Influenza Infection (Homo sapiens)

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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</div>

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Bibliography

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Mukaigawa J, Nayak DP.; ''Two signals mediate nuclear localization of influenza virus (A/WSN/33) polymerase basic protein 2.''; PubMed Europe PMC Scholia
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Brownlee GG, Sharps JL.; ''The RNA polymerase of influenza a virus is stabilized by interaction with its viral RNA promoter.''; PubMed Europe PMC Scholia
Crow M, Deng T, Addley M, Brownlee GG.; ''Mutational analysis of the influenza virus cRNA promoter and identification of nucleotides critical for replication.''; PubMed Europe PMC Scholia
Vreede FT, Jung TE, Brownlee GG.; ''Model suggesting that replication of influenza virus is regulated by stabilization of replicative intermediates.''; PubMed Europe PMC Scholia
Krug RM.; ''Priming of influenza viral RNA transcription by capped heterologous RNAs.''; PubMed Europe PMC Scholia
Bergmann M, Garcia-Sastre A, Carnero E, Pehamberger H, Wolff K, Palese P, Muster T.; ''Influenza virus NS1 protein counteracts PKR-mediated inhibition of replication.''; PubMed Europe PMC Scholia
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Suntharalingam M, Wente SR.; ''Peering through the pore: nuclear pore complex structure, assembly, and function.''; PubMed Europe PMC Scholia
Li ML, Rao P, Krug RM.; ''The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits.''; PubMed Europe PMC Scholia
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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
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
Veit M, Klenk HD, Kendal A, Rott R.; ''The M2 protein of influenza A virus is acylated.''; PubMed Europe PMC Scholia
Enami M, Sharma G, Benham C, Palese P.; ''An influenza virus containing nine different RNA segments.''; PubMed Europe PMC Scholia
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
Neumann G, Brownlee GG, Fodor E, Kawaoka Y.; ''Orthomyxovirus replication, transcription, and polyadenylation.''; PubMed Europe PMC Scholia
Garman E, Laver G.; ''Controlling influenza by inhibiting the virus's neuraminidase.''; PubMed Europe PMC Scholia
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
Martin K, Helenius A.; ''Transport of incoming influenza virus nucleocapsids into the nucleus.''; PubMed Europe PMC Scholia
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
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
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
Vreede FT, Brownlee GG.; ''Influenza virion-derived viral ribonucleoproteins synthesize both mRNA and cRNA in vitro.''; PubMed Europe PMC Scholia
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
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
Zhang J, Lamb RA.; ''Characterization of the membrane association of the influenza virus matrix protein in living cells.''; PubMed Europe PMC Scholia
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
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
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
Mikulásová A, Varecková E, Fodor E.; ''Transcription and replication of the influenza a virus genome.''; PubMed Europe PMC Scholia
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
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
Palese P, Tobita K, Ueda M, Compans RW.; ''Characterization of temperature sensitive influenza virus mutants defective in neuraminidase.''; PubMed Europe PMC Scholia
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
Schmitt AP, Lamb RA.; ''Escaping from the cell: assembly and budding of negative-strand RNA viruses.''; PubMed Europe PMC Scholia
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
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
Boulo S, Akarsu H, Ruigrok RW, Baudin F.; ''Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes.''; PubMed Europe PMC Scholia
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
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
Tatu U, Hammond C, Helenius A.; ''Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment.''; PubMed Europe PMC Scholia
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
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
Fortes P, Beloso A, Ortín J.; ''Influenza virus NS1 protein inhibits pre-mRNA splicing and blocks mRNA nucleocytoplasmic transport.''; PubMed Europe PMC Scholia
Chen Z, Krug RM.; ''Selective nuclear export of viral mRNAs in influenza-virus-infected cells.''; PubMed Europe PMC Scholia
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
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
Fodor E, Pritlove DC, Brownlee GG.; ''The influenza virus panhandle is involved in the initiation of transcription.''; PubMed Europe PMC Scholia
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
Morris SJ, Price GE, Barnett JM, Hiscox SA, Smith H, Sweet C.; ''Role of neuraminidase in influenza virus-induced apoptosis.''; PubMed Europe PMC Scholia
Takeda M, Leser GP, Russell CJ, Lamb RA.; ''Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion.''; PubMed Europe PMC Scholia
Veit M, Schmidt MF.; ''Timing of palmitoylation of influenza virus hemagglutinin.''; PubMed Europe PMC Scholia
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
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

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Revision	Action	Time	User	Comment
115105	view	18:57, 25 January 2021	Egonw	Removed an empty reference.
114625	view	16:08, 25 January 2021	ReactomeTeam	Reactome version 75
113585	view	08:08, 3 November 2020	Egonw	Removed the empty reference (we now know this is a book that the convertor cannot handle).
113073	view	11:13, 2 November 2020	ReactomeTeam	Reactome version 74
112844	view	05:16, 12 October 2020	Egonw	Removed an empty (and unused) reference
112308	view	15:22, 9 October 2020	ReactomeTeam	Reactome version 73
101951	view	12:13, 20 November 2018	Egonw	Removed an empty reference.
101207	view	11:10, 1 November 2018	ReactomeTeam	reactome version 66
100745	view	20:35, 31 October 2018	ReactomeTeam	reactome version 65
100289	view	19:12, 31 October 2018	ReactomeTeam	reactome version 64
99835	view	15:56, 31 October 2018	ReactomeTeam	reactome version 63
99392	view	14:33, 31 October 2018	ReactomeTeam	reactome version 62 (2nd attempt)
99088	view	12:39, 31 October 2018	ReactomeTeam	reactome version 62
94058	view	13:54, 16 August 2017	ReactomeTeam	reactome version 61
93687	view	11:31, 9 August 2017	ReactomeTeam	reactome version 61
87172	view	19:26, 18 July 2016	Mkutmon	Ontology Term : 'infectious disease pathway' added !
