Listeria monocytogenes entry into host cells (Homo sapiens)
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Description
Listeria monocytogenes is a short, gram-positive, nonspore-forming motile rod. Serotypes 1/2a, 1/2b and 4b make up more than 95% of isolates from humans, with serotype 4b causing most of the food-borne outbreaks. Listeria monocytogenes enters the body through the gastrointestinal tract after ingestion of contaminated food. The bacteria can survive food preservation procedures, such as refrigeration, low pH and high salt.
Listeria monocytogenes expresses several adhesin proteins at the cell surface that facilitate bacterial binding and entry to host cells. The bacteria can enter host cells through endocytosis mediated by binding of the bacterial InlA (internalin) protein to CDH1 (E-cadherin) at the host cell plasma membrane. Listeria monocytogenes can also enter host cells through endocytosis mediated by binding of the bacterial InlB protein to MET receptor tyrosine kinase at the host cell plasma membrane. Listeria monocytogenes proliferates inside the host cells and triggers formation of filopods, elongated protrusions of the host plasma membrane that contain bacteria. Filopods are ingested by adjacent cells, allowing Listeria monocytogenes to spread from cell to cell, invisible to the immune system of the host.
Listeria monocytogenes can cross the intestinal, blood-brain and placental barriers. In immunocompetent adults Listeria monocytogenes infection usually causes gastroenteritis. In infants infected in utero and in immunocompromised adults Listeria monocytogenes infection can result in meningoencephalitis and bacteremia (sepsis).
InlA is critical for crossing the intestinal barrier while both InlA and InlB are needed for crossing the placental barrier (Gessain et al. 2015) and, based on in vitro studies, the blood-cerebrospinal fluid barrier (Grundler et al. 2013). It seems that the intrinsic level of PI3K activity in Listeria-targeted host cells determines whether the entry depends on InlA only or InlA and InlB. The interaction of InlA with E-cadherin does not activate PI3K/AKT signaling while the interaction of InlB with the MET receptor activated the PI3K/AKT signal transduction cascade. Therefore, InlB-MET interaction may be important in tissues with low intrinsic PI3K activity (Gessain et al. 2015). Even if InlA-E-cadherin route is sufficient for bacterial entry, InlB may accelerate bacterial invasion (Pentecost et al. 2010). Cholesterol levels in host cell plasma membrane may also influence the preferred route for bacterial endocytosis (Seveau et al. 2004). In addition to InlA and InlB, many other virulence factors are involved in the Listeria monocytogenes infection cycle (Camejo et al. 2011) and will be annotated as mechanistic details become available.
For review, please refer to Bonazzi et al. 2009, Brooks et al. 2010, Camejo et al. 2011, Pizarro-Cerda et al. 2012. View original pathway at:Reactome.
Listeria monocytogenes expresses several adhesin proteins at the cell surface that facilitate bacterial binding and entry to host cells. The bacteria can enter host cells through endocytosis mediated by binding of the bacterial InlA (internalin) protein to CDH1 (E-cadherin) at the host cell plasma membrane. Listeria monocytogenes can also enter host cells through endocytosis mediated by binding of the bacterial InlB protein to MET receptor tyrosine kinase at the host cell plasma membrane. Listeria monocytogenes proliferates inside the host cells and triggers formation of filopods, elongated protrusions of the host plasma membrane that contain bacteria. Filopods are ingested by adjacent cells, allowing Listeria monocytogenes to spread from cell to cell, invisible to the immune system of the host.
Listeria monocytogenes can cross the intestinal, blood-brain and placental barriers. In immunocompetent adults Listeria monocytogenes infection usually causes gastroenteritis. In infants infected in utero and in immunocompromised adults Listeria monocytogenes infection can result in meningoencephalitis and bacteremia (sepsis).
InlA is critical for crossing the intestinal barrier while both InlA and InlB are needed for crossing the placental barrier (Gessain et al. 2015) and, based on in vitro studies, the blood-cerebrospinal fluid barrier (Grundler et al. 2013). It seems that the intrinsic level of PI3K activity in Listeria-targeted host cells determines whether the entry depends on InlA only or InlA and InlB. The interaction of InlA with E-cadherin does not activate PI3K/AKT signaling while the interaction of InlB with the MET receptor activated the PI3K/AKT signal transduction cascade. Therefore, InlB-MET interaction may be important in tissues with low intrinsic PI3K activity (Gessain et al. 2015). Even if InlA-E-cadherin route is sufficient for bacterial entry, InlB may accelerate bacterial invasion (Pentecost et al. 2010). Cholesterol levels in host cell plasma membrane may also influence the preferred route for bacterial endocytosis (Seveau et al. 2004). In addition to InlA and InlB, many other virulence factors are involved in the Listeria monocytogenes infection cycle (Camejo et al. 2011) and will be annotated as mechanistic details become available.
For review, please refer to Bonazzi et al. 2009, Brooks et al. 2010, Camejo et al. 2011, Pizarro-Cerda et al. 2012. View original pathway at:Reactome.
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CBLL1 may undergo SRC-mediated phosphorylation and subsequent auto-ubiquitination (Fujita et al. 2002).