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The Staphylococcus aureus esterase FmtA is essential for wall teichoic acid D-alanylation
Kirsten A Berry1, Mackenzie T A Verhoef1, Zhiyong Zheng2
1Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario, Canada.
Staphylococcus aureus wall teichoic acid (WTA) D-alanylation is essential for pathogen survival. We found the enzyme FmtA is critical for this process, with lipoteichoic acid (LTA) likely supplying D-alanine for WTA modification.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- * Staphylococcus aureus teichoic acids, including wall teichoic acids (WTAs) and lipoteichoic acids (LTAs), are crucial anionic glycopolymers.
- * Post-synthetic D-alanine (D-Ala) addition to these polymers regulates surface charge and pathogen survival.
- * Mechanisms controlling WTA D-alanylation are not fully understood, representing a significant knowledge gap.
Purpose of the Study:
- * To investigate the role of FmtA in the D-alanylation of Staphylococcus aureus teichoic acids.
- * To elucidate the relationship between LTA and WTA D-alanylation.
- * To understand how FmtA impacts bacterial surface properties and host interactions.
Main Methods:
- * Genetic inactivation of the fmtA gene in Staphylococcus aureus.
- * Analysis of D-Ala modification levels in WTA and LTA from wild-type and mutant strains.
- * Assessment of bacterial surface charge, adhesion, biofilm formation, and cell aggregation.
Main Results:
- * Inactivation of fmtA resulted in significantly reduced D-alanylation of WTA, while LTA D-alanylation remained normal.
- * fmtA mutants exhibited a more negative surface charge, decreased host cell adhesion, impaired biofilm formation, and altered cell aggregation.
- * These findings suggest LTA serves as the D-Ala donor for WTA modification, mediated by FmtA.
Conclusions:
- * FmtA is essential for the D-alanylation of wall teichoic acids in Staphylococcus aureus.
- * Lipoteichoic acid likely provides the D-alanine for WTA modification, a process dependent on FmtA.
- * Further research is needed to identify the acyltransferase responsible for incorporating D-Ala into WTA.
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