86810	view	09:27, 11 July 2016	ReactomeTeam	reactome version 56
83087	view	09:57, 18 November 2015	ReactomeTeam	Version54
81411	view	12:56, 21 August 2015	ReactomeTeam	Version53
76880	view	08:15, 17 July 2014	ReactomeTeam	Fixed remaining interactions
76585	view	11:56, 16 July 2014	ReactomeTeam	Fixed remaining interactions
75918	view	09:57, 11 June 2014	ReactomeTeam	Re-fixing comment source
75618	view	10:48, 10 June 2014	ReactomeTeam	Reactome 48 Update
74973	view	13:49, 8 May 2014	Anwesha	Fixing comment source for displaying WikiPathways description
74617	view	08:40, 30 April 2014	ReactomeTeam	New pathway

External references

DataNodes

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Name	Type	Database reference	Comment
18S rRNA [cytosol]	Protein	X03205 (EMBL)
28S rRNA [cytosol]	Protein	M11167 (EMBL)
2xMe-SNRPB [nucleoplasm]	Protein	P14678 (Uniprot-TrEMBL)
2xMe-SNRPD1 [nucleoplasm]	Protein	P62314 (Uniprot-TrEMBL)
2xMe-SNRPD3 [nucleoplasm]	Protein	P62318 (Uniprot-TrEMBL)
5.8S rRNA [cytosol]	Protein	J01866 (EMBL)
5S rRNA [cytosol]	Protein	V00589 (EMBL)
7-methylguanosine cap [nucleoplasm]	Metabolite	CHEBI:17825 (ChEBI)
80S ribosome	Complex	REACT_4330 (Reactome)
AAAS [nuclear envelope]	Protein	Q9NRG9 (Uniprot-TrEMBL)
ALYREF [nucleoplasm]	Protein	Q86V81 (Uniprot-TrEMBL)
Acidified Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore	Complex	REACT_9103 (Reactome)
Aminoacyl-tRNA	Metabolite	REACT_4792 (Reactome)
CALR	Protein	P27797 (Uniprot-TrEMBL)
CANX	Protein	P27824 (Uniprot-TrEMBL)
CCAR1 [nucleoplasm]	Protein	Q8IX12 (Uniprot-TrEMBL)
CD2BP2 [nucleoplasm]	Protein	O95400 (Uniprot-TrEMBL)
CLTA [plasma membrane]	Protein	P09496 (Uniprot-TrEMBL)
Clathrin	Complex	REACT_9338 (Reactome)
Cleaved HA Influenza A Viral Particle	Complex	REACT_9239 (Reactome)
Crm1:Ran GTPase:GDP	Complex	REACT_6660 (Reactome)
DHX9 [nucleoplasm]	Protein	Q08211 (Uniprot-TrEMBL)
DNAJC3	Protein	Q13217 (Uniprot-TrEMBL)
Elongated vRNA-mRNA Complex	Complex	REACT_9568 (Reactome)	Capped, synthesized RNA strand complementary to vRNA, plus viral polymerase and template vRNA (Plotch, 1977).
FAU [cytosol]	Protein	P62861 (Uniprot-TrEMBL)
FUS [nucleoplasm]	Protein	P35637 (Uniprot-TrEMBL)
GDP [cytosol]	Metabolite	CHEBI:17552 (ChEBI)
GRSF1(?-?)	Protein	Q12849 (Uniprot-TrEMBL)
GTF2F1(2-517) [nucleoplasm]	Protein	P35269 (Uniprot-TrEMBL)
GTF2F2(2-249) [nucleoplasm]	Protein	P13984 (Uniprot-TrEMBL)
GTP [nucleoplasm]	Metabolite	CHEBI:15996 (ChEBI)
Genomic RNA Segment 1 [cytosol]	Protein	AF389115 (EMBL)
Genomic RNA Segment 1 [endosome lumen]	Protein	AF389115 (EMBL)
Genomic RNA Segment 1 [extracellular region]	Protein	AF389115 (EMBL)
Genomic RNA Segment 1 [nucleoplasm]	Protein	AF389115 (EMBL)
Genomic RNA Segment 2 [cytosol]	Protein	AF389116 (EMBL)
Genomic RNA Segment 2 [endosome lumen]	Protein	AF389116 (EMBL)
Genomic RNA Segment 2 [extracellular region]	Protein	AF389116 (EMBL)
Genomic RNA Segment 2 [nucleoplasm]	Protein	AF389116 (EMBL)
Genomic RNA Segment 3 [cytosol]	Protein	AF389117 (EMBL)
Genomic RNA Segment 3 [endosome lumen]	Protein	AF389117 (EMBL)
Genomic RNA Segment 3 [extracellular region]	Protein	AF389117 (EMBL)
Genomic RNA Segment 3 [nucleoplasm]	Protein	AF389117 (EMBL)
Genomic RNA Segment 4 [cytosol]	Protein	AF389118 (EMBL)
Genomic RNA Segment 4 [endosome lumen]	Protein	AF389118 (EMBL)
Genomic RNA Segment 4 [extracellular region]	Protein	AF389118 (EMBL)
Genomic RNA Segment 4 [nucleoplasm]	Protein	AF389118 (EMBL)
Genomic RNA Segment 5 [cytosol]	Protein	AF389119 (EMBL)
Genomic RNA Segment 5 [endosome lumen]	Protein	AF389119 (EMBL)
Genomic RNA Segment 5 [extracellular region]	Protein	AF389119 (EMBL)
Genomic RNA Segment 5 [nucleoplasm]	Protein	AF389119 (EMBL)
Genomic RNA Segment 6 [cytosol]	Protein	AF389120 (EMBL)
Genomic RNA Segment 6 [endosome lumen]	Protein	AF389120 (EMBL)
Genomic RNA Segment 6 [extracellular region]	Protein	AF389120 (EMBL)
Genomic RNA Segment 6 [nucleoplasm]	Protein	AF389120 (EMBL)
Genomic RNA Segment 7 [cytosol]	Protein	AF389121 (EMBL)
Genomic RNA Segment 7 [endosome lumen]	Protein	AF389121 (EMBL)
Genomic RNA Segment 7 [extracellular region]	Protein	AF389121 (EMBL)
Genomic RNA Segment 7 [nucleoplasm]	Protein	AF389121 (EMBL)
Genomic RNA Segment 8 [cytosol]	Protein	AF389122 (EMBL)
Genomic RNA Segment 8 [endosome lumen]	Protein	AF389122 (EMBL)
