4.7 Article

The ColM Family, Polymorphic Toxins Breaching the Bacterial Cell Wall

Journal

MBIO
Volume 9, Issue 1, Pages -

Publisher

AMER SOC MICROBIOLOGY
DOI: 10.1128/mBio.02267-17

Keywords

bacteriocin; colicin M; diversifying recombination/selection; lipid II; periplasm; toxin-immunity module

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Funding

  1. FWO Vlaanderen (Fund for Scientific Research Flanders) [12M4618N]
  2. Intramural Research Program of the NIH, the National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)

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Bacteria host an arsenal of antagonism-mediating molecules to combat for ecologic space. Bacteriocins represent a pivotal group of secreted antibacterial peptides and proteins assisting in this fight, mainly eliminating relatives. Colicin M, a model for peptidoglycan-interfering bacteriocins in Gram-negative bacteria, appears to be part of a set of polymorphic toxins equipped with such a catalytic domain (ColM) targeting lipid II. Diversifying recombination has enabled parasitism of different receptors and has also given rise to hybrid bacteriocins in which ColM is associated with another toxin module. Remarkably, ColM toxins have recruited a diverse array of immunity partners, comprising cytoplasmic membrane-associated proteins with different topologies. Together, these findings suggest that different immunity mechanisms have evolved for ColM, in contrast to bacteriocins with nuclease activities.

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