node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
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 | sasG | SAOUHSC_00812 | SAOUHSC_02798 | 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 [...] | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | 0.777 |
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 | sasG | SAOUHSC_02963 | SAOUHSC_02798 | 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 [...] | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | 0.424 |
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 | sasG | SAOUHSC_02803 | SAOUHSC_02798 | 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 [...] | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | 0.731 |
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 |
hly | fnbA | SAOUHSC_01121 | SAOUHSC_02803 | 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. | 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 [...] | 0.749 |
hly | mgrA | SAOUHSC_01121 | SAOUHSC_00694 | 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. | Conserved hypothetical protein; Regulatory protein involved in autolytic activity, multidrug resistance and virulence. Controls autolysis by inactivating LytM, LytN (autolysins) and SarV (autolysis activator) and activating ArlRS, LrgAB and LytSR (autolysis inhibitors). Acts as a dual regulator for resistance to multiple drugs by inactivating NorB and tet38 and activating NorA. Positively controls the expression of virulence accessory gene regulator (agr) to promote alpha-hemolysin (hla) transcription and down-regulates staphylococcal accessory regulator (sarS), leading to repression o [...] | 0.443 |
hly | sasG | SAOUHSC_01121 | SAOUHSC_02798 | 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. | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | 0.432 |
mgrA | hly | SAOUHSC_00694 | SAOUHSC_01121 | Conserved hypothetical protein; Regulatory protein involved in autolytic activity, multidrug resistance and virulence. Controls autolysis by inactivating LytM, LytN (autolysins) and SarV (autolysis activator) and activating ArlRS, LrgAB and LytSR (autolysis inhibitors). Acts as a dual regulator for resistance to multiple drugs by inactivating NorB and tet38 and activating NorA. Positively controls the expression of virulence accessory gene regulator (agr) to promote alpha-hemolysin (hla) transcription and down-regulates staphylococcal accessory regulator (sarS), leading to repression o [...] | 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. | 0.443 |
sasG | clfA | SAOUHSC_02798 | SAOUHSC_00812 | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | 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 [...] | 0.777 |
sasG | clfB | SAOUHSC_02798 | SAOUHSC_02963 | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | 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 [...] | 0.424 |