Genomic RNA Segment 8 [extracellular region]	Protein	AF389122 (EMBL)
Genomic RNA Segment 8 [nucleoplasm]	Protein	AF389122 (EMBL)
Glycosylated NA Tetramer	Complex	REACT_10176 (Reactome)
Glycosylated NA Tetramer	Complex	REACT_10567 (Reactome)
Glycosylated NA Tetramer	Complex	REACT_10972 (Reactome)
Glycosylated NA [Golgi membrane]	Protein	P03468 (Uniprot-TrEMBL)
Glycosylated NA [endocytic vesicle membrane]	Protein	P03468 (Uniprot-TrEMBL)
Glycosylated NA [endoplasmic reticulum membrane]	Protein	P03468 (Uniprot-TrEMBL)
Glycosylated NA [extracellular region]	Protein	P03468 (Uniprot-TrEMBL)
Glycosylated NA [plasma membrane]	Protein	P03468 (Uniprot-TrEMBL)
Glycosylated NA	Protein	P03468 (Uniprot-TrEMBL)
Glycosylated and folded HA [endoplasmic reticulum membrane]	Protein	P03452 (Uniprot-TrEMBL)
Glycosylated and folded HA trimer	Complex	REACT_10412 (Reactome)
Glycosylated and folded HA trimer	Complex	REACT_10554 (Reactome)
Glycosylated and folded HA trimer	Complex	REACT_10717 (Reactome)
Glycosylated and folded HA	Protein	P03452 (Uniprot-TrEMBL)
Glycosylated, palmitylated and folded HA trimer:Lipid Raft Complex	Complex	REACT_10369 (Reactome)
Glycosylated, palmitylated and folded HA trimer:Lipid Raft Complex	Complex	REACT_10581 (Reactome)
Glycosylated, palmitylated and folded HA trimer	Complex	REACT_10197 (Reactome)
Glycosylated, palmitylated and folded HA trimer	Complex	REACT_10978 (Reactome)
Gycosylated NA Tetramer:Lipid Raft	Complex	REACT_10662 (Reactome)
Gycosylated NA Tetramer:Lipid Raft	Complex	REACT_10954 (Reactome)
Gycosylated NA Tetramer	Complex	REACT_10841 (Reactome)
H+ [endosome lumen]	Metabolite	CHEBI:15378 (ChEBI)
H+	Metabolite	CHEBI:15378 (ChEBI)
HA folded and glycosylated [endocytic vesicle membrane]	Protein	P03452 (Uniprot-TrEMBL)
HA folded and glycosylated [Golgi membrane]	Protein	P03452 (Uniprot-TrEMBL)
HA folded, glycosylated, and palmitylated [extracellular region]	Protein	P03452 (Uniprot-TrEMBL)
HA folded, glycosylated, and palmitylated [Golgi membrane]	Protein	P03452 (Uniprot-TrEMBL)
HA folded, glycosylated, and palmitylated [plasma membrane]	Protein	P03452 (Uniprot-TrEMBL)
HA mRNA [nucleoplasm]	Protein	V01088 (EMBL)
HA1 [endocytic vesicle membrane]	Protein	P03452 (Uniprot-TrEMBL)
HA1 [endosome lumen]	Protein	P03452 (Uniprot-TrEMBL)
HA1 [extracellular region]	Protein	P03452 (Uniprot-TrEMBL)
HA2 [endosome lumen]	Protein	P03452 (Uniprot-TrEMBL)
HA2 [extracellular region]	Protein	P03452 (Uniprot-TrEMBL)
HA	Protein	P03452 (Uniprot-TrEMBL)
HNRNPA0 [nucleoplasm]	Protein	Q13151 (Uniprot-TrEMBL)
HNRNPA1 [nucleoplasm]	Protein	P09651 (Uniprot-TrEMBL)
HNRNPA2B1 [nucleoplasm]	Protein	P22626 (Uniprot-TrEMBL)
HNRNPA3 [nucleoplasm]	Protein	P51991 (Uniprot-TrEMBL)
HNRNPC [nucleoplasm]	Protein	P07910 (Uniprot-TrEMBL)
HNRNPD [nucleoplasm]	Protein	Q14103 (Uniprot-TrEMBL)
HNRNPF(1-415) [nucleoplasm]	Protein	P52597 (Uniprot-TrEMBL)
HNRNPH1(1-449) [nucleoplasm]	Protein	P31943 (Uniprot-TrEMBL)
HNRNPH2 [nucleoplasm]	Protein	P55795 (Uniprot-TrEMBL)
HNRNPK [nucleoplasm]	Protein	P61978 (Uniprot-TrEMBL)
HNRNPL [nucleoplasm]	Protein	P14866 (Uniprot-TrEMBL)
HNRNPM [nucleoplasm]	Protein	P52272 (Uniprot-TrEMBL)
HNRNPR [nucleoplasm]	Protein	O43390 (Uniprot-TrEMBL)
HNRNPU [nucleoplasm]	Protein	Q00839 (Uniprot-TrEMBL)
HNRNPUL1 [nucleoplasm]	Protein	Q9BUJ2 (Uniprot-TrEMBL)
HSP90AA1	Protein	P07900 (Uniprot-TrEMBL)
HSPA1A(2-641)	Protein	P08107 (Uniprot-TrEMBL)
Host Derived Lipid Bilayer Membrane Rich In Sphingolipids And Cholesterol		REACT_9200 (Reactome)
IPO5	Protein	O00410 (Uniprot-TrEMBL)
Influenza A Viral Envelope Inserted Into The Endocytic Vesicle Membrane	Complex	REACT_9160 (Reactome)
Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore	Complex	REACT_9315 (Reactome)
Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane	Complex	REACT_9257 (Reactome)
Influenza A Viral Particle With A Fusion Competent HA2	Complex	REACT_9163 (Reactome)
Influenza A Viral Particle	Complex	REACT_10742 (Reactome)
Influenza A Viral Particle	Complex	REACT_9077 (Reactome)
Influenza cRNA (complete)		REACT_9879 (Reactome)
Initiated cRNA-vRNA Complex	Complex	REACT_9672 (Reactome)	cRNA bound by NP and trimeric polymerase, capable of vRNA synthesis from the cRNA template.
Initiated vRNA Transcription Complex	Complex	REACT_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 Complex	Complex	REACT_9685 (Reactome)	vRNA bound by NP and trimeric polymerase, capable of complementary RNA synthesis.
