBL)
RPS18 ProteinP62269 (Uniprot-TrEMBL)
RPS19 ProteinP39019 (Uniprot-TrEMBL)
RPS20 ProteinP60866 (Uniprot-TrEMBL)
RPS21 ProteinP63220 (Uniprot-TrEMBL)
RPS23 ProteinP62266 (Uniprot-TrEMBL)
RPS24 ProteinP62847 (Uniprot-TrEMBL)
RPS25 ProteinP62851 (Uniprot-TrEMBL)
RPS26 ProteinP62854 (Uniprot-TrEMBL)
RPS27 ProteinP42677 (Uniprot-TrEMBL)
RPS27AProteinP62979 (Uniprot-TrEMBL)
RPS28 ProteinP62857 (Uniprot-TrEMBL)
RPS29 ProteinP62273 (Uniprot-TrEMBL)
RPS2ProteinP15880 (Uniprot-TrEMBL)
RPS3 ProteinP23396 (Uniprot-TrEMBL)
RPS3A ProteinP61247 (Uniprot-TrEMBL)
RPS4X ProteinP62701 (Uniprot-TrEMBL)
RPS4Y1ProteinP22090 (Uniprot-TrEMBL)
RPS5ProteinP46782 (Uniprot-TrEMBL)
RPS6 ProteinP62753 (Uniprot-TrEMBL)
RPS7 ProteinP62081 (Uniprot-TrEMBL)
RPS8ProteinP62241 (Uniprot-TrEMBL)
RPS9 ProteinP46781 (Uniprot-TrEMBL)
RPSA ProteinP08865 (Uniprot-TrEMBL)
Ran GTPase GTPComplexREACT_6698 (Reactome)
Ribonucleoprotein ComplexREACT_9223 (Reactome)
Ribonucleoprotein ComplexREACT_9227 (Reactome)
SA MetaboliteCHEBI:21622 (ChEBI)
SAMetaboliteCHEBI:21622 (ChEBI)
SEH1L-2 ProteinQ96EE3-2 (Uniprot-TrEMBL)
SMC1A ProteinQ14683 (Uniprot-TrEMBL)
SNRNP70 ProteinP08621 (Uniprot-TrEMBL)
SNRPA ProteinP09012 (Uniprot-TrEMBL)
SNRPD2 ProteinP62316 (Uniprot-TrEMBL)
SNRPE ProteinP62304 (Uniprot-TrEMBL)
SNRPF ProteinP62306 (Uniprot-TrEMBL)
SNRPG ProteinP62308 (Uniprot-TrEMBL)
SRRM1 ProteinQ8IYB3 (Uniprot-TrEMBL)
SRSF1 ProteinQ07955 (Uniprot-TrEMBL)
SRSF2 ProteinQ01130 (Uniprot-TrEMBL)
SRSF3 ProteinP84103 (Uniprot-TrEMBL)
SRSF5 ProteinQ13243 (Uniprot-TrEMBL)
SRSF6 ProteinQ13247 (Uniprot-TrEMBL)
SRSF7 ProteinQ16629 (Uniprot-TrEMBL)
SRSF9 ProteinQ13242 (Uniprot-TrEMBL)
SUGP1 ProteinQ8IWZ8 (Uniprot-TrEMBL)
Segment 1 RNPComplexREACT_10624 (Reactome)
Segment 2 RNPComplexREACT_10270 (Reactome)
Segment 3 RNPComplexREACT_10968 (Reactome)
Segment 4 RNPComplexREACT_10933 (Reactome)
Segment 5 RNPComplexREACT_10746 (Reactome)
Segment 6 RNPComplexREACT_10870 (Reactome)
Segment 7 RNPComplexREACT_10503 (Reactome)
Segment 8 RNPComplexREACT_10273 (Reactome)
Sialic Acid Bound Influenza A Viral ParticleComplexREACT_10492 (Reactome)
Sialic Acid Bound Influenza A Viral ParticleComplexREACT_9232 (Reactome)
Spliceosomal E ComplexComplexREACT_4545 (Reactome)
TPR ProteinP12270 (Uniprot-TrEMBL)
U1 snRNA ProteinV00590 (EMBL)
U2AF1 ProteinQ01081 (Uniprot-TrEMBL)
U2AF2 ProteinP26368 (Uniprot-TrEMBL)
UBA52ProteinP62987 (Uniprot-TrEMBL)
Viral PolymeraseComplexREACT_9586 (Reactome) Heterotrimeric influenza viral polymerase complex consisting of PB1, PB2, and PA; although capable of being imported into the nucleus independently, the three subunits of the influenza polymerase assemble in the nucleus to form a mature ternary polymerase complex that binds viral vRNA or cRNA (reviewed in Buolo et al., 2006).
