Trimeric autotransporters: a distinct subfamily of autotransporter proteins

Trends Microbiol. 2005 May;13(5):199-205. doi: 10.1016/j.tim.2005.03.004.

Abstract

Autotransporter proteins are a large family of gram-negative bacterial extracellular proteins. These proteins have a characteristic arrangement of functional domains, including an N-terminal signal peptide, an internal passenger domain, and a C-terminal translocator domain. Recent studies have identified a novel subfamily of autotransporters, defined by a short trimeric C-terminal translocator domain and known as trimeric autotransporters. In this article, we review our current knowledge of the structural and functional characteristics of trimeric autotransporters, highlighting the distinctions between this subfamily and conventional autotransporters. We speculate that trimeric autotransporters evolved to enable high-affinity multivalent adhesive interactions with host surfaces and circulating host molecules to take place.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Adhesins, Bacterial / chemistry
  • Adhesins, Bacterial / genetics
  • Adhesins, Bacterial / metabolism*
  • Adhesins, Bacterial / physiology
  • Biological Transport / physiology
  • Haemophilus influenzae / genetics
  • Haemophilus influenzae / metabolism*
  • Phylogeny
  • Yersinia enterocolitica / genetics
  • Yersinia enterocolitica / metabolism*

Substances

  • Adhesins, Bacterial
  • Hia adhesin
  • YadA protein, Yersinia