Inter-Membrane Spanning HA2 [endocytic vesicle membrane]	Protein	P03452 (Uniprot-TrEMBL)
Intracellular assembly complex	Complex	REACT_10426 (Reactome)
KPNA1 [cytosol]	Protein	P52294 (Uniprot-TrEMBL)
KPNA1 [nucleoplasm]	Protein	P52294 (Uniprot-TrEMBL)
KPNA1	Protein	P52294 (Uniprot-TrEMBL)
KPNB1 [cytosol]	Protein	Q14974 (Uniprot-TrEMBL)
KPNB1 [nucleoplasm]	Protein	Q14974 (Uniprot-TrEMBL)
KPNB1	Protein	Q14974 (Uniprot-TrEMBL)
Lipid Raft		REACT_10385 (Reactome)
M1 [cytosol]	Protein	P03485 (Uniprot-TrEMBL)
M1 [endosome lumen]	Protein	P03485 (Uniprot-TrEMBL)
M1 [extracellular region]	Protein	P03485 (Uniprot-TrEMBL)
M1 [nucleoplasm]	Protein	P03485 (Uniprot-TrEMBL)
M1 mRNA [nucleoplasm]	Protein	AF389121 (EMBL)
M1 mRNA	Rna	AF389121 (EMBL)
M1	Protein	P03485 (Uniprot-TrEMBL)
M2 Tetramer	Complex	REACT_10281 (Reactome)
M2 Tetramer	Complex	REACT_10501 (Reactome)
M2 Tetramer	Complex	REACT_10683 (Reactome)
M2 [Golgi membrane]	Protein	P06821 (Uniprot-TrEMBL)
M2 [cytosol]	Protein	P06821 (Uniprot-TrEMBL)
M2 [endocytic vesicle membrane]	Protein	P06821 (Uniprot-TrEMBL)
M2 [endoplasmic reticulum membrane]	Protein	P06821 (Uniprot-TrEMBL)
M2 [endosome lumen]	Protein	P06821 (Uniprot-TrEMBL)
M2 mRNA [nucleoplasm]	Protein	AF389121 (EMBL)
M2 mRNA	Rna	AF389121 (EMBL)
M2	Protein	P06821 (Uniprot-TrEMBL)
Mature intronless transcript derived mRNA with m7G cap removed		REACT_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 mRNA		REACT_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 [endosome lumen]	Protein	P03468 (Uniprot-TrEMBL)
NA mRNA [nucleoplasm]	Protein	J02146 (EMBL)
NA	Protein	P03468 (Uniprot-TrEMBL)
NCBP1 [nucleoplasm]	Protein	Q09161 (Uniprot-TrEMBL)
NCBP2 [nucleoplasm]	Protein	P52298 (Uniprot-TrEMBL)
NEP/NS2 [extracellular region]	Protein	P03508 (Uniprot-TrEMBL)
NEP/NS2 [nucleoplasm]	Protein	P03508 (Uniprot-TrEMBL)
NEP/NS2 [cytosol]	Protein	P03508 (Uniprot-TrEMBL)
NEP/NS2 [endosome lumen]	Protein	P03508 (Uniprot-TrEMBL)
NEP/NS2	Protein	P03508 (Uniprot-TrEMBL)
NFX.1 [nucleoplasm]	Protein	O43831 (Uniprot-TrEMBL)
NP [Golgi membrane]	Protein	P03466 (Uniprot-TrEMBL)
NP [cytosol]	Protein	P03466 (Uniprot-TrEMBL)
NP [endosome lumen]	Protein	P03466 (Uniprot-TrEMBL)
NP [extracellular region]	Protein	P03466 (Uniprot-TrEMBL)
NP [nucleoplasm]	Protein	P03466 (Uniprot-TrEMBL)
NP [plasma membrane]	Protein	P03466 (Uniprot-TrEMBL)
NP mRNA [nucleoplasm]	Protein	J02147 (EMBL)
NP:Lipid Raft	Complex	REACT_10315 (Reactome)
NP:Lipid Raft	Complex	REACT_10830 (Reactome)
NP	Protein	P03466 (Uniprot-TrEMBL)
NS1 [cytosol]	Protein	P03496 (Uniprot-TrEMBL)
NS1 mRNA [nucleoplasm]	Protein	J02150 (EMBL)
NS1 mRNA	Rna	J02150 (EMBL)
NS1	Protein	P03496 (Uniprot-TrEMBL)
NS2 mRNA [nucleoplasm]	Protein	J02150 (EMBL)
NS2 mRNA	Rna	J02150 (EMBL)
NTP	Metabolite	REACT_4491 (Reactome)
NUP107 [nuclear envelope]	Protein	P57740 (Uniprot-TrEMBL)
NUP133 [nuclear envelope]	Protein	Q8WUM0 (Uniprot-TrEMBL)
NUP153 [nucleoplasm]	Protein	P49790 (Uniprot-TrEMBL)
NUP155 [nuclear envelope]	Protein	O75694 (Uniprot-TrEMBL)
NUP160 [nuclear envelope]	Protein	Q12769 (Uniprot-TrEMBL)
NUP188(2-1749) [nuclear envelope]	Protein	Q5SRE5 (Uniprot-TrEMBL)
NUP205(2-2012) [nuclear envelope]	Protein	Q92621 (Uniprot-TrEMBL)
NUP210 [nuclear envelope]	Protein	Q8TEM1 (Uniprot-TrEMBL)
NUP214 [cytosol]	Protein	P35658 (Uniprot-TrEMBL)
NUP35 [nuclear envelope]	Protein	Q8NFH5 (Uniprot-TrEMBL)
NUP37 [nuclear envelope]	Protein	Q8NFH4 (Uniprot-TrEMBL)
NUP43 [nuclear envelope]	Protein	Q8NFH3 (Uniprot-TrEMBL)
NUP50 [nucleoplasm]	Protein	Q9UKX7 (Uniprot-TrEMBL)
NUP54 [nuclear envelope]	Protein	Q7Z3B4 (Uniprot-TrEMBL)
NUP62 [nuclear envelope]	Protein	P37198 (Uniprot-TrEMBL)
NUP85 [nuclear envelope]	Protein	Q9BW27 (Uniprot-TrEMBL)
NUP88 [cytosol]	Protein	Q99567 (Uniprot-TrEMBL)
NUP93 [nuclear envelope]	Protein	Q8N1F7 (Uniprot-TrEMBL)
NUP98-5 [nuclear envelope]	Protein	P52948-5 (Uniprot-TrEMBL)
NUPL1-2 [nuclear envelope]	Protein	Q9BVL2-1 (Uniprot-TrEMBL)
NUPL2 [cytosol]	Protein	O15504 (Uniprot-TrEMBL)
Nuclear Pore Complex (NPC)	Complex	REACT_5542 (Reactome)
Nup45 [nuclear envelope]	Protein	Q9BVL2-2 (Uniprot-TrEMBL)
P1 mRNA [nucleoplasm]	Protein	J02151 (EMBL)
PA [cytosol]	Protein	P03433 (Uniprot-TrEMBL)
PA [endosome lumen]	Protein	P03433 (Uniprot-TrEMBL)
