Recent insights into Pasteurella multocida toxin and other G-protein-modulating bacterial toxins

Brenda A. Wilson, Mengfei Ho

Research output: Contribution to journalReview article


Over the past few decades, our understanding of the bacterial protein toxins that modulate G proteins has advanced tremendously through extensive biochemical and structural analyses. This article provides an updated survey of the various toxins that target G proteins, ending with a focus on recent mechanistic insights in our understanding of the deamidating toxin family. The dermonecrotic toxin from Pasteurella multocida (PMT) was recently added to the list of toxins that disrupt G-protein signal transduction through selective deamidation of their targets. The C3 deamidase domain of PMT has no sequence similarity to the deamidase domains of the dermonecrotic toxins from Escherichia coli (cytotoxic necrotizing factor [CNF]1-3), Yersinia (CNFY) and Bordetella (dermonecrotic toxin). The structure of PMT-C3 belongs to a family of transglutaminase-like proteins, with active site Cys-His-Asp catalytic triads distinct from E. coli CNF1.

Original languageEnglish (US)
Pages (from-to)1185-1201
Number of pages17
JournalFuture Microbiology
Issue number8
StatePublished - Aug 1 2010



  • GTPase
  • Pasteurella multocida toxin
  • cysteine protease
  • cytotoxic necrotizing factor
  • deamidation
  • dermonecrotic toxin
  • heterotrimeric G proteins
  • signal transduction
  • transglutamination

ASJC Scopus subject areas

  • Microbiology
  • Microbiology (medical)

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