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J Biol Chem, Vol. 273, Issue 44, 29143-29149, October 30, 1998

Anchor Structure of Staphylococcal Surface Proteins
III. ROLE OF THE FemA, FemB, AND FemX FACTORS IN ANCHORING SURFACE PROTEINS TO THE BACTERIAL CELL WALL

Hung Ton-That, Harald Labischinski^§, Brigitte Berger-Bächi^¶, and Olaf Schneewind

From the  Department of Microbiology and Immunology, UCLA School of Medicine, Los Angeles, California 90095, ^§ Bayer AG, Pharma Research Antiinfectives I, D-42096 Wuppertal, Germany, and the ^¶ Institute of Medical Microbiology, University of Zürich, CH-8028 Zürich, Switzerland

Surface proteins of Staphylococcus aureus are covalently linked to the bacterial cell wall by a mechanism requiring a COOH-terminal sorting signal with a conserved LPXTG motif. Cleavage between the threonine and the glycine of the LPXTG motif liberates the carboxyl of threonine to form an amide bond with the pentaglycyl cross-bridge in the staphylococcal peptidoglycan. Here, we asked whether altered peptidoglycan cross-bridges interfere with the sorting reaction and investigated surface protein anchoring in staphylococcal fem mutants. S. aureus strains carrying mutations in the femA, femB, femAB, or the femAX genes synthesize altered cross-bridges, and each of these strains displayed decreased sorting activity. Characterization of cell wall anchor structures purified from the fem mutants revealed that surface proteins were linked to cross-bridges containing one, three, or five glycyl residues, but not to the -amino of lysyl in muropeptides without glycine. When tested in a femAB strain synthesizing cross-bridges with mono-, tri-, and pentaglycyl as well as tetraglycyl-monoseryl, surface proteins were found anchored mostly to the five-residue cross-bridges (pentaglycyl or tetraglycyl-monoseryl). Thus, although wild-type peptidoglycan appears to be the preferred substrate for the sorting reaction, altered cell wall cross-bridges can be linked to the COOH-terminal end of surface proteins.

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