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- W3158541284 abstract "Surface proteins of Staphylococcus aureus play vital roles in bacterial physiology and pathogenesis. Recent work suggests that surface proteins are spatially regulated by a YSIRK/GXXS signal peptide that promotes cross-wall targeting at the mid-cell, though the mechanisms remain unclear. We previously showed that protein A (SpA), a YSIRK/GXXS protein and key staphylococcal virulence factor, mis-localizes in a ltaS mutant deficient in lipoteichoic acid (LTA) production. Here, we identified that SpA contains another cross-wall targeting signal, the LysM domain, which, in addition to the YSIRK/GXXS signal peptide, significantly enhances SpA cross-wall targeting. We show that LTA synthesis, but not LtaS, is required for SpA septal anchoring and cross-wall deposition. Interestingly, LTA is predominantly found at the peripheral cell membrane and is diminished at the septum of dividing staphylococcal cells, suggesting a restriction mechanism for SpA septal localization. Finally, we show that D-alanylation of LTA abolishes SpA cross-wall deposition by disrupting SpA distribution in the peptidoglycan layer without altering SpA septal anchoring. Our study reveals that multiple factors contribute to the spatial regulation and cross-wall targeting of SpA via different mechanisms, which coordinately ensures efficient incorporation of surface proteins into the growing peptidoglycan during the cell cycle." @default.
- W3158541284 created "2021-05-10" @default.
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- W3158541284 date "2021-06-14" @default.
- W3158541284 modified "2023-10-17" @default.
- W3158541284 title "Spatial regulation of protein A in <i>Staphylococcus aureus</i>" @default.
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- W3158541284 doi "https://doi.org/10.1111/mmi.14734" @default.
- W3158541284 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8403129" @default.
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- W3158541284 hasPublicationYear "2021" @default.
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