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J Biol Chem, Vol. 274, Issue 34, 24316-24320, August 20, 1999
From the Department of Microbiology and Immunology, UCLA School of
Medicine, Los Angeles, California 90095
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 amino of the pentaglycine cross-bridge in
the staphylococcal peptidoglycan. We asked whether antibiotic cell wall
synthesis inhibitors interfere with the anchoring of surface proteins.
Penicillin G, a transpeptidation inhibitor, had no effect on surface
protein anchoring, whereas vancomycin and moenomycin, inhibitors of
cell wall polymerization into peptidoglycan strands, slowed the sorting
reaction. Cleavage of surface protein precursors did not require a
mature assembled cell wall and was observed in staphylococcal
protoplasts. A search for chemical inhibitors of the sorting reaction
identified methanethiosulfonates and
p-hydroxymercuribenzoic acid. Thus, sortase, the enzyme
proposed to cleave surface proteins at the LPXTG motif,
appears to be a sulfhydryl-containing enzyme that utilizes
peptidoglycan precursors but not an assembled cell wall as a substrate
for the anchoring of surface protein.
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