The cell envelope of Staphylococcus aureus selectively controls the sorting of virulence factors

Cell envelope Lipoteichoic acid
DOI: 10.1038/s41467-021-26517-z Publication Date: 2021-10-26T10:03:16Z
ABSTRACT
Abstract Staphylococcus aureus bi-component pore-forming leukocidins are secreted toxins that directly target and lyse immune cells. Intriguingly, one of the leukocidins, Leukocidin AB (LukAB), is found associated with bacterial cell envelope in addition to into extracellular milieu. Here, we report retention LukAB on cells provides S. a pre-synthesized active toxin kills On bacteria, distributed as discrete foci two distinct compartments: membrane-proximal surface-exposed. Through genetic screens, show membrane lipid, lysyl-phosphatidylglycerol (LPG), lipoteichoic acid (LTA) contribute deposition release. Furthermore, by studying non-covalently surface-bound proteins discovered sorting additional exoproteins, such IsaB, Hel, ScaH, Geh, also controlled LPG LTA. Collectively, our study reveals multistep secretion system controls exoprotein storage protein translocation across wall.
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