Staphylococcus aureus sortase mutants defective in the display of surface proteins and in the pathogenesis of animal infections

Creators: Mazmanian, Sarkis K.; Liu, Gwen; Jensen, Eric R.; Lenoy, Eileen; Schneewind, Olaf

Abstract

Many Gram-positive bacteria covalently tether their surface adhesins to the cell wall peptidoglycan. We find that surface proteins of Staphylococcus aureus are linked to the cell wall by sortase, an enzyme that cleaves polypeptides at a conserved LPXTG motif. S. aureus mutants lacking sortase fail to process and display surface proteins and are defective in the establishment of infections. Thus, the cell wall envelope of Gram-positive bacteria represents a surface organelle responsible for interactions with the host environment during the pathogenesis of bacterial infections.

Additional Information

Copyright © 2000 by the National Academy of Sciences Edited by John J. Mekalanos, Harvard Medical School, Boston, MA, and approved February 24, 2000 (received for review December 1, 1999). Published online before print April 18, 2000, 10.1073/pnas.080520697 We thank C. Draper, T. Foster, J. Lee, and W. Navarre for materials. S.K.M. is supported by the Predoctoral Training Program in Genetics (T32GM07104) and E.R.J. by the Tumor Immunology Training Grant (T32CA009120). Work in the laboratory of O.S. is supported by Grant AI33987 from the National Institute of Allergy and Infectious Diseases, Infectious Disease Branch. This paper was submitted directly (Track II) to the PNAS office. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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