MassIVE MSV000086238

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Staphylococcus aureus cell envelope controls the secretion of selective virulence factors

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Description

Staphylococcus aureus bi-component pore-forming leukocidins are secreted molecules that contribute to the pathogenesis by directly targeting and lysing immune cells. However, Leukocidin AB (LukAB) is found anchored to the bacterial cell envelope in addition to secreted into the extracellular milieu. Here, we report that the retention of LukAB to the bacteria provides S. aureus with a ready to be deployed toxin to target primary human neutrophils. On the bacteria, LukAB is distributed as discrete foci in two distinct envelope-associated compartments. Through genetic screens, we show that a membrane lipid, lysyl-phosphatidylglycerol, and lipoteichoic acids contribute to LukAB secretion. SDS is used to isolate the non-covalently surface-bound proteome and analyze it using mass spectrometry. As expected LukAB is present in the SDS susceptible compartment. Furthermore, the exploration of the non-covalently surface-bound proteome demonstrates that the secretion of IsaB, Hel, ScaH, and Geh also requires these cell envelope structures. Collectively, our study reveals the mechanism as well as the pathogenic role of a multistep secretion system for a selection of S. aureus proteins. [doi:10.25345/C5NF5S] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Methicillin-resistant Staphylococcus aureus ; non-covalently bound to cell envelope ; leukocidins ; LukAB

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Principal Investigators:
(in alphabetical order) 		Beatrix Ueberheide, NYU School of Medicine, USA
Submitting User: Trixi
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