SEDS glycosyltransferases in <i>E. faecalis</i> are upregulated by the CroS/R two-component system to enhance peptidoglycan synthesis during cell wall stress.

ABSTRACT: Enterococci are commensals of the intestinal tract that are intrinsically resistant to cephalosporins, antibiotics that inhibit peptidoglycan synthesis. Prior treatment with cephalosporins is a risk factor for acquiring an enterococcal infection. We previously showed that FtsW, a SEDS (shape, elongation, division, and sporulation) protein, is essential for enterococcal cephalosporin resistance. SEDS proteins catalyze glycosyltransferase reactions to polymerize strands of peptidoglycan. Bacterial genomes typically only encode for two SEDS proteins, FtsW and RodA, that form the core of two different peptidoglycan synthases thought to function at distinct locations in the cell. However, a few bacterial genera, including enterococci, encode homologs of not only FtsW

SUBMITTER: Nelson ME 

PROVIDER: S-EPMC12724132 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature