Related Experiment Videos

Association of Pasteurella multocida toxin with vimentin

Hiroaki Shime1, Takahiro Ohnishi, Kaori Nagao

  • 1Department of Bacterial Toxinology, Research Institute for Microbial Diseases. Research Center for Structural and Functional Proteomics, Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.

Infection and Immunity
|October 16, 2002
PubMed

Insights

Researchers identified vimentin as a cellular protein that interacts with Pasteurella multocida toxin (PMT). The N-terminal head domain of vimentin binds to a specific region of the PMT, clarifying toxin-host interactions.

Area of Science:

  • Molecular biology
  • Cellular biology
  • Microbiology

Background:

  • Pasteurella multocida toxin (PMT) is a virulence factor involved in various diseases.
  • The precise molecular mechanisms of PMT action remain incompletely understood.
  • Identifying host cell targets of PMT is crucial for understanding its pathogenesis.

Purpose of the Study:

  • To identify cellular proteins that interact with Pasteurella multocida toxin (PMT).
  • To elucidate the specific region of PMT involved in host cell protein binding.
  • To determine the domain of the interacting host protein responsible for binding.

Main Methods:

  • Ligand overlay assay to detect protein-protein interactions.
  • Peptide mass fingerprinting for protein identification.
  • Analysis of protein domains to map binding sites.

Main Results:

  • A 60-kDa cellular protein was found to bind to PMT.
  • The interacting protein was identified as vimentin.
  • Vimentin binds to amino acids 840-985 of PMT.
  • The N-terminal head domain of vimentin mediates the interaction with PMT.

Conclusions:

  • Vimentin is a cellular binding partner of Pasteurella multocida toxin.
  • The interaction involves a specific region of PMT and the N-terminal domain of vimentin.
  • This finding provides insights into the molecular mechanisms of PMT pathogenesis.

Related Concept Videos