IreK-Mediated, Cell Wall-Protective Phosphorylation in Enterococcus faecalis

• DOI: 10.1021/acs.jproteome.1c00635
• Publication Date: 2021-10-21T20:35:25Z
• Authors: Anthony A. Iannetta; Nicole E. Minton; Alexis A. Uitenbroek; Jaime L. Little; Caroline R. Stanton; Christopher J. Kr...; Leslie M. Hicks
• Keywords: Enterococcus faecalis

Enterococcus faecalis is a Gram-positive bacterium that major cause of hospital-acquired infections due, in part, to its intrinsic resistance cell wall-active antimicrobials. One critical determinant this the transmembrane kinase IreK, which belongs penicillin-binding protein and serine/threonine kinase-associated family bacterial signaling proteins involved with regulation wall homeostasis. The activity IreK enhanced response stress, but direct substrates phosphorylation, leading antimicrobial resistance, are largely unknown. To better understand stress-modulated phosphorylation events contributing wild type E. cells treated antimicrobials, chlorhexidine or ceftriaxone, were examined via phosphoproteomics. Among most prominent changes was increased divisome components after both treatments, suggesting modulates division stress. Phosphorylation mediated by then determined similar analysis ΔireK mutant strain, revealing potential peptidoglycan biosynthesis within CroS/R two-component system, another signal transduction pathway promotes resistance. These results reveal insights into biological functions IreK.