Molecular biology of Pasteurella multocida toxin

Curr Top Microbiol Immunol. 2012:361:73-92. doi: 10.1007/82_2012_201.

Abstract

Pasteurella multocida toxin (PMT) is the causative agent of progressive atrophic rhinitis in swine. The 146 kDa single-chain toxin harbours discrete domains important for receptor binding, internalisation and biological activity. The molecular basis of the toxin's activity is the deamidation of a specific glutamine residue in the α-subunit of heterotrimeric G proteins. This results in an inhibition of the inherent GTPase activity leading to a constitutively active phenotype of the G protein. Due to the ability of the toxin to act on various families of heterotrimeric G proteins, a large subset of signal transduction pathways is stimulated.

Publication types

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

MeSH terms

  • Animals
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Bacterial Toxins / chemistry*
  • Bacterial Toxins / genetics
  • Bacterial Toxins / metabolism
  • Glutamine / genetics
  • Glutamine / metabolism
  • Heterotrimeric GTP-Binding Proteins / chemistry
  • Heterotrimeric GTP-Binding Proteins / genetics
  • Heterotrimeric GTP-Binding Proteins / metabolism*
  • Humans
  • Models, Molecular
  • Pasteurella Infections / genetics
  • Pasteurella Infections / metabolism*
  • Pasteurella Infections / microbiology
  • Pasteurella multocida / genetics*
  • Pasteurella multocida / metabolism
  • Protein Binding
  • Protein Structure, Tertiary
  • Rhinitis, Atrophic / genetics
  • Rhinitis, Atrophic / metabolism*
  • Rhinitis, Atrophic / microbiology
  • Signal Transduction / genetics
  • Swine
  • Up-Regulation

Substances

  • Bacterial Proteins
  • Bacterial Toxins
  • Pasteurella multocida toxin
  • Glutamine
  • Heterotrimeric GTP-Binding Proteins