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Bacterial bunker blueprints: IreK-mediated, cell wall protective phosphorylation in Enterococcus faecalis

ABSTRACT: Enterococcus faecalis is a Gram-positive bacterium that is a major cause of hospital-acquired infections due to its intrinsic resistance to cell wall-active antimicrobials. One critical determinant of this resistance is the transmembrane kinase IreK, which belongs to the PASTA kinase family of bacterial signaling proteins involved with the regulation of cell wall homeostasis. IreK has enhanced activity in response to cell wall stress, but direct substrates of IreK phosphorylation leading to antimicrobial resistance are largely unknown. To better understand stress-modulated phosphorylation events contributing to virulence, wild type E. faecalis treated with cell wall-active chlorhexidine and ceftriaxone were examined via phosphoproteomics. Among the most prominent changes were increased phosphorylation of divisome components after both treatments, implicating cell division proteins in antimicrobial defense signaling. Phosphorylation mediated by IreK was then determined via similar analysis with a E. faecalis ΔireK mutant strain, revealing potential IreK substrates involved with the formation/maintenance of biofilms and within the E. faecalis two-component system, another common signal transduction pathway for antimicrobial resistance. These results reveal critical insights into the biological functions of IreK and the mechanisms of E. faecalis antimicrobial resistance.

INSTRUMENT(S): Q Exactive HF-X

ORGANISM(S): Enterococcus Faecalis (streptococcus Faecalis)

SUBMITTER: Leslie Hicks

LAB HEAD: Leslie Hicks

PROVIDER: PXD023265 | Pride | 2021-11-03

REPOSITORIES: Pride

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