Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity). Binds plasminogen when expressed on the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity, which in turn contributes to tissue invasion and virulence; Belongs to the enolase family.

Elongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.

Flagellin protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...]

Flagellin protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Internalin A; Mediates the entry of L.monocytogenes into host intestinal epithelial cells; transformation with inlA alone allows L.innocua (a non-invasive species) to be taken up by host cells. Binds to human receptor cadherin-1 (E-cadherin, CDH1); the chicken homolog of cadherin-1 but not cadherin- 2 function as receptors. Mouse cadherin-1 is not a receptor, however mutating a single surface-exposed residue (Glu-172 to Pro in mouse) allows cadherin-1 to act as a receptor for InlA ; Belongs to the internalin family.

Flagellin protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Internalin B; Mediates the entry of L.monocytogenes into normally non- phagocytic mammalian host cells. Its host receptor is hepatocyte growth factor receptor (HGF receptor, a tyrosine kinase, MET) which is tyrosine-phosphorylated in response to InlB. Downstream targets MAPK1/MAPK3 (Erk1/2) and AKT are phosphorylated in response to InlB, which also causes cell colony scattering. Complement component 1 Q subcomponent-binding protein (gC1q-R, C1QBP) has been suggested to also act an InlB receptor, but this is less certain. Stimulation of Tyr-phosphorylation of MET by InlB is potentiated [...]

Flagellin protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Similar to internalin protein, putative peptidoglycan bound protein (LPXTG motif).

Flagellin protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Similar to internalin proteins, putative peptidoglycan bound protein (LPXTG motif).

Flagellin protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Similar to flagellar hook-associated protein FlgK.

Flagellin protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Flagellar hook-associated protein 2; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.

Flagellin protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Similar to internalin proteins, putative peptidoglycan bound protein (LPXTG motif).

Flagellin protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Phosphatidylinositol-specific phospholipase c; Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Important factor in pathogenesis, PI-PLC activity is present only in virulent listeria species. It may participate in the lysis of the phagolysosomal membrane.

Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...]

Flagellin protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...]

P60 extracellular protein, invasion associated protein Iap; This major extracellular protein may be involved in the invasion of non-professional phagocytic cells by Listeria; Belongs to the peptidase C40 family.

Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...]

Internalin A; Mediates the entry of L.monocytogenes into host intestinal epithelial cells; transformation with inlA alone allows L.innocua (a non-invasive species) to be taken up by host cells. Binds to human receptor cadherin-1 (E-cadherin, CDH1); the chicken homolog of cadherin-1 but not cadherin- 2 function as receptors. Mouse cadherin-1 is not a receptor, however mutating a single surface-exposed residue (Glu-172 to Pro in mouse) allows cadherin-1 to act as a receptor for InlA ; Belongs to the internalin family.

Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...]

Internalin B; Mediates the entry of L.monocytogenes into normally non- phagocytic mammalian host cells. Its host receptor is hepatocyte growth factor receptor (HGF receptor, a tyrosine kinase, MET) which is tyrosine-phosphorylated in response to InlB. Downstream targets MAPK1/MAPK3 (Erk1/2) and AKT are phosphorylated in response to InlB, which also causes cell colony scattering. Complement component 1 Q subcomponent-binding protein (gC1q-R, C1QBP) has been suggested to also act an InlB receptor, but this is less certain. Stimulation of Tyr-phosphorylation of MET by InlB is potentiated [...]

Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...]

Listeria nuclear targeted protein A; Relieves the repression of host cell immune response genes (interferon-stimulated genes) by blocking the recruitment of host BAHD1 to these genes. May modulate interferon-mediated immune response to control bacterial colonization of the host.

Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...]

Internalin J; Involved in several steps of L.monocytogenes infection by both intravenous and oral infection. Probably acts as an adhesion; upon ectopic expression in L.innocula bacteria adhere better to human cell lines.

Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...]

Zinc metalloproteinase precursor; Probably linked to the pathogenesis of listerial infection; Belongs to the peptidase M4 family.

Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...]

Phosphatidylinositol-specific phospholipase c; Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Important factor in pathogenesis, PI-PLC activity is present only in virulent listeria species. It may participate in the lysis of the phagolysosomal membrane.

P60 extracellular protein, invasion associated protein Iap; This major extracellular protein may be involved in the invasion of non-professional phagocytic cells by Listeria; Belongs to the peptidase C40 family.

Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...]

P60 extracellular protein, invasion associated protein Iap; This major extracellular protein may be involved in the invasion of non-professional phagocytic cells by Listeria; Belongs to the peptidase C40 family.

Internalin A; Mediates the entry of L.monocytogenes into host intestinal epithelial cells; transformation with inlA alone allows L.innocua (a non-invasive species) to be taken up by host cells. Binds to human receptor cadherin-1 (E-cadherin, CDH1); the chicken homolog of cadherin-1 but not cadherin- 2 function as receptors. Mouse cadherin-1 is not a receptor, however mutating a single surface-exposed residue (Glu-172 to Pro in mouse) allows cadherin-1 to act as a receptor for InlA ; Belongs to the internalin family.