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• W2046191483 startingPage "16241" @default.
• W2046191483 abstract "Surface proteins of <i>Staphylococcus aureus</i> are anchored to the cell wall peptidoglycan by a mechanism requiring a C-terminal sorting signal with an LP<i>X</i>TG motif. Surface proteins are first synthesized in the bacterial cytoplasm and then transported across the cytoplasmic membrane. Cleavage of the N-terminal signal peptide of the cytoplasmic surface protein P1 precursor generates the extracellular P2 species, which is the substrate for the cell wall anchoring reaction. Sortase, a membrane-anchored transpeptidase, cleaves P2 between the threonine (T) and the glycine (G) of the LP<i>X</i>TG motif and catalyzes the formation of an amide bond between the carboxyl group of threonine and the amino group of cell wall cross-bridges. We have used metabolic labeling of staphylococcal cultures with [³²P]phosphoric acid to reveal a P3 intermediate. The ³²P-label of immunoprecipitated surface protein is removed by treatment with lysostaphin, a glycyl-glycine endopeptidase that separates the cell wall anchor structure. Furthermore, the appearance of P3 is prevented in the absence of sortase or by the inhibition of cell wall synthesis.³²P-Labeled cell wall anchor species bind to nisin, an antibiotic that is known to form a complex with lipid II. Thus, it appears that the P3 intermediate represents surface protein linked to the lipid II peptidoglycan precursor. The data support a model whereby lipid II-linked polypeptides are incorporated into the growing peptidoglycan via the transpeptidation and transglycosylation reactions of cell wall synthesis, generating mature cell wall-linked surface protein." @default.
• W2046191483 created "2016-06-24" @default.
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• W2046191483 date "2002-05-01" @default.
• W2046191483 modified "2023-10-16" @default.
• W2046191483 title "Anchoring of Surface Proteins to the Cell Wall of Staphylococcus aureus" @default.
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• W2046191483 doi "https://doi.org/10.1074/jbc.m109194200" @default.
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