Secreted proteases control autolysin-mediated biofilm growth of Staphylococcus aureus.
Secreted proteases control autolysin-mediated biofilm growth of Staphylococcus aureus.
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DOI:
10.1074/jbc.m113.502039
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发表时间:
2013-10-11
期刊:
影响因子:
--
通讯作者:
Schneewind O
中科院分区:
文献类型:
--
作者:
Chen C;Krishnan V;Macon K;Manne K;Narayana SV;Schneewind O
Background: Esp, a secreted protease of Staphylococcus epidermidis, blocks biofilm formation of Staphylococcus aureus and its ability to colonize human nares. Results: Esp cleaves autolysin, thereby preventing the release of staphylococcal DNA as biofilm matrix. Conclusion: Secreted proteases control S. aureus biofilm development and host colonization. Significance: Methods that promote autolysin degradation may also prevent S. aureus colonization of humans. Staphylococcus epidermidis, a commensal of humans, secretes Esp protease to prevent Staphylococcus aureus biofilm formation and colonization. Blocking S. aureus colonization may reduce the incidence of invasive infectious diseases; however, the mechanism whereby Esp disrupts biofilms is unknown. We show here that Esp cleaves autolysin (Atl)-derived murein hydrolases and prevents staphylococcal release of DNA, which serves as extracellular matrix in biofilms. The three-dimensional structure of Esp was revealed by x-ray crystallography and shown to be highly similar to that of S. aureus V8 (SspA). Both atl and sspA are necessary for biofilm formation, and purified SspA cleaves Atl-derived murein hydrolases. Thus, S. aureus biofilms are formed via the controlled secretion and proteolysis of autolysin, and this developmental program appears to be perturbed by the Esp protease of S. epidermidis.