Secretion of virulence determinants by the general secretory pathway in gram-negative pathogens: an evolving story

Microbes Infect. 2000 Jul;2(9):1061-72. doi: 10.1016/s1286-4579(00)01260-0.


Secretion of proteins by the general secretory pathway (GSP) is a two-step process requiring the Sec translocase in the inner membrane and a separate substrate-specific secretion apparatus for translocation across the outer membrane. Gram-negative bacteria with pathogenic potential use the GSP to deliver virulence factors into the extracellular environment for interaction with the host. Well-studied examples of virulence determinants using the GSP for secretion include extracellular toxins, pili, curli, autotransporters, and crystaline S-layers. This article reviews our current understanding of the GSP and discusses examples of terminal branches of the GSP which are utilized by factors implicated in bacterial virulence.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Bacterial Outer Membrane Proteins / metabolism*
  • Bacterial Proteins*
  • Bacterial Toxins / metabolism
  • Biological Transport
  • Carrier Proteins / metabolism
  • Escherichia coli Proteins*
  • Fimbriae, Bacterial / metabolism
  • Glycoside Hydrolases / metabolism
  • Gram-Negative Bacteria / metabolism*
  • Gram-Negative Bacteria / pathogenicity
  • Membrane Transport Proteins*
  • Molecular Chaperones / metabolism
  • SEC Translocation Channels
  • SecA Proteins
  • Structure-Activity Relationship
  • Virulence


  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Bacterial Toxins
  • Carrier Proteins
  • Escherichia coli Proteins
  • Membrane Transport Proteins
  • Molecular Chaperones
  • SEC Translocation Channels
  • Glycoside Hydrolases
  • pullulanase
  • Adenosine Triphosphatases
  • SecA Proteins