| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ABD29286.1 | sspA | SAOUHSC_00105 | SAOUHSC_00988 | Phosphonate ABC transporter, substrate-binding protein, putative. | Glutamyl endopeptidase precursor, putative; Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobu [...] | 0.572 |
| clfA | clfB | SAOUHSC_00812 | SAOUHSC_02963 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | 0.733 |
| clfA | fnbA | SAOUHSC_00812 | SAOUHSC_02803 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Fibronectin-binding protein precursor, putative; Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding sit [...] | 0.901 |
| clfA | hly | SAOUHSC_00812 | SAOUHSC_01121 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Alpha-hemolysin precursor; Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Inhibits host neutrophil chemotaxis to the lesion region (Probable). Heptamer oligomerization and pore formation is required for lytic activity (By similarity). Belongs to the aerolysin family. | 0.753 |
| clfA | lip2 | SAOUHSC_00812 | SAOUHSC_00300 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Lipase precursor. | 0.473 |
| clfA | sspA | SAOUHSC_00812 | SAOUHSC_00988 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Glutamyl endopeptidase precursor, putative; Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobu [...] | 0.567 |
| clfA | sspB | SAOUHSC_00812 | SAOUHSC_00987 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Cysteine protease precursor, putative; Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin- 3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin. | 0.438 |
| clfB | clfA | SAOUHSC_02963 | SAOUHSC_00812 | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | 0.733 |
| clfB | fnbA | SAOUHSC_02963 | SAOUHSC_02803 | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | Fibronectin-binding protein precursor, putative; Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding sit [...] | 0.601 |
| clfB | hly | SAOUHSC_02963 | SAOUHSC_01121 | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | Alpha-hemolysin precursor; Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Inhibits host neutrophil chemotaxis to the lesion region (Probable). Heptamer oligomerization and pore formation is required for lytic activity (By similarity). Belongs to the aerolysin family. | 0.613 |
| clfB | lip2 | SAOUHSC_02963 | SAOUHSC_00300 | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | Lipase precursor. | 0.477 |
| clfB | sspA | SAOUHSC_02963 | SAOUHSC_00988 | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | Glutamyl endopeptidase precursor, putative; Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobu [...] | 0.504 |
| clfB | sspB | SAOUHSC_02963 | SAOUHSC_00987 | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | Cysteine protease precursor, putative; Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin- 3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin. | 0.415 |
| fnbA | clfA | SAOUHSC_02803 | SAOUHSC_00812 | Fibronectin-binding protein precursor, putative; Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding sit [...] | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | 0.901 |
| fnbA | clfB | SAOUHSC_02803 | SAOUHSC_02963 | Fibronectin-binding protein precursor, putative; Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding sit [...] | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | 0.601 |
| fnbA | hly | SAOUHSC_02803 | SAOUHSC_01121 | Fibronectin-binding protein precursor, putative; Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding sit [...] | Alpha-hemolysin precursor; Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Inhibits host neutrophil chemotaxis to the lesion region (Probable). Heptamer oligomerization and pore formation is required for lytic activity (By similarity). Belongs to the aerolysin family. | 0.749 |
| fnbA | sspA | SAOUHSC_02803 | SAOUHSC_00988 | Fibronectin-binding protein precursor, putative; Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding sit [...] | Glutamyl endopeptidase precursor, putative; Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobu [...] | 0.502 |
| fnbA | sspB | SAOUHSC_02803 | SAOUHSC_00987 | Fibronectin-binding protein precursor, putative; Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding sit [...] | Cysteine protease precursor, putative; Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin- 3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin. | 0.482 |
| hly | clfA | SAOUHSC_01121 | SAOUHSC_00812 | Alpha-hemolysin precursor; Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Inhibits host neutrophil chemotaxis to the lesion region (Probable). Heptamer oligomerization and pore formation is required for lytic activity (By similarity). Belongs to the aerolysin family. | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | 0.753 |
| hly | clfB | SAOUHSC_01121 | SAOUHSC_02963 | Alpha-hemolysin precursor; Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Inhibits host neutrophil chemotaxis to the lesion region (Probable). Heptamer oligomerization and pore formation is required for lytic activity (By similarity). Belongs to the aerolysin family. | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | 0.613 |