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J Biol Chem, Vol. 275, Issue 13, 9876-9881, March 31, 2000

Anchoring of Surface Proteins to the Cell Wall of Staphylococcus aureus
SORTASE CATALYZED IN VITRO TRANSPEPTIDATION REACTION USING LPXTG PEPTIDE AND NH2-GLY3 SUBSTRATES*

Hung Ton-ThatDagger , Sarkis K. MazmanianDagger , Kym F. Faull§, and Olaf SchneewindDagger

From the Dagger  Department of Microbiology & Immunology and § The Pasarow Mass Spectrometry Laboratory, Departments of Psychiatry & Biobehavioral Sciences and Chemistry & Biochemistry, and The Neuropsychiatric Institute, UCLA School of Medicine, Los Angeles, California 90095

Staphylococcus aureus sortase anchors surface proteins to the cell wall envelope by cleaving polypeptides at the LPXTG motif. Surface proteins are linked to the peptidoglycan by an amide bond between the C-terminal carboxyl and the amino group of the pentaglycine cross-bridge. We find that purified recombinant sortase hydrolyzed peptides bearing an LPXTG motif at the peptide bond between threonine and glycine. In the presence of NH2-Gly3, sortase catalyzed exclusively a transpeptidation reaction, linking the carboxyl group of threonine to the amino group of NH2-Gly3. In the presence of amino group donors the rate of sortase mediated cleavage at the LPXTG motif was increased. Hydrolysis and transpeptidation required the sulfhydryl of cysteine 184, suggesting that sortase catalyzed the transpeptidation reaction of surface protein anchoring via the formation of a thioester acyl-enzyme intermediate.

* This work was supported by United States Public Health Service Grant AI 38897.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Microbiology & Immunology, UCLA School of Medicine, 10833 Le Conte Ave., Los Angeles, CA 90095. Tel.: 310-206-0997; Fax: 310-267-0173; E-mail: olafs@ucla.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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