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Journal of Bacteriology, April 2008, p. 3046-3056, Vol. 190, No. 8
0021-9193/08/$08.00+0     doi:10.1128/JB.01880-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Late-Stage Polyribitol Phosphate Wall Teichoic Acid Biosynthesis in Staphylococcus aureus{triangledown}

Timothy C. Meredith,1 Jonathan G. Swoboda,2 and Suzanne Walker1,2*

Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115,1 Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 021382

Received 29 November 2007/ Accepted 6 February 2008

Wall teichoic acids are cell wall polymers that maintain the integrity of the cellular envelope and contribute to the virulence of Staphylococcus aureus. Despite the central role of wall teichoic acid in S. aureus virulence, details concerning the biosynthetic pathway of the predominant wall teichoic acid polymer are lacking, and workers have relied on a presumed similarity to the putative polyribitol phosphate wall teichoic acid pathway in Bacillus subtilis. Using high-resolution polyacrylamide gel electrophoresis for analysis of wall teichoic acid extracted from gene deletion mutants, a revised assembly pathway for the late-stage ribitol phosphate-utilizing enzymes is proposed. Complementation studies show that a putative ribitol phosphate polymerase, TarL, catalyzes both the addition of the priming ribitol phosphate onto the linkage unit and the subsequent polymerization of the polyribitol chain. It is known that the putative ribitol primase, TarK, is also a bifunctional enzyme that catalyzes both ribitol phosphate priming and polymerization. TarK directs the synthesis of a second, electrophoretically distinct polyribitol-containing teichoic acid that we designate K-WTA. The biosynthesis of K-WTA in S. aureus strain NCTC8325 is repressed by the accessory gene regulator (agr) system. The demonstration of regulated wall teichoic acid biosynthesis has implications for cell envelope remodeling in relation to S. aureus adhesion and pathogenesis.


* Corresponding author. Mailing address: Department of Microbiology and Molecular Genetics, Harvard Medical School, 633 Armenise Building, 200 Longwood Ave., Boston, MA 02115. Phone: (617) 432-5488. Fax: (617) 738-7664. E-mail: suzanne_walker{at}hms.harvard.edu

{triangledown} Published ahead of print on 15 February 2008.


Journal of Bacteriology, April 2008, p. 3046-3056, Vol. 190, No. 8
0021-9193/08/$08.00+0     doi:10.1128/JB.01880-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.




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