PA [extracellular region]	Protein	P03433 (Uniprot-TrEMBL)
PA [nucleoplasm]	Protein	P03433 (Uniprot-TrEMBL)
PA mRNA [nucleoplasm]	Protein	V01106 (EMBL)
PA	Protein	P03433 (Uniprot-TrEMBL)
PB1 [cytosol]	Protein	P03431 (Uniprot-TrEMBL)
PB1 [endosome lumen]	Protein	P03431 (Uniprot-TrEMBL)
PB1 [extracellular region]	Protein	P03431 (Uniprot-TrEMBL)
PB1 [nucleoplasm]	Protein	P03431 (Uniprot-TrEMBL)
PB1 mRNA	Rna	J02151 (EMBL)
PB1-F2	Protein	P0C0U1 (Uniprot-TrEMBL)
PB1	Protein	P03431 (Uniprot-TrEMBL)
PB2 [cytosol]	Protein	P03428 (Uniprot-TrEMBL)
PB2 [endosome lumen]	Protein	P03428 (Uniprot-TrEMBL)
PB2 [extracellular region]	Protein	P03428 (Uniprot-TrEMBL)
PB2 [nucleoplasm]	Protein	P03428 (Uniprot-TrEMBL)
PB2	Protein	P03428 (Uniprot-TrEMBL)
PCBP1 [nucleoplasm]	Protein	Q15365 (Uniprot-TrEMBL)
PCBP2 [nucleoplasm]	Protein	Q15366 (Uniprot-TrEMBL)
POLR2A [nucleoplasm]	Protein	P24928 (Uniprot-TrEMBL)
POLR2B [nucleoplasm]	Protein	P30876 (Uniprot-TrEMBL)
POLR2C [nucleoplasm]	Protein	P19387 (Uniprot-TrEMBL)
POLR2D(2-142) [nucleoplasm]	Protein	O15514 (Uniprot-TrEMBL)
POLR2E [nucleoplasm]	Protein	P19388 (Uniprot-TrEMBL)
POLR2F(1-127) [nucleoplasm]	Protein	P61218 (Uniprot-TrEMBL)
POLR2G [nucleoplasm]	Protein	P62487 (Uniprot-TrEMBL)
POLR2H [nucleoplasm]	Protein	P52434 (Uniprot-TrEMBL)
POLR2I [nucleoplasm]	Protein	P36954 (Uniprot-TrEMBL)
POLR2J [nucleoplasm]	Protein	P52435 (Uniprot-TrEMBL)
POLR2K [nucleoplasm]	Protein	P53803 (Uniprot-TrEMBL)
POLR2L [nucleoplasm]	Protein	P62875 (Uniprot-TrEMBL)
POM121 [nuclear envelope]	Protein	Q96HA1 (Uniprot-TrEMBL)
PTBP1 [nucleoplasm]	Protein	P26599 (Uniprot-TrEMBL)
Pi	Metabolite	CHEBI:18367 (ChEBI)
RAE1 [nuclear envelope]	Protein	P78406 (Uniprot-TrEMBL)
RAN [cytosol]	Protein	P62826 (Uniprot-TrEMBL)
RAN [nucleoplasm]	Protein	P62826 (Uniprot-TrEMBL)
RANBP2 [cytosol]	Protein	P49792 (Uniprot-TrEMBL)
RBM5 [nucleoplasm]	Protein	P52756 (Uniprot-TrEMBL)
RBMX(1-391) [nucleoplasm]	Protein	P38159 (Uniprot-TrEMBL)
RNA Polymerase II (phosphorylated):TFIIF:capped pre-mRNA	Complex	REACT_3935 (Reactome)
RNP Complex:Karyopherin alpha	Complex	REACT_9328 (Reactome)
RNP pre-assembly complex	Complex	REACT_11005 (Reactome)
RNP:Karyopherin alpha:Karyopherin beta complex	Complex	REACT_9158 (Reactome)
RNP:Karyopherin alpha:Karyopherin beta complex	Complex	REACT_9341 (Reactome)
RNPS1 [nucleoplasm]	Protein	Q15287 (Uniprot-TrEMBL)
RPL10 [cytosol]	Protein	P27635 (Uniprot-TrEMBL)
RPL10A [cytosol]	Protein	P62906 (Uniprot-TrEMBL)
RPL11 [cytosol]	Protein	P62913 (Uniprot-TrEMBL)
RPL12 [cytosol]	Protein	P30050 (Uniprot-TrEMBL)
RPL13(2-211) [cytosol]	Protein	P26373 (Uniprot-TrEMBL)
RPL13A [cytosol]	Protein	P40429 (Uniprot-TrEMBL)
RPL14 [cytosol]	Protein	P50914 (Uniprot-TrEMBL)
RPL15(2-204) [cytosol]	Protein	P61313 (Uniprot-TrEMBL)
RPL17 [cytosol]	Protein	P18621 (Uniprot-TrEMBL)
RPL18 [cytosol]	Protein	Q07020 (Uniprot-TrEMBL)
RPL18A [cytosol]	Protein	Q02543 (Uniprot-TrEMBL)
RPL19 [cytosol]	Protein	P84098 (Uniprot-TrEMBL)
RPL21 [cytosol]	Protein	P46778 (Uniprot-TrEMBL)
RPL22 [cytosol]	Protein	P35268 (Uniprot-TrEMBL)
RPL23 [cytosol]	Protein	P62829 (Uniprot-TrEMBL)
RPL23A [cytosol]	Protein	P62750 (Uniprot-TrEMBL)
RPL24 [cytosol]	Protein	P83731 (Uniprot-TrEMBL)
RPL26 [cytosol]	Protein	P61254 (Uniprot-TrEMBL)
RPL26L1(2-145) [cytosol]	Protein	Q9UNX3 (Uniprot-TrEMBL)
RPL27(2-136) [cytosol]	Protein	P61353 (Uniprot-TrEMBL)
RPL27A [cytosol]	Protein	P46776 (Uniprot-TrEMBL)
RPL28 [cytosol]	Protein	P46779 (Uniprot-TrEMBL)
RPL29 [cytosol]	Protein	P47914 (Uniprot-TrEMBL)
RPL3 [cytosol]	Protein	P39023 (Uniprot-TrEMBL)
RPL30(2-115) [cytosol]	Protein	P62888 (Uniprot-TrEMBL)
RPL31 [cytosol]	Protein	P62899 (Uniprot-TrEMBL)
RPL32 [cytosol]	Protein	P62910 (Uniprot-TrEMBL)
RPL34 [cytosol]	Protein	P49207 (Uniprot-TrEMBL)
RPL35 [cytosol]	Protein	P42766 (Uniprot-TrEMBL)
RPL35A [cytosol]	Protein	P18077 (Uniprot-TrEMBL)
RPL36 [cytosol]	Protein	Q9Y3U8 (Uniprot-TrEMBL)
RPL36A [cytosol]	Protein	P83881 (Uniprot-TrEMBL)
RPL37 [cytosol]	Protein	P61927 (Uniprot-TrEMBL)
RPL37A [cytosol]	Protein	P61513 (Uniprot-TrEMBL)
RPL38 [cytosol]	Protein	P63173 (Uniprot-TrEMBL)
RPL39 [cytosol]	Protein	P62891 (Uniprot-TrEMBL)
RPL3L(2-407) [cytosol]	Protein	Q92901 (Uniprot-TrEMBL)
RPL4 [cytosol]	Protein	P36578 (Uniprot-TrEMBL)
RPL41 [cytosol]	Protein	P62945 (Uniprot-TrEMBL)
RPL5 [cytosol]	Protein	P46777 (Uniprot-TrEMBL)