Viral ProteinsComplexREACT_9572 (Reactome)
XPO1 ProteinO14980 (Uniprot-TrEMBL)
XPO1ProteinO14980 (Uniprot-TrEMBL)
YBX1 ProteinP67809 (Uniprot-TrEMBL)
cRNPComplexREACT_9556 (Reactome) Extended cRNA complexed with viral NP and trimeric polymerase.
p-S5-POLR2A ProteinP24928 (Uniprot-TrEMBL)
palmitylated M2 ProteinP06821 (Uniprot-TrEMBL)
palmitylated M2 TetramerComplexREACT_10389 (Reactome)
palmitylated M2 TetramerComplexREACT_10582 (Reactome)
vRNA ProteinREACT_9646 (Reactome)
vRNA ComplexREACT_9729 (Reactome)
vRNA Transcription ComplexComplexREACT_9896 (Reactome) The 5' and 3' ends of the vRNA bound to the PB1 subunit of the viral RNA polymerase; PB2 bound to the methylated cap on a host pre-mRNA amino acids (Cianci, 1995; Brownlee, 2002; Honda, 1999).
vRNP

M1 NEP

NP		ComplexREACT_9710 (Reactome)
vRNP

M1

NEP		ComplexREACT_9569 (Reactome)
vRNP M1 for ExportComplexREACT_9769 (Reactome)
vRNP Export ComplexComplexREACT_9906 (Reactome)
vRNP destined for ExportComplexREACT_9574 (Reactome)
vRNPComplexREACT_9584 (Reactome) A three dimensional crystal structure of NP suggests that this molecule forms a trimer that binds viral RNA (Ye et al., 2006). Mutiple NP trimers complex vRNA or cRNA.
viral mRNARnaREACT_9782 (Reactome)
viral mRNAProteinREACT_9819 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
80S ribosomemim-catalysisREACT_9514 (Reactome)
80S ribosomemim-catalysisREACT_9524 (Reactome)
Aminoacyl-tRNAREACT_9514 (Reactome)
Aminoacyl-tRNAREACT_9524 (Reactome)
CALRArrowREACT_6177 (Reactome)
CANXArrowREACT_6177 (Reactome)
ClathrinArrowREACT_6262 (Reactome)
Cleaved HA Influenza A Viral ParticleREACT_6232 (Reactome)
Crm1

Ran GTPase

GDP		ArrowREACT_6136 (Reactome)
DNAJC3ArrowREACT_9514 (Reactome)
GRSF1ArrowREACT_9514 (Reactome)
Glycosylated NA TetramerArrowREACT_6225 (Reactome)
Glycosylated NA TetramerArrowREACT_6273 (Reactome)
Glycosylated NA TetramerREACT_6225 (Reactome)
Glycosylated NA TetramerREACT_6273 (Reactome)
Glycosylated NA TetramerREACT_9947 (Reactome)
Glycosylated and folded HA trimerArrowREACT_6225 (Reactome)
Glycosylated and folded HA trimerArrowREACT_6273 (Reactome)
Glycosylated and folded HA trimerREACT_6225 (Reactome)
Glycosylated and folded HA trimerREACT_6273 (Reactome)
Glycosylated, palmitylated and folded HA trimer Lipid Raft ComplexArrowREACT_10039 (Reactome)
Glycosylated, palmitylated and folded HA trimer Lipid Raft ComplexREACT_10039 (Reactome)
Glycosylated, palmitylated and folded HA trimerREACT_10077 (Reactome)
Glycosylated, palmitylated and folded HA trimerREACT_6146 (Reactome)
Gycosylated NA Tetramer Lipid RaftArrowREACT_10039 (Reactome)
Gycosylated NA Tetramer Lipid RaftREACT_10039 (Reactome)
Gycosylated NA TetramerREACT_10077 (Reactome)
H+ArrowREACT_6230 (Reactome)
H+REACT_6315 (Reactome)
HSP90AA1ArrowREACT_9428 (Reactome)
HSPA1ATBarREACT_9407 (Reactome)
Host Derived Lipid Bilayer Membrane Rich In Sphingolipids And CholesterolREACT_6193 (Reactome)
IPO5ArrowREACT_9428 (Reactome)
Influenza A Viral Envelope Inserted Into The Endocytic Vesicle MembraneArrowREACT_6230 (Reactome)
Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open PoreREACT_6315 (Reactome)
Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Poremim-catalysisREACT_6315 (Reactome)
Influenza A Viral ParticleArrowREACT_6262 (Reactome)
Influenza cRNA ArrowREACT_9438 (Reactome)
Initiated cRNA-vRNA ComplexREACT_9438 (Reactome)
Initiated vRNA Transcription ComplexArrowREACT_6239 (Reactome)
Initiated vRNA Transcription ComplexREACT_6210 (Reactome)
Initiated vRNA-cRNA ComplexREACT_9404 (Reactome)
Intracellular assembly complexREACT_6193 (Reactome)
KPNA1ArrowREACT_6164 (Reactome)
KPNA1REACT_6138 (Reactome)
KPNB1ArrowREACT_6164 (Reactome)
KPNB1REACT_6322 (Reactome)
Lipid RaftREACT_6146 (Reactome)
Lipid RaftREACT_6271 (Reactome)
Lipid RaftREACT_9947 (Reactome)
M1 mRNAREACT_9402 (Reactome)
M1ArrowREACT_6230 (Reactome)
M1REACT_10077 (Reactome)
M1REACT_9407 (Reactome)
M2 TetramerArrowREACT_6225 (Reactome)
M2 TetramerArrowREACT_6273 (Reactome)
M2 TetramerREACT_6225 (Reactome)
M2 TetramerREACT_6273 (Reactome)
M2 mRNAArrowREACT_9402 (Reactome)
M2 mRNAArrowREACT_9528 (Reactome)
M2 mRNAREACT_9528 (Reactome)
Mature intronless transcript derived mRNA with m7G cap removedArrowREACT_6239 (Reactome)
