1n67

Structural highlights

Function

CLFA_STAAE 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 cell proliferative response in vitro, contributing significantly to the immunostimulatory activity of S.aureus.^{[1] [2] [3] [4]}

Evolutionary Conservation

Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Fibrinogen binding protein

References

1. ↑ Dominiecki ME, Weiss J. Antibacterial action of extracellular mammalian group IIA phospholipase A2 against grossly clumped Staphylococcus aureus. Infect Immun. 1999 May;67(5):2299-305. PMID:10225887
2. ↑ Siboo IR, Cheung AL, Bayer AS, Sullam PM. Clumping factor A mediates binding of Staphylococcus aureus to human platelets. Infect Immun. 2001 May;69(5):3120-7. PMID:11292731 doi:http://dx.doi.org/10.1128/IAI.69.5.3120-3127.2001
3. ↑ O'Brien L, Kerrigan SW, Kaw G, Hogan M, Penades J, Litt D, Fitzgerald DJ, Foster TJ, Cox D. Multiple mechanisms for the activation of human platelet aggregation by Staphylococcus aureus: roles for the clumping factors ClfA and ClfB, the serine-aspartate repeat protein SdrE and protein A. Mol Microbiol. 2002 May;44(4):1033-44. PMID:12010496
4. ↑ Palmqvist N, Patti JM, Tarkowski A, Josefsson E. Expression of staphylococcal clumping factor A impedes macrophage phagocytosis. Microbes Infect. 2004 Feb;6(2):188-95. PMID:14998517 doi:http://dx.doi.org/10.1016/j.micinf.2003.11.005