The genetics of glycosylation in Gram-negative bacteria

FEMS Microbiol Lett. 2003 Jan 28;218(2):211-22. doi: 10.1111/j.1574-6968.2003.tb11520.x.

Abstract

In recent years there has been a dramatic increase in reports of glycosylation of proteins in various Gram-negative systems including Neisseria meningitidis, Neisseria gonorrhoeae, Campylobacter jejuni, Pseudomonas aeruginosa, Escherichia coli, Caulobacter crescentus, Aeromonas caviae and Helicobacter pylori. Although this growing list contains many important pathogens (reviewed by Benz and Schmidt [Mol. Microbiol. 45 (2002) 267-276]) and the glycosylations are found on proteins important in pathogenesis such as pili, adhesins and flagella the precise role(s) of the glycosylation of these proteins remains to be determined. Furthermore, the details of the glycosylation biosynthetic process have not been determined in any of these systems. The definition of the precise role of glycosylation and the mechanism of biosynthesis will be facilitated by a detailed understanding of the genes involved.

Publication types

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

MeSH terms

  • Aeromonas / genetics
  • Aeromonas / metabolism
  • Campylobacter / genetics
  • Campylobacter / metabolism
  • Caulobacter crescentus / genetics
  • Caulobacter crescentus / metabolism
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Fimbriae Proteins / genetics
  • Fimbriae Proteins / metabolism
  • Fimbriae, Bacterial / genetics
  • Fimbriae, Bacterial / metabolism
  • Flagellin / genetics
  • Flagellin / metabolism
  • Glycosylation
  • Gram-Negative Bacteria / genetics*
  • Gram-Negative Bacteria / metabolism
  • Helicobacter pylori / genetics
  • Helicobacter pylori / metabolism
  • Models, Molecular
  • Neisseria / genetics
  • Neisseria / metabolism
  • Pseudomonas / genetics
  • Pseudomonas / metabolism

Substances

  • Flagellin
  • Fimbriae Proteins