Mature intronless transcript derived mRNAREACT_6142 (Reactome)
NAmim-catalysisREACT_6348 (Reactome)
NEP/NS2ArrowREACT_6230 (Reactome)
NEP/NS2REACT_10077 (Reactome)
NEP/NS2REACT_6303 (Reactome)
NP Lipid RaftArrowREACT_10039 (Reactome)
NP Lipid RaftREACT_10039 (Reactome)
NPArrowREACT_6142 (Reactome)
NPArrowREACT_9485 (Reactome)
NPArrowREACT_9513 (Reactome)
NPREACT_10077 (Reactome)
NPREACT_6271 (Reactome)
NPREACT_9404 (Reactome)
NPREACT_9438 (Reactome)
NPREACT_9490 (Reactome)
NS1 mRNAREACT_9402 (Reactome)
NS1ArrowREACT_9514 (Reactome)
NS2 mRNAArrowREACT_9402 (Reactome)
NS2 mRNAArrowREACT_9528 (Reactome)
NS2 mRNAREACT_9528 (Reactome)
NTPREACT_6210 (Reactome)
NTPREACT_9404 (Reactome)
NTPREACT_9438 (Reactome)
NTPREACT_9513 (Reactome)
Nuclear Pore Complex ArrowREACT_6136 (Reactome)
Nuclear Pore Complex ArrowREACT_6289 (Reactome)
PAREACT_10077 (Reactome)
PAREACT_9428 (Reactome)
PAREACT_9485 (Reactome)
PB1 mRNAREACT_9524 (Reactome)
PB1REACT_10077 (Reactome)
PB1REACT_9428 (Reactome)
PB1REACT_9485 (Reactome)
PB2REACT_10077 (Reactome)
PB2REACT_9428 (Reactome)
PB2REACT_9485 (Reactome)
PiArrowREACT_6136 (Reactome)
REACT_10039 (Reactome) Once processed, the viral proteins are transported from the golgi apparatus to the plasma membrane.
REACT_10062 (Reactome) The integral membrane protein NA is synthesized on membrane-bound ribosomes and subsequently transported across the ER where it is folded and glycosylated. Subsequently NA is assembled into a tetramer.
REACT_10077 (Reactome) As influenza viruses bud from the plasma membrane of infected cells, complete virions are not seen inside cells. In polarized epithelial cells, assembly and budding of influenza occurs from the apical plasma membrane (Schmitt, 2004). For efficient assembly, all virion components must accumulate at the budding site, and it is believed that the viral glycoprotein accumulation determines the site of virus assembly and budding (Nayak, 2004). M1 is thought to be the bridge between the envelope glycoproteins and the RNPs for assembly (Schmitt, 2004). M2 is also required, because if it is not present RNPs are not packaged into budding virions (McCown, 2005), however it role is not known.
REACT_10095 (Reactome) The integral membrane protein M2 is synthesized on membrane-bound ribosomes and subsequently transported across the ER, where it is folded and assembled into a tetramer.
REACT_10123 (Reactome) The M2 from influenza A virus is a 97-residue protein with a single transmembrane helix that associates to form a tetramer in the endoplasmic reticulum (Salom et al, 2000). A 15-20-residue segment C-terminal to the membrane-spanning region has been postulated to aid in the stabilization of the tetrameric assembly (Kochendoerfer et al 1999).
REACT_10133 (Reactome) Palmitoylation of influenza A M2 occurs in the ER, or cis golgi network, following tetramerisation. The palmitoylation reaction proceeds via a labile thioester type bond at a specific residue of M2 (Sugrue et al., 1990).
REACT_6136 (Reactome) Viral RNP, bound by M1 and NEP/NS2 interacting with CRM1, are shuttled through the nuclear pore into the cytoplasm (Martin, 1991; O'Neill, 1998; Buolo, 2006). This mechanism may resemble export of HIV-1 ribonucleoprotein, where the HIV-1 Rev export protein interacts with CRM1 (Askjaer, 1998). A number of cofactors are implicated in CRM1-mediated export, including the small GTPase Ran, Ran-binding proteins 1 and 3, and a guanine nucleotide exchange factor (Nilsson, 2001; Nemergut, 2002; Petosa, 2004). Ternary CRM1-cofactor-cargo complexes likely interact transiently with nuclear pore proteins (nucleoporins) as they traverse the pore (reviewed in Suntharalingam, 2003). RanGTP is hydrolyzed to RanGDP in the cytoplasm, an activity that can be stimulated by NEP/NS2 (Akarsu, 2003). Influenza infection activates Raf/MEK/ERK signaling, which is necessary for NEP/NS2-mediated export of viral RNP (Pleschka, 2001; Marjuki, 2006). Influenza vRNP complexes released into the cytoplasm do not re-enter the nucleus, as they are thought to remain bound by M1, preventing re-import (Martin, 1991). It has been suggested that M1 binding of zinc cations could distinguish M1 bound to the vRNP from polymerized, matrix M1 present in nascent virions (Elster, 1994).
