| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| aur | clfA | SAXN108_2908 | SAXN108_0856 | annotation not available | Clumping factor A; 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 [...] | 0.647 |
| aur | ebpS | SAXN108_2908 | SAXN108_1502 | annotation not available | Elastin-binding protein EbpS; Promotes binding of soluble elastin peptides and tropoelastin to S.aureus cells although it is not able to promote bacterial adherence to immobilized elastin and, therefore, is not a microbial surface component recognizing adhesive matrix molecule (MSCRAMM). May be involved in sensing the environment or in nutrient transport, since its loss caused a growth defect | 0.598 |
| aur | fnbA | SAXN108_2908 | SAXN108_2750 | annotation not available | Fibronectin-binding protein A; 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 site localized within [...] | 0.731 |
| aur | hysA | SAXN108_2908 | SAXN108_2455 | annotation not available | annotation not available | 0.631 |
| aur | sak | SAXN108_2908 | SAXN108_2047 | annotation not available | annotation not available | 0.732 |
| aur | splA | SAXN108_2908 | SAXN108_1846 | annotation not available | annotation not available | 0.816 |
| aur | splE | SAXN108_2908 | SAXN108_1842 | annotation not available | annotation not available | 0.786 |
| aur | sspA | SAXN108_2908 | SAXN108_1046 | annotation not available | Glutamyl endopeptidase; 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 immunoglobulin classes IgG, Ig [...] | 0.914 |
| clfA | aur | SAXN108_0856 | SAXN108_2908 | Clumping factor A; 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 [...] | annotation not available | 0.647 |
| clfA | ebpS | SAXN108_0856 | SAXN108_1502 | Clumping factor A; 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 [...] | Elastin-binding protein EbpS; Promotes binding of soluble elastin peptides and tropoelastin to S.aureus cells although it is not able to promote bacterial adherence to immobilized elastin and, therefore, is not a microbial surface component recognizing adhesive matrix molecule (MSCRAMM). May be involved in sensing the environment or in nutrient transport, since its loss caused a growth defect | 0.875 |
| clfA | fnbA | SAXN108_0856 | SAXN108_2750 | Clumping factor A; 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 [...] | Fibronectin-binding protein A; 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 site localized within [...] | 0.471 |
| clfA | hysA | SAXN108_0856 | SAXN108_2455 | Clumping factor A; 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 [...] | annotation not available | 0.576 |
| clfA | katA | SAXN108_0856 | SAXN108_1351 | Clumping factor A; 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 [...] | Catalase; Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. Involved in resistance to paraquat when fur is absent and to tert-butyl hydroperoxide. Is important for survival under glucose starvation and desiccation conditions. Not required for virulence although is necessary for nasal colonization | 0.576 |
| clfA | sak | SAXN108_0856 | SAXN108_2047 | Clumping factor A; 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 [...] | annotation not available | 0.803 |
| clfA | sdrD | SAXN108_0856 | SAXN108_0618 | Clumping factor A; 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 [...] | Serine-aspartate repeat-containing protein D; Cell surface-associated calcium-binding protein which possibly mediates interactions of S.aureus with components of the extracellular matrix of higher eukaryotes. Binds 14-15 calcium ions (By similarity) | 0.528 |
| clfA | splA | SAXN108_0856 | SAXN108_1846 | Clumping factor A; 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 [...] | annotation not available | 0.520 |
| clfA | sspA | SAXN108_0856 | SAXN108_1046 | Clumping factor A; 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 [...] | Glutamyl endopeptidase; 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 immunoglobulin classes IgG, Ig [...] | 0.732 |
| ebpS | aur | SAXN108_1502 | SAXN108_2908 | Elastin-binding protein EbpS; Promotes binding of soluble elastin peptides and tropoelastin to S.aureus cells although it is not able to promote bacterial adherence to immobilized elastin and, therefore, is not a microbial surface component recognizing adhesive matrix molecule (MSCRAMM). May be involved in sensing the environment or in nutrient transport, since its loss caused a growth defect | annotation not available | 0.598 |
| ebpS | clfA | SAXN108_1502 | SAXN108_0856 | Elastin-binding protein EbpS; Promotes binding of soluble elastin peptides and tropoelastin to S.aureus cells although it is not able to promote bacterial adherence to immobilized elastin and, therefore, is not a microbial surface component recognizing adhesive matrix molecule (MSCRAMM). May be involved in sensing the environment or in nutrient transport, since its loss caused a growth defect | Clumping factor A; 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 [...] | 0.875 |
| ebpS | fnbA | SAXN108_1502 | SAXN108_2750 | Elastin-binding protein EbpS; Promotes binding of soluble elastin peptides and tropoelastin to S.aureus cells although it is not able to promote bacterial adherence to immobilized elastin and, therefore, is not a microbial surface component recognizing adhesive matrix molecule (MSCRAMM). May be involved in sensing the environment or in nutrient transport, since its loss caused a growth defect | Fibronectin-binding protein A; 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 site localized within [...] | 0.890 |
