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 [...]

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.

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 [...]

Phospholipase C; Important role in the infectious process. May contribute to efficient lysis of the two-membrane vacuoles that surround the bacteria after direct cell-to-cell spread.

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.

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 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 [...]

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.

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

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.

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.

Phospholipase C; Important role in the infectious process. May contribute to efficient lysis of the two-membrane vacuoles that surround the bacteria after direct cell-to-cell spread.

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.

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.

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.

Fosfomycin resistance protein FosX; Catalyzes the hydration of fosfomycin. Belongs to the fosfomycin resistance protein 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.

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

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.

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.

Phospholipase C; Important role in the infectious process. May contribute to efficient lysis of the two-membrane vacuoles that surround the bacteria after direct cell-to-cell spread.

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 [...]