REACT_6137 (Reactome) There is evidence for the association of M1 with lipid rafts in influenza infected cells, whereas M1 expressed alone remains soluble (Ali et al., 2000; Zhang and Lamb, 1996), suggesting association of M1 with other viral proteins in targetting to the cell membrane. Coexpression of HA and NA together with M1 has been shown to promote raft association of M1. This association requires the TMD and cytoplasmic tails of HA and NA (Ali et al, 2000; Zhang et al, 2000). This is consistent with M1 becoming associated with HA and NA during their passage through the exocytic pathway to raft domains in the apical membrane. alternatively M1 may use the cytoskeleton to reach the virus assembly site, as M1 interacts with cytoskeletal components (Alvalos et al., 1997). The M1 interaction depends on the presence of RNP and is most likely mediated by direct binding of F-actin by NP (Digard et al., 1999).
REACT_6138 (Reactome) The eight influenza virus genome segments never exist as naked RNA but are associated with four viral proteins to form viral ribonucleoprotein complexes (vRNPs). The major viral protein in the RNP complex is the nucleocapsid protein (NP), which coats the RNA. The remaining proteins PB1, PB2 and PA bind to the partially complementary ends of the viral RNA, creating the distinctive panhandle structure. The influenza viral NP behaves like a nuclear localization sequence (NLS) containing protein. The RNP docks at the nuclear envelope only in the presence of the heterodimeric karyopherin alpha and beta complex. Here karyopherin alpha recognizes the RNP.
REACT_6141 (Reactome) Trimerisation of the fully folded and fully oxidised HA monomer is thought to occur in the endoplasmic reticulum and ERGIC compartment, following dissociation of HA from calnexin. Trimerisation is generally thought to be the final step in HA maturation occurring in the endoplasmic reticulum before transport to the Golgi apparatus, although Yewdell et al (1988) provide data suggesing that trimerisation may occur within the Golgi.
REACT_6142 (Reactome) The 5' end of the vRNA associates with a binding site on the PB1 subunit of the viral RNA polymerase, distinct from the 3' vRNA binding site, which is subsequenty bound forming a loop. These binding events set off allosteric conformational changes in the trimeric polymerase complex that induce PB2 binding of the methylated cap on a host pre-mRNA (Plotch, 1981; Cianci, 1995; Li, 1998; Brownlee, 2002; Kolpashchikov, 2004). PB2 amino acids 242-282 and 538-577 are involved in cap binding (Honda, 1999). Direct or indirect interaction with active, transcribing host RNA polymerase II is thought to supply host mRNA for the caps (Bouloy, 1978; Engelhardt, 2005).
REACT_6146 (Reactome) Influenza virus buds preferentially from lipid rafts (Scheiffele et al, 1999). NA protein individually accumulates at, and is selectively incorporated into rafts (Kundu et al., 1996). The signals for raft association lie within the transmembranse domain (TMD), (Barman et al., 2001, Barman et al., 2004), and raft association of NA has been shown to be essential for efficient virus replication. This is believed to be due to a requirement for a concentration of NA at specific areas of the plasma membrane to support a level of NA incorporation into budding particles sufficient to allow for efficient virus release (Barman et al., 2004).
REACT_6164 (Reactome) Once the viral RNP and heterodimeric karyopherin complex has been transported into the nucleus the RNP dissasociates from the heterodimeric karyopherins.
REACT_6176 (Reactome) The concerted structural change of several hemagglutinin molecules opens a pore through which the viral RNP will be able to pass into the host cell cytosol.
REACT_6177 (Reactome) The ectodomain of HA is translocated into the ER lumen, where it undergoes a series of folding events mediated by the formation of disulfide bonds and glycosylation reactions. The formation of a discrete intermediate species of highly folded monomeric protein preceeds trimerisation. The folding process is efficient and rapid, with greater than 90% of the protein trafficked to the golgi apparatus; and mature HA0 subunits appearing in a matter of a few minutes. Calnexin and calreticulin have been identified as cellular lectins which interact transiently with newly synthesized HA by attaching to partially trimmed N-linked oligosaccharides (Herbert et al., 1997), facilitating correct folding of the HA molecule.
REACT_6180 (Reactome) The fusion peptide of its HA2 subunit interacts with the endosome membrane. The transmembrane domain of the HA2 is inserted into the viral membrane and the fusion peptide is inserted into the endosomal membrane. In the acidic pH structure of HA the two ends of the HA complex are in juxtaposition.
REACT_6181 (Reactome) Glycosylation of NA occurs within the endoplasmic reticulum and is believed to be neccessary for proper tetramerization of the NA dimers. Sugar residues become attached to four of the five potential glycosylation sites in the head of N1 neuraminidase (Hausman et al., 1997).
REACT_6187 (Reactome) The hemagglutinin of influenza virus is palmitoylated with long-chain fatty acids.
Palmitoylation of HA is believed to occur in the cis golgi network (Veit 1993), shortly after trimerisation of the molecule, and before cleavage of the HA into HA1 and HA2. HA is palmitoylated through thioester linkages at three cysteine residues located in the cytoplasmic domain and at the carboxy-terminal end of the transmembrane region. Lack of acylation has no obvious influence on the biological activities of HA.
REACT_6193 (Reactome) The final step in the budding process is the fusion of the lipid membrane surrounding the virion core, producing an extracellular enveloped virus particle.
