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Biofilms contribute to virulence ofStaphylococcus aureus . Formation of biofilms is multifactorial, involving polysaccharide, protein, and DNA components, which are controlled by various regulators. Here we report that deletion of thersp gene resulted in an increase in biofilm formation in strain MW2, suggesting that Rsp is a repressor of biofilm formation. Using SDS-PAGE, we found that Rsp profoundly affected cell surface and secreted proteins. Thersp gene was transcribed monocistronically, and the transcripts were most abundant at the exponential growth phase. Microarray analyses revealed that Rsp represses 75 genes, including 9 genes encoding cell wall-anchored proteins, and activates 22 genes, including 5 genes encoding secreted proteases. Among these genes,fnbA ,fnbB ,sasG , andspa (which encode cell wall-anchored proteins) andsplABCD (which encode secreted proteases) have been implicated in biofilm formation. To deconvolute Rsp's contribution to biofilm formation, we analyzed deletion mutants of these genes either in the wild-type or in thersp mutant background. We found thatfnbA deletion in thersp mutant restored biofilm formation to the wild-type level, indicating that FnbA plays a major role in Rsp regulation of biofilm formation. Further studies revealed that Rsp inhibited biofilm formation at the stage of primary attachment through repressingfnbA . Rsp belongs to the AraC/XylS family of regulatory proteins. We expressed the putative Rsp DNA binding domain (RspDBD ) inEscherichia coli and showed that RspDBD was able to specifically bind to a short DNA fragment containing thefnbA promoter, suggesting that Rsp repressesfnbA expression by direct DNA binding.

Rsp Inhibits Attachment and Biofilm Formation by Repressing fnbA in Staphylococcus aureus MW2