Anchor Structure of Staphylococcal Surface Proteins

Surface proteins of the Gram-positive organismStaphylococcus aureus are anchored to the bacterial cell wall by a transpeptidation mechanism during which the polypeptide is cleaved between the threonine (T) and the glycine (G) of the LPXTG motif. The carboxyl of threonine is subsequently amide linked to the amino of the pentaglycyl cross-bridge within the staphylococcal peptidoglycan. Previous work examined the anchor structure of surface proteins solubilized from the peptidoglycan by treatment with lysostaphin or φ11 hydrolase and identified COOH-terminally linked triglycyl orl-Ala-d-iGln-l-Lys(Gly5)-d-Ala and MurNAc-[l-Ala-d-iGln-l-Lys(Gly5)-d-Ala](β1–4)-GlcNAc, respectively. Here, we report the anchor structure of surface proteins solubilized with N-acetylmuramidase andN-acetylmuramyl-l-alanine amidase.N-Acetylmuramidase-released surface protein was linked to MurNAc-[l-Ala-d-iGln-l-Lys(Gly5)-d-Ala](β1–4)-GlcNAc, whereas N-acetylmuramyl-l-alanine amidase treatment of the cell wall solubilized surface proteins linked tol-Ala-d-iGln-l-Lys(Gly5)-d-Ala. Most, but not all, anchor structures were cross-linked to other cell wall subunits, in which the d-alanyl at position four was amide linked to the pentaglycyl of a neighboring wall peptide.

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