REACT_6194 (Reactome) Virus NEP/NS2 interacts with human CRM1 (hCRM1), possibly dependent on a nuclear export signal (NES) motif in the NEP/NS2 N-terminal region (O'Neill, 1998; Neumann, 2000). The CRM1/exportin-1 pathway is a cellular mechanism for nuclear export, with CRM1 interacting with the Ran small GTPase and a cargo molecule's leucine-rich NES (Fukuda, 1997; Petosa, 2004). Leptomycin B, which specifically inhibits hCRM1, blocks export of viral RNP (Elton, 2001; Ma, 2001; Watanabe, 2001). Thus, NEP/NS2 interaction with cellular nuclear export machinery is essential for nuclear export of vRNP complexes and influenza virus release. A role for NP protein interaction with export machinery has also been proposed (Elton, 2001).
REACT_6210 (Reactome) Catalyzed by the RNA polymerase activity of the viral PB1 subunit, an mRNA complementary to the bound vRNA is synthesized (Plotch, 1977). PA and PB2 move down the growing mRNA in complex with PB1, with PB2 possibly dissociating from the cap (Braam, 1983). However, the 5’ end of the vRNA may remain bound during elongation as the template is threaded through in a 3’ to 5’ direction until a polyadenylation signal is encountered (Poon, 1998; Zheng, 1999).
REACT_6219 (Reactome) The low pH of the endosome causes the viral HA (hemagglutinin) to undergo a structural change which frees the fusion peptide of its HA2 subunit.
REACT_6225 (Reactome) Viral proteins are packaged into a golgi apparatus bound transport vesicle.
REACT_6230 (Reactome) The influx of H+ ions into the virion disrupts protein-protein interactions, resulting in the release of the viral RNP from the viral matrix (M1) protein. The uncoating process is complete with the appearance of free RNP complexes in the cytosol.
REACT_6231 (Reactome) Tetramerisation of the NA occurs in the ER following an initial dimerisation step. Tetramerisation is believed to be dependant on glycosylation of the NA molecules
REACT_6232 (Reactome) Influenza viruses bind via their surface HA (hemagglutinin) to sialic acid in alpha 2,3 or alpha 2,6 linkage with galactose on the host cell surface. Sialic acid in 2,6 linkages is characteristic of human cells while 2,3 linkages are characteristic of avian cells. The specificity of influenza HA for sialic acid in alpha 2,6 or alpha 2,3 linkages is a feature restricting the transfer of influenza viruses between avian species and humans. This species barrier can be overcome, however. Notably, passaged viruses adapt to their host through mutation in the receptor binding site of the viral HA gene.
REACT_6239 (Reactome) The host cell mRNA bound to viral RNA polymerase PB2 subunit is cleaved by the viral RNA polymerase PB1 subunit's endonuclease activity, and the capped 5' end plus 10-13 nucleotides of the host mRNA remains bound to the polymerase complex (Plotch, 1981; Krug, 1981; Hagen, 1994; Cianci, 1995, Li, 1998; Li, 2001). Viral mRNA may be protected against cap-snatching by the polymerase complex itself, which tightly binds capped viral mRNA (Shih, 1996). A guanine residue, complementary to a cytosine in the vRNA, is added to the host-derived cap, catalyzed by the RNA polymerase activity of the PB1 viral RNA polymerase subunit (Beaton, 1981; Toyoda, 1986).
REACT_6262 (Reactome) Virus particles bound to the cell surface can be internalized by four mechanisms. Most internalization appears to be mediated by clathrin-coated pits.
REACT_6264 (Reactome) A poly-uridine sequence motif, consisting in most cases of 5-7 U residues, abuts the "panhandle" duplex structure in the vRNA; this sequence is approximately 16 nucleotides from the 5' end of this RNA duplex structure within the vRNA promoter. Encountering this signal, the viral RNA polymerase stutters, leading to the synthesis of a poly-A tail on the viral mRNA (Robertson, 1981; Luo, 1991; Li,1994; Poon, 1998; Zheng et al. 1999).
REACT_6271 (Reactome) There is evidence that NP alone is intrinsically targeted to the apical plasma membrane and associates with lipid rafts in a cholesterol-dependent manner, which suggests that RNPs could reach the assembly site independently of the other viral components.
REACT_6273 (Reactome) Once the tranport vesicle arrives at the golgi apparatus, it docks and dumps its contents into the golgi lumen.
REACT_6289 (Reactome) These RNPs (10-20nm wide) are too large to passively diffuse into the nucleus and therefore, once released from an incoming particle they must rely on the active import mechanism of the host cell nuclear pore complex (NPC). Once the RNP heterodimeric karyopherin complex docks at the NPC, it is transported into the nucleus.
REACT_6303 (Reactome) Structural characterization of NEP/NS2 suggests that acidic residues in the C-terminus of NEP/NS2 bind to M1, with Trp78 critical for interaction (Ward, 1995; Yasuda, 1993; Akarsu, 2003).
REACT_6309 (Reactome) The integral membrane protein HA is synthesized on membrane-bound ribosomes and subsequently transported across the endoplasmic reticulum, where it is folded, glycosylated, and assembled into a trimer.
