Structural insights into bacterial recognition of intestinal mucins

Curr Opin Struct Biol. 2014 Oct:28:23-31. doi: 10.1016/j.sbi.2014.07.002. Epub 2014 Aug 6.

Abstract

The mucosal layer covering our gut epithelium represents the first line of host defenses against the luminal content, while enabling contacts between the resident microbiota and the host. Mucus is mainly composed of mucins, large glycoproteins containing a protein core and a high number of O-linked oligosaccharides. Mucin glycans act as binding sites or carbon sources for the intestinal microbes, thereby functioning as a host-specific determinant affecting the microbiota composition and human health. Reflecting the structural diversity of mucin glycans and their prime location, commensal and pathogenic microbes have evolved a range of adhesins allowing their interaction with the host. However, despite the recognised importance of mucin glycans in modulating intestinal homeostasis, information on carbohydrate-binding proteins from gut bacteria is disparate. This review is focussed on recent structural insights into host-microbe interactions mediated by mucins.

Publication types

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

MeSH terms

  • Animals
  • Bacteria / chemistry*
  • Bacteria / metabolism
  • Binding Sites
  • Carbohydrate Metabolism
  • Carbohydrates / chemistry
  • Humans
  • Intestinal Mucosa / metabolism
  • Intestines / microbiology
  • Models, Molecular
  • Molecular Conformation
  • Mucins / chemistry*
  • Mucins / metabolism
  • Mucous Membrane / metabolism
  • Mucous Membrane / microbiology
  • Mucus / chemistry
  • Mucus / metabolism
  • Mucus / microbiology
  • Protein Binding
  • Substrate Specificity

Substances

  • Carbohydrates
  • Mucins