RPL6 [cytosol]	Protein	Q02878 (Uniprot-TrEMBL)
RPL7 [cytosol]	Protein	P18124 (Uniprot-TrEMBL)
RPL7A [cytosol]	Protein	P62424 (Uniprot-TrEMBL)
RPL8 [cytosol]	Protein	P62917 (Uniprot-TrEMBL)
RPL9 [cytosol]	Protein	P32969 (Uniprot-TrEMBL)
RPLP0 [cytosol]	Protein	P05388 (Uniprot-TrEMBL)
RPLP1(2-114) [cytosol]	Protein	P05386 (Uniprot-TrEMBL)
RPLP2 [cytosol]	Protein	P05387 (Uniprot-TrEMBL)
RPS10 [cytosol]	Protein	P46783 (Uniprot-TrEMBL)
RPS11 [cytosol]	Protein	P62280 (Uniprot-TrEMBL)
RPS12 [cytosol]	Protein	P25398 (Uniprot-TrEMBL)
RPS13(2-151) [cytosol]	Protein	P62277 (Uniprot-TrEMBL)
RPS14 [cytosol]	Protein	P62263 (Uniprot-TrEMBL)
RPS15 [cytosol]	Protein	P62841 (Uniprot-TrEMBL)
RPS15A [cytosol]	Protein	P62244 (Uniprot-TrEMBL)
RPS16 [cytosol]	Protein	P62249 (Uniprot-TrEMBL)
RPS17 [cytosol]	Protein	P08708 (Uniprot-TrEMBL)
RPS18 [cytosol]	Protein	P62269 (Uniprot-TrEMBL)
RPS19 [cytosol]	Protein	P39019 (Uniprot-TrEMBL)
RPS2(2-293) [cytosol]	Protein	P15880 (Uniprot-TrEMBL)
RPS20 [cytosol]	Protein	P60866 (Uniprot-TrEMBL)
RPS21 [cytosol]	Protein	P63220 (Uniprot-TrEMBL)
RPS23 [cytosol]	Protein	P62266 (Uniprot-TrEMBL)
RPS24 [cytosol]	Protein	P62847 (Uniprot-TrEMBL)
RPS25 [cytosol]	Protein	P62851 (Uniprot-TrEMBL)
RPS26 [cytosol]	Protein	P62854 (Uniprot-TrEMBL)
RPS27 [cytosol]	Protein	P42677 (Uniprot-TrEMBL)
RPS27A(77-156) [cytosol]	Protein	P62979 (Uniprot-TrEMBL)
RPS28 [cytosol]	Protein	P62857 (Uniprot-TrEMBL)
RPS29 [cytosol]	Protein	P62273 (Uniprot-TrEMBL)
RPS3 [cytosol]	Protein	P23396 (Uniprot-TrEMBL)
RPS3A [cytosol]	Protein	P61247 (Uniprot-TrEMBL)
RPS4X [cytosol]	Protein	P62701 (Uniprot-TrEMBL)
RPS4Y1(2-263) [cytosol]	Protein	P22090 (Uniprot-TrEMBL)
RPS5(1-204) [cytosol]	Protein	P46782 (Uniprot-TrEMBL)
RPS6 [cytosol]	Protein	P62753 (Uniprot-TrEMBL)
RPS7 [cytosol]	Protein	P62081 (Uniprot-TrEMBL)
RPS8(2-208) [cytosol]	Protein	P62241 (Uniprot-TrEMBL)
RPS9 [cytosol]	Protein	P46781 (Uniprot-TrEMBL)
RPSA [cytosol]	Protein	P08865 (Uniprot-TrEMBL)
Ran GTPase:GTP	Complex	REACT_6698 (Reactome)
Ribonucleoprotein (RNP) Complex	Complex	REACT_9223 (Reactome)
Ribonucleoprotein (RNP) Complex	Complex	REACT_9227 (Reactome)
SA [plasma membrane]	Metabolite	CHEBI:21622 (ChEBI)
SA	Metabolite	CHEBI:21622 (ChEBI)
SEH1L-2 [nuclear envelope]	Protein	Q96EE3-2 (Uniprot-TrEMBL)
SMC1A [nucleoplasm]	Protein	Q14683 (Uniprot-TrEMBL)
SNRNP70 [nucleoplasm]	Protein	P08621 (Uniprot-TrEMBL)
SNRPA [nucleoplasm]	Protein	P09012 (Uniprot-TrEMBL)
SNRPD2 [nucleoplasm]	Protein	P62316 (Uniprot-TrEMBL)
SNRPE [nucleoplasm]	Protein	P62304 (Uniprot-TrEMBL)
SNRPF [nucleoplasm]	Protein	P62306 (Uniprot-TrEMBL)
SNRPG [nucleoplasm]	Protein	P62308 (Uniprot-TrEMBL)
SRRM1 [nucleoplasm]	Protein	Q8IYB3 (Uniprot-TrEMBL)
SRSF1 [nucleoplasm]	Protein	Q07955 (Uniprot-TrEMBL)
SRSF2 [nucleoplasm]	Protein	Q01130 (Uniprot-TrEMBL)
SRSF3 [nucleoplasm]	Protein	P84103 (Uniprot-TrEMBL)
SRSF5 [nucleoplasm]	Protein	Q13243 (Uniprot-TrEMBL)
SRSF6 [nucleoplasm]	Protein	Q13247 (Uniprot-TrEMBL)
SRSF7 [nucleoplasm]	Protein	Q16629 (Uniprot-TrEMBL)
SRSF9 [nucleoplasm]	Protein	Q13242 (Uniprot-TrEMBL)
SUGP1 [nucleoplasm]	Protein	Q8IWZ8 (Uniprot-TrEMBL)
Segment 1 RNP	Complex	REACT_10624 (Reactome)
Segment 2 RNP	Complex	REACT_10270 (Reactome)
Segment 3 RNP	Complex	REACT_10968 (Reactome)
Segment 4 RNP	Complex	REACT_10933 (Reactome)
Segment 5 RNP	Complex	REACT_10746 (Reactome)
Segment 6 RNP	Complex	REACT_10870 (Reactome)
Segment 7 RNP	Complex	REACT_10503 (Reactome)
Segment 8 RNP	Complex	REACT_10273 (Reactome)
Sialic Acid Bound Influenza A Viral Particle	Complex	REACT_10492 (Reactome)
Sialic Acid Bound Influenza A Viral Particle	Complex	REACT_9232 (Reactome)
Spliceosomal E Complex	Complex	REACT_4545 (Reactome)
TPR [nucleoplasm]	Protein	P12270 (Uniprot-TrEMBL)
U1 snRNA [nucleoplasm]	Protein	V00590 (EMBL)
U2AF1 [nucleoplasm]	Protein	Q01081 (Uniprot-TrEMBL)
U2AF2 [nucleoplasm]	Protein	P26368 (Uniprot-TrEMBL)
UBA52(77-128) [cytosol]	Protein	P62987 (Uniprot-TrEMBL)
Viral Polymerase	Complex	REACT_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 Proteins	Complex	REACT_9572 (Reactome)
XPO1 [cytosol]	Protein	O14980 (Uniprot-TrEMBL)
XPO1 [nucleoplasm]	Protein	O14980 (Uniprot-TrEMBL)
XPO1	Protein	O14980 (Uniprot-TrEMBL)
YBX1 [nucleoplasm]	Protein	P67809 (Uniprot-TrEMBL)
cRNP	Complex	REACT_9556 (Reactome)	Extended cRNA complexed with viral NP and trimeric polymerase.