REACT_6315 (Reactome) The uncoating of influenza viruses in endosomes is blocked by changes in pH caused by weak bases (e.g. ammonium chloride and chloroquine) or ionophores (e.g. monensin). Effective uncoating is also dependent on the presence of the viral M2 ion channel protein. Early on it was recognized that amantadine and rimantadine inhibit replication immediately following virus infection. Later it was found that the virus-associated M2 protein allows the influx of H+ ions from the endosome into the virion. This disrupts protein-protein interactions, resulting in the release of viral RNP free of the viral matrix (M1) protein. Amantadine and rimantadine have been shown to block the ion channel activity of the M2 protein and thus uncoating.
REACT_6322 (Reactome) The eight influenza virus genome segments are associated with four viral proteins to form viral ribonucleoprotein complexes (vRNPs). The major viral protein in the RNP complex is the nucleocapsid protein (NP), which coats the RNA. The remaining proteins PB1, PB2 and PA bind to the partially complementary ends of the viral RNA. The influenza viral NP behaves like a nuclear localization sequence (NLS) containing protein. The RNP docks at the nuclear envelope only in the presence of the heterodimeric karyopherin alpha and beta complex. Once the NLS is recognized by karyopherin alpha the karyopherin beta subunit joins the complex.
REACT_6336 (Reactome) The random incorporation model as its name suggests proposes that there is no selection at all on which vRNPs are packaged. It is assumed that each vRNP has equal probability of being packaged, and that if enough vRNPS are packaged a particular percentage of budding virions will receive at least one copy of each genome segment. This model is supported by evidence that infectious virions may possess more than eight vRNPs assuring the presence of a full complement of eight vRNPs in a significant percentage of virus particles. Mathematical analysis of packaging suggested that twelve RNA segments would need to be packaged in order to obtain approximately 10% of virus particles that are fully infectious (Enami, 1991), a number that is compatible with experimental data (Donald, 1954). Due to the low amount of RNA per virion (estimated at 1-2% w/w), enumeration of the precise number of RNAs packaged in a virion is difficult.
REACT_6348 (Reactome) The release of influenza virus particles after seperation of the virus and infected cell membrane is an active process. During the budding process, HA on the surface of the newly budding virion binds to cell surface molecules containing sialic acid residues as seen during attachment. The NA glycoproteins neuraminidase activity is essential to cleave the link between the HA and sialic acid on the surface of the host cell from which the budding virus is emeging from. Thus the NA mediated cleavage of sialic acid residues terminally linked to glycoproteins and glycolipids is the final step in releasing the virus particle from the host cell. This essential role of NA in release of virus particle has been demonstrated with the use of NA inhibitors (Palese, 1976; Luo, 1999; Garman, 2004), ts NA mutant viruses (Palese, 1974) and with viruses lacking NA activity (Liu, 1995). In all cases, viruses remain bound to the cell surface in clumps in the absence of NA enzymatic activity, resulting in loss of infectivity. Addition of exogenous sialidase results in virus release and recovery of infectivity. The sialidase activity of the NA is also important for removing sialic acid from the HA on virus particles, if this is not removed, virus particles aggregate.
REACT_9402 (Reactome) The viral polymerase complex produces positive-sense viral mRNA with host-cell derived 5' methyl caps. Alternately spliced mRNA transcribed from M and NS vRNA segments 7 and 8, producing the spliced mRNA for M2 and NEP/NS2, respectively, are thought to be coupled to the cellular splicing and export mechanisms (Lamb, 1980; Lamb, 1981; Chen, 2000; Li, 2001). As segments 7 and 8 each encode two proteins, splicing must be regulated allowing for alternative mRNAs, with the spliced products in the minority (approximately 10%). M1 splicing may be regulated by the viral polymerase and the cellular SR splicing protein SF2/ASF (Shih, 1995; Shih, 1996); while NS1 splicing appears to be regulated by the viral mRNA intrinsically (Alonso-Caplen, 1991; Valcarel, 1991).
REACT_9404 (Reactome) Virion vRNP is capable of synthesizing cRNA immediately following entry into the cell nucleus (Vreede, 2006). The PB1 subunit principally catalyzes extension (Nakagawa, 1996). However, cRNA does not accumulate until later in the infection process, possiby requiring NP and the trimeric polymerase for stabilization (Vreede, 2004). The vRNA template is released.
REACT_9407 (Reactome) M1 protein binds to viral RNP through its C-terminal domain (Baudin, 2001). The influenza M1 protein accumulates in the infected cell nucleus through a nuclear localization signal (NLS) RKLKR (residues 101-105) in its N-terminus (Ye, 1999). A host cell protein, HSP70, is thought to inhibit M1 binding at nonpermissive temperatures (Hirayama et al., 2004).
REACT_9428 (Reactome) The mature ternary influenza viral polymerase complex consists of PB1, PB2, and PA. The N-terminus of PB1 (residues 1-48) interacts with PB2, and amino acids 506-659 in PB1 interact with the PA subunit (Gonzalez, 1996; Perez, 2001). Although monomeric PB1, PB2 and PA, as well as PB1-PB2 and PB1-PA dimers are likely to exist in infected cells, it is believed that most of the polymerase proteins are assembled into the trimeric PB1-PB2-PA complex (Detjen, 1987). Newly synthesized subunits of the polymerase are imported into the nucleus through nuclear localization signals (NLS), which interact with cellular importin family proteins (Jones, 1986; Buolo, 2006). Importin beta-3 (Ran binding protein 5) facilitates nuclear import of PB1 and a PB1-PA dimer (Deng, 2006); coexpression of PA with PB1 was shown to enhance the import of PB1 (Fodor, 2004). A PB1-PB2 dimer has been found to interact with the molecular chaperone heat shock protein 90 (HSP90) to facilitate import (Naito, 2007). The three subunits assembled in the nucleus form a mature ternary polymerase complex that binds viral vRNA or cRNA (Jones, 1986; Buolo, 2006).
