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Analysis of the Substrate Specificity of the Staphylococcus aureus Sortase Transpeptidase SrtA†

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Johnson Research Foundation and Department of Biochemistry and Biophysics, The University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6059
Cite this: Biochemistry 2004, 43, 6, 1541–1551
Publication Date (Web):January 24, 2004
https://doi.org/10.1021/bi035920j
Copyright © 2004 American Chemical Society
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    Abstract

    The Staphylococcus aureus sortase transpeptidase SrtA isoform is responsible for the covalent attachment of virulence and colonization-associated proteins to the bacterial peptidoglycan. SrtA utilizes two substrates, undecaprenol-pyrophosphoryl-MurNAc(GlcNAc)-Ala-d-isoGlu-Lys(ε-Gly5)-d-Ala-d-Ala (branched Lipid II) and secreted proteins containing a highly conserved C-terminal LPXTG sequence. SrtA simultaneously cleaves the Thr−Gly bond of the LPXTG-containing protein and forms a new amide bond with the nucleophilic amino group of the Gly5 portion of branched Lipid II, anchoring the protein to this key intermediate that is subsequently polymerized into peptidoglycan. Here we describe the development of a general in vitro method for elucidating the substrate specificity of sortase enzymes. In addition, using immunofluorescence, cell adhesion assays, and transmission electron microscopy, we establish links between in vitro substrate specificity and in vivo function of the S. aureus sortase isoforms. Results from these studies provide strong supporting evidence of a primary role of the SrtA isoform in S. aureus adhesion and host colonization, illustrate a lack of specificity cross talk between SrtA and SrtB isoforms, and highlight the potential of SrtA as a target for the development of antivirulence chemotherapeutics against Gram-positive bacterial pathogens.

    †

     This work was generously supported by grants from the National Institutes of Health (AI46611 and GM65539), the American Cancer Society (RPG-99-312-01), the McCabe Fund, and the University of Pennsylvania Research Foundation. B.A.F. is the recipient of an NSF predoctoral fellowship.

    *

     To whom correspondence should be addressed:  Department of Biochemistry and Biophysics, The University of Pennsylvania School of Medicine, 905A Stellar-Chance Building, 422 Curie Blvd., Philadelphia, PA 19104-6059. Phone:  (215) 898-7619. Fax:  (215) 573-8052. E-mail:  [email protected].

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