p-S5-POLR2A [nucleoplasm]	Protein	P24928 (Uniprot-TrEMBL)
palmitylated M2 Tetramer	Complex	REACT_10389 (Reactome)
palmitylated M2 Tetramer	Complex	REACT_10582 (Reactome)
palmitylated M2 [Golgi membrane]	Protein	P06821 (Uniprot-TrEMBL)
palmitylated M2 [extracellular region]	Protein	P06821 (Uniprot-TrEMBL)
palmitylated M2 [plasma membrane]	Protein	P06821 (Uniprot-TrEMBL)
vRNA (Genomic):NP Complex	Complex	REACT_9729 (Reactome)
vRNA (genomic)	Protein	REACT_9646 (Reactome)
vRNA Transcription Complex	Complex	REACT_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 Export Complex	Complex	REACT_9906 (Reactome)
vRNP destined for Export	Complex	REACT_9574 (Reactome)
vRNP:M1 for Export	Complex	REACT_9769 (Reactome)
vRNP:M1:NEP:NP	Complex	REACT_9710 (Reactome)
vRNP:M1:NEP	Complex	REACT_9569 (Reactome)
vRNP	Complex	REACT_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 mRNA	Rna	REACT_9782 (Reactome)
viral mRNA	Protein	REACT_9819 (Reactome)

Annotated Interactions

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Source	Target	Type	Database reference	Comment
80S ribosome		mim-catalysis	REACT_9514 (Reactome)
80S ribosome		mim-catalysis	REACT_9524 (Reactome)
	Acidified Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore	Arrow	REACT_6315 (Reactome)
Acidified Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore			REACT_6230 (Reactome)
Aminoacyl-tRNA			REACT_9514 (Reactome)
Aminoacyl-tRNA			REACT_9524 (Reactome)
CALR		Arrow	REACT_6177 (Reactome)
CANX		Arrow	REACT_6177 (Reactome)
Clathrin		Arrow	REACT_6262 (Reactome)
Cleaved HA Influenza A Viral Particle			REACT_6232 (Reactome)
	Crm1:Ran GTPase:GDP	Arrow	REACT_6136 (Reactome)
DNAJC3		Arrow	REACT_9514 (Reactome)
	Elongated vRNA-mRNA Complex	Arrow	REACT_6210 (Reactome)
Elongated vRNA-mRNA Complex			REACT_6264 (Reactome)
GRSF1(?-?)		Arrow	REACT_9514 (Reactome)
	Glycosylated NA Tetramer	Arrow	REACT_6225 (Reactome)
	Glycosylated NA Tetramer	Arrow	REACT_6231 (Reactome)
	Glycosylated NA Tetramer	Arrow	REACT_6273 (Reactome)
Glycosylated NA Tetramer			REACT_6225 (Reactome)
Glycosylated NA Tetramer			REACT_6273 (Reactome)
Glycosylated NA Tetramer			REACT_9947 (Reactome)
	Glycosylated NA	Arrow	REACT_6181 (Reactome)
Glycosylated NA			REACT_6231 (Reactome)
	Glycosylated and folded HA trimer	Arrow	REACT_6141 (Reactome)
	Glycosylated and folded HA trimer	Arrow	REACT_6225 (Reactome)
	Glycosylated and folded HA trimer	Arrow	REACT_6273 (Reactome)
Glycosylated and folded HA trimer			REACT_6187 (Reactome)
Glycosylated and folded HA trimer			REACT_6225 (Reactome)
Glycosylated and folded HA trimer			REACT_6273 (Reactome)
	Glycosylated and folded HA	Arrow	REACT_6177 (Reactome)
Glycosylated and folded HA			REACT_6141 (Reactome)
	Glycosylated, palmitylated and folded HA trimer:Lipid Raft Complex	Arrow	REACT_10039 (Reactome)
	Glycosylated, palmitylated and folded HA trimer:Lipid Raft Complex	Arrow	REACT_6146 (Reactome)
Glycosylated, palmitylated and folded HA trimer:Lipid Raft Complex			REACT_10039 (Reactome)
	Glycosylated, palmitylated and folded HA trimer	Arrow	REACT_6187 (Reactome)
Glycosylated, palmitylated and folded HA trimer			REACT_10077 (Reactome)
Glycosylated, palmitylated and folded HA trimer			REACT_6146 (Reactome)
	Gycosylated NA Tetramer:Lipid Raft	Arrow	REACT_10039 (Reactome)
	Gycosylated NA Tetramer:Lipid Raft	Arrow	REACT_9947 (Reactome)
Gycosylated NA Tetramer:Lipid Raft			REACT_10039 (Reactome)
Gycosylated NA Tetramer			REACT_10077 (Reactome)
	H+	Arrow	REACT_6230 (Reactome)
H+			REACT_6315 (Reactome)
	HA	Arrow	REACT_6309 (Reactome)
HA			REACT_6177 (Reactome)
HA			REACT_6309 (Reactome)
HSP90AA1		Arrow	REACT_9428 (Reactome)
HSPA1A(2-641)		TBar	REACT_9407 (Reactome)
Host Derived Lipid Bilayer Membrane Rich In Sphingolipids And Cholesterol			REACT_6193 (Reactome)
IPO5		Arrow	REACT_9428 (Reactome)
	Influenza A Viral Envelope Inserted Into The Endocytic Vesicle Membrane	Arrow	REACT_6230 (Reactome)
	Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore	Arrow	REACT_6176 (Reactome)
Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore			REACT_6315 (Reactome)
Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore		mim-catalysis	REACT_6315 (Reactome)
	Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane	Arrow	REACT_6180 (Reactome)
Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane			REACT_6176 (Reactome)
	Influenza A Viral Particle With A Fusion Competent HA2	Arrow	REACT_6219 (Reactome)
Influenza A Viral Particle With A Fusion Competent HA2			REACT_6180 (Reactome)
	Influenza A Viral Particle	Arrow	REACT_6262 (Reactome)
	Influenza A Viral Particle	Arrow	REACT_6348 (Reactome)
Influenza A Viral Particle			REACT_6219 (Reactome)
	Influenza cRNA (complete)	Arrow	REACT_9438 (Reactome)
	Initiated cRNA-vRNA Complex	Arrow	REACT_9487 (Reactome)
Initiated cRNA-vRNA Complex			REACT_9438 (Reactome)
	Initiated vRNA Transcription Complex	Arrow	REACT_6239 (Reactome)
Initiated vRNA Transcription Complex			REACT_6210 (Reactome)
	Initiated vRNA-cRNA Complex	Arrow	REACT_9513 (Reactome)
Initiated vRNA-cRNA Complex			REACT_9404 (Reactome)
	Intracellular assembly complex	Arrow	REACT_10077 (Reactome)
Intracellular assembly complex			REACT_6193 (Reactome)
	KPNA1	Arrow	REACT_6164 (Reactome)
KPNA1			REACT_6138 (Reactome)
	KPNB1	Arrow	REACT_6164 (Reactome)
KPNB1			REACT_6322 (Reactome)
Lipid Raft			REACT_6146 (Reactome)
Lipid Raft			REACT_6271 (Reactome)
Lipid Raft			REACT_9947 (Reactome)
M1 mRNA			REACT_9402 (Reactome)
	M1	Arrow	REACT_6137 (Reactome)
	M1	Arrow	REACT_6230 (Reactome)
M1			REACT_10077 (Reactome)
M1			REACT_6137 (Reactome)
M1			REACT_9407 (Reactome)
	M2 Tetramer	Arrow	REACT_10123 (Reactome)
	M2 Tetramer	Arrow	REACT_6225 (Reactome)
	M2 Tetramer	Arrow	REACT_6273 (Reactome)