REACT_9438 (Reactome) vRNA is synthesized from the complementary cRNA strand by the trimeric polymerase complex, and bound by free NP protein (Honda, 1988; Mikulasova, 2000; Neumann, 2004). The PB1 subunit, with PA, catalyzes extension (Nakagawa, 1996). The cRNA is released.
REACT_9485 (Reactome) The nascent vRNP complexes, one for each gene segment, contain the negative-sense viral RNA and polymerase proteins (PB1, PB2, PA, and NP). In a model using negative-sense viral RNP reconstituted from transfected cells, there are multiple NP complexes and one polymerase complex arranged along a closed vRNA loop (Area et al., 2004). The three-dimensional structure of NP has revealed that three NP molecules form a stable trimer, interacting through beta-sheets b5, b6, and b7 in the C-terminal domain of the protein (Ye, 2006), with the viral RNA wrapping around the outside of the complex. Viral RNA from purified virions is present in an RNase-sensitive complex with NP and PB1, PB2, and PA, consistent with this structural model (Baudin et al, 1994; Ruigrok et al., 1995; Klumpp et al., 1997). It is not clear what controls the fate of vRNP, whether it is destined to become a template for transcription, for replication, or for export into the cytoplasm for packaging into virions at the plasma membrane, nor how distinct sub-nuclear localization and NP distribution at the nuclear matrix might mark, or polarize, a vRNP for export (Elton, 2005; Takizawa et al., 2006).
REACT_9487 (Reactome) Initiation of synthesis of the viral genomic RNA (vRNA) is thought to require hairpin (or panhandle/corkscrew) RNA loop structures formed by both the 5' and 3' ends of the cRNA (Pritlove, 1995; Crow, 2004; Park, 2003; Deng, 2006). The cRNA promoter has a similar structure to the vRNA promoter, but slight sequence differences are believed to result in a stronger cRNA promoter. As with the vRNA promoter, the polymerase is thought to first bind to the 5' end of the cRNA, then to the 3' end, and subsequently initiate RNA synthesis.
REACT_9490 (Reactome) Viral genomic RNA (vRNA) and complementary RNA (cRNA) are likely bound by the influenza nucleoprotein (NP) immediately upon synthesis. Although two nuclear localization signals have been mapped in the NP, an unconventional N-terminal NLS and a bipartite NLS within amino acids 198-216 (Wang, 1997; Neumann, 1997; Ozawa, 2007), the crystal structure of the NP suggests that only the unconventional NLS is exposed and can be used as a functional NLS (Ye, 2006). This unconvenetional NLS interacts with importins alpha-1 and -2 (Cros et al., 2005; Wang et al., 1997; Buolo et al., 2006). The three-dimensional structure of NP has revealed that NP molecules associate as a trimer, interacting through beta-sheets b5, b6, and b7 in the C-terminal domain of the protein; the viral RNA likely wraps around the outside of the complex (Ye, 2006).
REACT_9513 (Reactome) Viral vRNA, complexed with NP protein, is bound by the trimeric viral polymerase complex in a stable secondary structure-dependent manner, referred to as a panhandle, fork or cork-screw (Fodor, 1994; Brownlee, 2002; Park, 2003; Crow, 2004). This RNA structure is made of both the 5’ and 3' ends of the vRNA. The polymerase is thought to first bind the 5' end of the vRNA and then the 3' end. Synthesis of cRNA initiates without a host cell methylated RNA cap as a primer (Beaton, 1986; Galarza, 1996; Deng, 2006; Engehardt, 2006).
REACT_9514 (Reactome) Spliced and unspliced viral mRNA exported into the cytoplasm are translated by the host cell ribosomal translation machinery (reviewed in Kash, 2006). At least ten viral proteins are synthesized: HA, NA, PB1, PB2, PA, NP, NS1, NEP/NS2 (from spliced NS mRNA), M1, and M2 (from spliced M mRNA). The abundance of each of these proteins is thought to be controlled by differential mRNA abundances and stability (Tekamp, 1980; Hatada, 1989). As the localization of the nascent polypeptides is different between viral proteins with transmembrane domains (HA, NA and M2, which translocate to the ER and are transported through the Golgi to the plasma membrane) and soluble viral proteins (such as NP, the polymerase subunits, and NS1), mechanisms linking the translation of particular viral mRNA with subsequent protein localization rely on signal sequences recognized by the cell.
REACT_9524 (Reactome) For most influenza A strains (such as PR8), the PB1 mRNA segment produces a second protein, PB1-F2, from the +1 open reading frame (Chen, 2001). PB1-F2 is a pro-apoptotic, mitochondria-localized protein (Chen, 2001; Gibbs, 2003) that oligomerizes (Bruns, 2007) and sensitizes cells to death in concert with the mitochondrial ANT3 and VDAC proteins (Zamarin, 2005).
