.gif?ad=15653&adview=true)
Staphylococcus aureus sortase mutants defective in the display of surface proteins and in the pathogenesis of animal infections
- *Department of Microbiology and Immunology, University of California, Los Angeles, School of Medicine, 10833 Le Conte Avenue, Los Angeles, CA 90095; and †Department of Infectious Disease Research, Wyeth–Ayerst Research, 401 North Middletown Road, Pearl River, NY 10965
-
Edited by John J. Mekalanos, Harvard Medical School, Boston, MA, and approved February 24, 2000 (received for review December 1, 1999)
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.
Footnotes
-
↵ ‡ To whom reprint requests should be addressed. E-mail: olafs{at}ucla.edu.
-
This paper was submitted directly (Track II) to the PNAS office.
-
Article published online before print: Proc. Natl. Acad. Sci. USA, 10.1073/pnas.080520697.
-
Article and publication date are at www.pnas.org/cgi/doi/10.1073/pnas.080520697
- Abbreviations:
- Clf,
- clumping factor;
- Fnb,
- fibronectin-binding protein;
- Seb,
- staphylococcal enterotoxin B;
- Spa,
- staphylococcal protein A;
- SrtA,
- staphylococcal surface protein sorting A;
- TCA,
- trichloroacetic acid;
- cfu,
- colony-forming unit
- Copyright © The National Academy of Sciences