M2 Tetramer			REACT_10133 (Reactome)
M2 Tetramer			REACT_6225 (Reactome)
M2 Tetramer			REACT_6273 (Reactome)
	M2 mRNA	Arrow	REACT_9402 (Reactome)
	M2 mRNA	Arrow	REACT_9528 (Reactome)
M2 mRNA			REACT_9528 (Reactome)
	M2	Arrow	REACT_10095 (Reactome)
M2			REACT_10095 (Reactome)
M2			REACT_10123 (Reactome)
	Mature intronless transcript derived mRNA with m7G cap removed	Arrow	REACT_6239 (Reactome)
Mature intronless transcript derived mRNA			REACT_6142 (Reactome)
	NA	Arrow	REACT_10062 (Reactome)
NA			REACT_10062 (Reactome)
NA			REACT_6181 (Reactome)
NA		mim-catalysis	REACT_6348 (Reactome)
	NEP/NS2	Arrow	REACT_6230 (Reactome)
NEP/NS2			REACT_10077 (Reactome)
NEP/NS2			REACT_6303 (Reactome)
	NP:Lipid Raft	Arrow	REACT_10039 (Reactome)
	NP:Lipid Raft	Arrow	REACT_6271 (Reactome)
NP:Lipid Raft			REACT_10039 (Reactome)
NP		Arrow	REACT_6142 (Reactome)
NP		Arrow	REACT_9485 (Reactome)
NP		Arrow	REACT_9513 (Reactome)
NP			REACT_10077 (Reactome)
NP			REACT_6271 (Reactome)
NP			REACT_9404 (Reactome)
NP			REACT_9438 (Reactome)
NP			REACT_9490 (Reactome)
NS1 mRNA			REACT_9402 (Reactome)
NS1		Arrow	REACT_9514 (Reactome)
	NS2 mRNA	Arrow	REACT_9402 (Reactome)
	NS2 mRNA	Arrow	REACT_9528 (Reactome)
NS2 mRNA			REACT_9528 (Reactome)
NTP			REACT_6210 (Reactome)
NTP			REACT_9404 (Reactome)
NTP			REACT_9438 (Reactome)
NTP			REACT_9513 (Reactome)
Nuclear Pore Complex (NPC)		Arrow	REACT_6136 (Reactome)
Nuclear Pore Complex (NPC)		Arrow	REACT_6289 (Reactome)
PA			REACT_10077 (Reactome)
PA			REACT_9428 (Reactome)
PA			REACT_9485 (Reactome)
PB1 mRNA			REACT_9524 (Reactome)
	PB1-F2	Arrow	REACT_9524 (Reactome)
PB1			REACT_10077 (Reactome)
PB1			REACT_9428 (Reactome)
PB1			REACT_9485 (Reactome)
PB2			REACT_10077 (Reactome)
PB2			REACT_9428 (Reactome)
PB2			REACT_9485 (Reactome)
	Pi	Arrow	REACT_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 5â€™ end of the vRNA may remain bound during elongation as the template is threaded through in a 3â€™ to 5â€™ 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 5Ã¢â‚¬â„¢ 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 (phosphorylated):TFIIF:capped pre-mRNA		Arrow	REACT_6142 (Reactome)
	RNP Complex:Karyopherin alpha	Arrow	REACT_6138 (Reactome)
RNP Complex:Karyopherin alpha			REACT_6322 (Reactome)
	RNP pre-assembly complex	Arrow	REACT_6336 (Reactome)
RNP pre-assembly complex			REACT_10077 (Reactome)
	RNP:Karyopherin alpha:Karyopherin beta complex	Arrow	REACT_6289 (Reactome)
	RNP:Karyopherin alpha:Karyopherin beta complex	Arrow	REACT_6322 (Reactome)
RNP:Karyopherin alpha:Karyopherin beta complex			REACT_6164 (Reactome)
RNP:Karyopherin alpha:Karyopherin beta complex			REACT_6289 (Reactome)
Ran GTPase:GTP			REACT_6136 (Reactome)
	Ribonucleoprotein (RNP) Complex	Arrow	REACT_6164 (Reactome)
	Ribonucleoprotein (RNP) Complex	Arrow	REACT_6230 (Reactome)
Ribonucleoprotein (RNP) Complex			REACT_6138 (Reactome)
	SA	Arrow	REACT_6262 (Reactome)
SA			REACT_6193 (Reactome)
SA			REACT_6232 (Reactome)
Segment 1 RNP			REACT_6336 (Reactome)
Segment 2 RNP			REACT_6336 (Reactome)
Segment 3 RNP			REACT_6336 (Reactome)
Segment 4 RNP			REACT_6336 (Reactome)
Segment 5 RNP			REACT_6336 (Reactome)
Segment 6 RNP			REACT_6336 (Reactome)
Segment 7 RNP			REACT_6336 (Reactome)
Segment 8 RNP			REACT_6336 (Reactome)
	Sialic Acid Bound Influenza A Viral Particle	Arrow	REACT_6193 (Reactome)
	Sialic Acid Bound Influenza A Viral Particle	Arrow	REACT_6232 (Reactome)
Sialic Acid Bound Influenza A Viral Particle			REACT_6262 (Reactome)
Sialic Acid Bound Influenza A Viral Particle			REACT_6348 (Reactome)
	Viral Polymerase	Arrow	REACT_6264 (Reactome)
	Viral Polymerase	Arrow	REACT_9404 (Reactome)
	Viral Polymerase	Arrow	REACT_9428 (Reactome)
	Viral Polymerase	Arrow	REACT_9438 (Reactome)
Viral Polymerase			REACT_6142 (Reactome)
Viral Polymerase			REACT_9487 (Reactome)
Viral Polymerase			REACT_9513 (Reactome)
Viral Polymerase		mim-catalysis	REACT_6210 (Reactome)
Viral Polymerase		mim-catalysis	REACT_6239 (Reactome)
Viral Polymerase		mim-catalysis	REACT_6264 (Reactome)
Viral Polymerase		mim-catalysis	REACT_9404 (Reactome)
Viral Polymerase		mim-catalysis	REACT_9438 (Reactome)
Viral Polymerase		mim-catalysis	REACT_9487 (Reactome)
Viral Polymerase		mim-catalysis	REACT_9513 (Reactome)
	Viral Proteins	Arrow	REACT_9514 (Reactome)
XPO1			REACT_6194 (Reactome)
	cRNP	Arrow	REACT_9404 (Reactome)
	cRNP	Arrow	REACT_9438 (Reactome)
cRNP			REACT_9487 (Reactome)
	palmitylated M2 Tetramer	Arrow	REACT_10039 (Reactome)
	palmitylated M2 Tetramer	Arrow	REACT_10133 (Reactome)
palmitylated M2 Tetramer			REACT_10039 (Reactome)
palmitylated M2 Tetramer			REACT_10077 (Reactome)
	vRNA (Genomic):NP Complex	Arrow	REACT_6264 (Reactome)
	vRNA (Genomic):NP Complex	Arrow	REACT_9404 (Reactome)
	vRNA (Genomic):NP Complex	Arrow	REACT_9438 (Reactome)
	vRNA (Genomic):NP Complex	Arrow	REACT_9490 (Reactome)
vRNA (Genomic):NP Complex			REACT_6142 (Reactome)
vRNA (Genomic):NP Complex			REACT_9513 (Reactome)
vRNA (genomic)			REACT_9490 (Reactome)
	vRNA Transcription Complex	Arrow	REACT_6142 (Reactome)
vRNA Transcription Complex			REACT_6239 (Reactome)
	vRNP Export Complex	Arrow	REACT_6194 (Reactome)
vRNP Export Complex			REACT_6136 (Reactome)
	vRNP destined for Export	Arrow	REACT_9485 (Reactome)
vRNP destined for Export			REACT_9407 (Reactome)
	vRNP:M1 for Export	Arrow	REACT_9407 (Reactome)
vRNP:M1 for Export			REACT_6303 (Reactome)
	vRNP:M1:NEP:NP	Arrow	REACT_6136 (Reactome)
	vRNP:M1:NEP	Arrow	REACT_6303 (Reactome)
vRNP:M1:NEP			REACT_6194 (Reactome)
vRNP			REACT_9485 (Reactome)
	viral mRNA	Arrow	REACT_6264 (Reactome)
	viral mRNA	Arrow	REACT_9529 (Reactome)
viral mRNA			REACT_9514 (Reactome)
viral mRNA			REACT_9529 (Reactome)

Influenza Infection (Homo sapiens)

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