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Published on: June 24, 2016
Late-stage polyribitol phosphate wall teichoic acid biosynthesis in Staphylococcus aureus
Timothy C Meredith1, Jonathan G Swoboda, Suzanne Walker
1Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Ave., Boston, MA 02115, USA.
Researchers revised the Staphylococcus aureus wall teichoic acid (WTA) pathway, identifying TarL as a bifunctional enzyme. They also discovered a second WTA type, K-WTA, regulated by the agr system.
Area of Science:
- Microbiology
- Biochemistry
- Cell Biology
Background:
- Wall teichoic acids (WTAs) are crucial for Staphylococcus aureus cell envelope integrity and virulence.
- The precise biosynthetic pathway for S. aureus WTA has remained largely unelucidated, with prior research assuming similarities to Bacillus subtilis pathways.
Purpose of the Study:
- To elucidate the late-stage enzymatic pathway for the predominant polyribitol phosphate (PRP) WTA in Staphylococcus aureus.
- To identify and characterize novel WTA species and their regulatory mechanisms in S. aureus.
Main Methods:
- High-resolution polyacrylamide gel electrophoresis was employed to analyze WTA from gene deletion mutants.
- Complementation studies were performed to assess enzyme function in WTA synthesis.
Main Results:
- A revised pathway for ribitol phosphate-utilizing enzymes was proposed, with TarL identified as a bifunctional enzyme catalyzing both priming and polymerization.
- A second, distinct WTA, designated K-WTA, was identified, synthesized by TarK.
- K-WTA biosynthesis was found to be repressed by the accessory gene regulator (agr) system in S. aureus NCTC8325.
Conclusions:
- The study refines our understanding of S. aureus WTA biosynthesis, highlighting the bifunctional nature of TarL and TarK.
- The discovery of K-WTA and its regulation by the agr system provides new insights into cell envelope remodeling and its impact on S. aureus pathogenesis and adhesion.
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