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
Summary
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.