Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.

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 [...]

Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.

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.

Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.

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 [...]

Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.

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.

Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.

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.

Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.

Listeriolysin positive regulatory protein; Positively regulates expression of listeriolysin, of 1- phosphadidylinositol phosphodiesterase (PI-PLC) and other virulence factors.

D-alanine-activating enzyme (dae),D-alanine-D-alanyl carrier protein ligase (dcl); Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D- alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net cha [...]

D-alanyl carrier protein; Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC- carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.

D-alanyl carrier protein; Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC- carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.

D-alanine-activating enzyme (dae),D-alanine-D-alanyl carrier protein ligase (dcl); Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D- alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net cha [...]

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 [...]

Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.

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 [...]

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 [...]

Listeriolysin positive regulatory protein; Positively regulates expression of listeriolysin, of 1- phosphadidylinositol phosphodiesterase (PI-PLC) and other virulence factors.

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.

Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.

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 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.

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 [...]

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.

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.

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.

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.