Vibrio cholerae amino acids go on the defense

J Biol Chem. 2017 Dec 22;292(51):21216-21217. doi: 10.1074/jbc.H117.000868.

Abstract

Gram-negative bacteria remodel their surfaces to interact with the environment, particularly to protect pathogens from immune surveillance and host defenses. The enzyme AlmG is known to be involved in remodeling the Vibrio cholerae surface, but its specific role was not clear. A new study characterizes AlmG at the molecular level, showing it defies phylogenetic expectations to add amino acids to lipopolysaccharide (LPS). This LPS modification plays a pivotal role in V. cholerae resistance to antimicrobial peptides, weapons of the innate immune system against infections.

Keywords: Vibrio cholera; aminoacylation; antimicrobial peptide (AMP); lipid A; lipopolysaccharide (LPS); polymyxin B; synthetic biology.

Publication types

  • Research Support, Non-U.S. Gov't
  • Comment

MeSH terms

  • Acyltransferases / genetics
  • Amino Acids
  • Bacterial Proteins / genetics
  • Lipid A
  • Pandemics
  • Phylogeny
  • Polymyxins
  • Vibrio cholerae*

Substances

  • Amino Acids
  • Bacterial Proteins
  • Lipid A
  • Polymyxins
  • Acyltransferases