REACT_9528 (Reactome) In the cases of spliced, polyadenylated mRNA transcribed from M (segment 7) and NS (segment 8) vRNA templates (producing the spliced mRNA for M2 and NS2/NEP, respectively), export may be coupled to aspects of the cellular splicing and export mechanisms (Chen, 2000; Alonso-Caplan et al, 1992; Amorim, 2006). Simultaneously, the export of cellular mRNA appear to be inhibited by the viral NS1 protein, which binds to the cellular cleavage and polyadenylation specificity factor (CPSF), preventing polyadenylation and completion of pre-mRNA processing (Nemerof et al., 1998; Fortes, 1994; Lu, 1994; Li, 2001).
REACT_9529 (Reactome) The viral polymerase complex produces positive-sense viral mRNA with host-cell derived 5' methyl caps. Capped viral mRNAs are selectively exported from the host cell nucleus through a currently unclear mechanism that may rely on components of the host cell mRNA export machinery (Chen, 2000; Engelhardt, 2006). Polyadenylation of viral mRNA appears be required for influenza mRNA export (Poon, 2000). A coupling of viral mRNA export with cellular pre-mRNA processing complexes, recruited by phosphorylation of host RNA polymerase II C-terminal domain which interacts with the viral polymerase (Engelhardt, 2005), has been proposed as controlling the export of a subset (M1, HA, and NS1, but not NP) of viral mRNA from the nucleus (Amorim, 2007).
REACT_9947 (Reactome) Influenza virus buds preferentially from lipid rafts (Scheiffele et al, 1999). NA protein individually accumulates at, and is selectively incorporated into rafts (Kundu et al., 1996). The signals for raft association lie within the transmembranse domain (TMD), (Barman et al., 2001, Barman et al., 2004), and raft association of NA has been shown to be essential for efficient virus replication. This is believed to be due to a requirement for a concentration of NA at specific areas of the plasma membrane to support a level of NA incorporation into budding particles sufficient to allow for efficient virus release (Barman et al., 2004).
RNA Polymerase II ArrowREACT_6142 (Reactome)
RNP Complex Karyopherin alphaREACT_6322 (Reactome)
RNP pre-assembly complexREACT_10077 (Reactome)
Ran GTPase GTPREACT_6136 (Reactome)
Ribonucleoprotein ArrowREACT_6164 (Reactome)
Ribonucleoprotein ArrowREACT_6230 (Reactome)
Ribonucleoprotein REACT_6138 (Reactome)
SAArrowREACT_6262 (Reactome)
SAREACT_6193 (Reactome)
SAREACT_6232 (Reactome)
Segment 1 RNPREACT_6336 (Reactome)
Segment 2 RNPREACT_6336 (Reactome)
Segment 3 RNPREACT_6336 (Reactome)
Segment 4 RNPREACT_6336 (Reactome)
Segment 5 RNPREACT_6336 (Reactome)
Segment 6 RNPREACT_6336 (Reactome)
Segment 7 RNPREACT_6336 (Reactome)
Segment 8 RNPREACT_6336 (Reactome)
Viral PolymeraseArrowREACT_6264 (Reactome)
Viral PolymeraseArrowREACT_9404 (Reactome)
Viral PolymeraseArrowREACT_9438 (Reactome)
Viral PolymeraseREACT_6142 (Reactome)
Viral PolymeraseREACT_9487 (Reactome)
Viral PolymeraseREACT_9513 (Reactome)
Viral Polymerasemim-catalysisREACT_6210 (Reactome)
Viral Polymerasemim-catalysisREACT_6239 (Reactome)
Viral Polymerasemim-catalysisREACT_6264 (Reactome)
Viral Polymerasemim-catalysisREACT_9404 (Reactome)
Viral Polymerasemim-catalysisREACT_9438 (Reactome)
Viral Polymerasemim-catalysisREACT_9487 (Reactome)
Viral Polymerasemim-catalysisREACT_9513 (Reactome)
XPO1REACT_6194 (Reactome)
cRNPArrowREACT_9404 (Reactome)
cRNPArrowREACT_9438 (Reactome)
cRNPREACT_9487 (Reactome)
palmitylated M2 TetramerArrowREACT_10039 (Reactome)
palmitylated M2 TetramerREACT_10039 (Reactome)
palmitylated M2 TetramerREACT_10077 (Reactome)
vRNA ArrowREACT_6264 (Reactome)
vRNA ArrowREACT_9404 (Reactome)
vRNA ArrowREACT_9438 (Reactome)
vRNA REACT_6142 (Reactome)
vRNA REACT_9490 (Reactome)
vRNA REACT_9513 (Reactome)
vRNP

M1 NEP

NP		ArrowREACT_6136 (Reactome)
vRNP

M1

NEP		REACT_6194 (Reactome)
vRNP M1 for ExportREACT_6303 (Reactome)
vRNP Export ComplexREACT_6136 (Reactome)
vRNP destined for ExportREACT_9407 (Reactome)
vRNPREACT_9485 (Reactome)
viral mRNAArrowREACT_6264 (Reactome)
viral mRNAREACT_9514 (Reactome)

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