| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 [...] | 0.539 |
| clfA | hlb | SAOUHSC_00812 | SAOUHSC_02240 | 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 [...] | Truncated beta-hemolysin; Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Beta-hemolysin is a phospholipase C with specific activity toward sphingomyelins. Has a high specificity for sphingomyelin, hydrolyzes lysophosphatidylcholine at a much lower rate, but has no activity towards phosphatidylcholine, phosphatidylethanolamine, or phosphatidylserine; Belongs to the neutral sphingomyelinase family. | 0.474 |
| 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. | 0.618 |
| clfA | icaA | SAOUHSC_00812 | SAOUHSC_03002 | 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 [...] | Intercellular adhesion protein A, putative; N-acetylglucosaminyltransferase that catalyzes the polymerization of single monomer units of UDP-N-acetylglucosamine to produce the linear homopolymer poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also referred to as PIA), a biofilm adhesin polysaccharide. Requires IcaD for full activity (By similarity). | 0.618 |
| clfA | sarA | SAOUHSC_00812 | SAOUHSC_00620 | 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 [...] | Staphylococcal accessory regulator T, putative; Global regulator with both positive and negative effects that controls expression of several virulence factors and biofilm formation process in a cell density-dependent manner. In a strain-dependent manner plays a role in multidrug resistance mechanism. Is required for transcription of primary transcripts RNAII and RNAIII generated by agr (virulence accessory gene regulator) locus. Acts as a transcriptional activator of the genes encoding, among others, for fibronectin binding proteins (fnbA and fnbB), hemolysins (hla, hld, hlgB and hlgC) [...] | 0.458 |
| 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 [...] | 0.537 |
| clfB | hlb | SAOUHSC_02963 | SAOUHSC_02240 | 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 [...] | Truncated beta-hemolysin; Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Beta-hemolysin is a phospholipase C with specific activity toward sphingomyelins. Has a high specificity for sphingomyelin, hydrolyzes lysophosphatidylcholine at a much lower rate, but has no activity towards phosphatidylcholine, phosphatidylethanolamine, or phosphatidylserine; Belongs to the neutral sphingomyelinase family. | 0.435 |
| 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. | 0.618 |
| clfB | icaA | SAOUHSC_02963 | SAOUHSC_03002 | 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 [...] | Intercellular adhesion protein A, putative; N-acetylglucosaminyltransferase that catalyzes the polymerization of single monomer units of UDP-N-acetylglucosamine to produce the linear homopolymer poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also referred to as PIA), a biofilm adhesin polysaccharide. Requires IcaD for full activity (By similarity). | 0.618 |
| clfB | sarA | SAOUHSC_02963 | SAOUHSC_00620 | 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 [...] | Staphylococcal accessory regulator T, putative; Global regulator with both positive and negative effects that controls expression of several virulence factors and biofilm formation process in a cell density-dependent manner. In a strain-dependent manner plays a role in multidrug resistance mechanism. Is required for transcription of primary transcripts RNAII and RNAIII generated by agr (virulence accessory gene regulator) locus. Acts as a transcriptional activator of the genes encoding, among others, for fibronectin binding proteins (fnbA and fnbB), hemolysins (hla, hld, hlgB and hlgC) [...] | 0.425 |
| 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 [...] | 0.539 |
| 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 [...] | 0.537 |
| fnbA | hlb | SAOUHSC_02803 | SAOUHSC_02240 | 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 [...] | Truncated beta-hemolysin; Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Beta-hemolysin is a phospholipase C with specific activity toward sphingomyelins. Has a high specificity for sphingomyelin, hydrolyzes lysophosphatidylcholine at a much lower rate, but has no activity towards phosphatidylcholine, phosphatidylethanolamine, or phosphatidylserine; Belongs to the neutral sphingomyelinase family. | 0.498 |
| 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. | 0.618 |
| fnbA | icaA | SAOUHSC_02803 | SAOUHSC_03002 | 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 [...] | Intercellular adhesion protein A, putative; N-acetylglucosaminyltransferase that catalyzes the polymerization of single monomer units of UDP-N-acetylglucosamine to produce the linear homopolymer poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also referred to as PIA), a biofilm adhesin polysaccharide. Requires IcaD for full activity (By similarity). | 0.626 |
| fnbA | saeR | SAOUHSC_02803 | SAOUHSC_00715 | 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 [...] | Response regulator, putative; Member of the two-component regulatory system SaeR/SaeS involved in the regulation of staphylococcal virulence factors in a strain-dependent fashion. Probably functions as a transcriptional regulator via a specific DNA-binding domain, recognizing motifs near the promoter sequences of target genes. SaeR/SaeS activates the expression of exoproteins involved in adhesion and invasion of host cells, including hemolysins (Hla, Hlb), Coa, DNase, Spa and cell wall- associated proteins (Emp, Eap, FnbA). Acts probably downstream of the Agr system in the regulatory c [...] | 0.512 |
| fnbA | saeS | SAOUHSC_02803 | SAOUHSC_00714 | 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 [...] | Sensor histidine kinase SaeS, putative; Member of the two-component regulatory system SaeR/SaeS involved in the regulation of staphylococcal virulence factors in a strain-dependent fashion. Probably functions as a membrane-associated protein kinase that upon sensing the appropriate signal, autophosphorylates and in turn activates the cytosolic response regulator SaeR. SaeR/SaeS activates the expression of exoproteins involved in adhesion and invasion of host cells, including hemolysins (hla, hlb), coa, Dnase, spa and cell wall-associated proteins (emp, eap, fnbA). Acts probably downstr [...] | 0.450 |
| fnbA | sarA | SAOUHSC_02803 | SAOUHSC_00620 | 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 [...] | Staphylococcal accessory regulator T, putative; Global regulator with both positive and negative effects that controls expression of several virulence factors and biofilm formation process in a cell density-dependent manner. In a strain-dependent manner plays a role in multidrug resistance mechanism. Is required for transcription of primary transcripts RNAII and RNAIII generated by agr (virulence accessory gene regulator) locus. Acts as a transcriptional activator of the genes encoding, among others, for fibronectin binding proteins (fnbA and fnbB), hemolysins (hla, hld, hlgB and hlgC) [...] | 0.559 |
| hlb | clfA | SAOUHSC_02240 | SAOUHSC_00812 | Truncated beta-hemolysin; Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Beta-hemolysin is a phospholipase C with specific activity toward sphingomyelins. Has a high specificity for sphingomyelin, hydrolyzes lysophosphatidylcholine at a much lower rate, but has no activity towards phosphatidylcholine, phosphatidylethanolamine, or phosphatidylserine; Belongs to the neutral sphingomyelinase 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 [...] | 0.474 |
| hlb | clfB | SAOUHSC_02240 | SAOUHSC_02963 | Truncated beta-hemolysin; Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Beta-hemolysin is a phospholipase C with specific activity toward sphingomyelins. Has a high specificity for sphingomyelin, hydrolyzes lysophosphatidylcholine at a much lower rate, but has no activity towards phosphatidylcholine, phosphatidylethanolamine, or phosphatidylserine; Belongs to the neutral sphingomyelinase 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 [...] | 0.435 |
