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Infection and Immunity, November 2002, p. 6460-6463, Vol. 70, No. 11
0019-9567/02/$04.00+0 DOI: 10.1128/IAI.70.11.6460-6463.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
Department of Bacterial Toxinology, Research Institute for Microbial Diseases,1 Research Center for Structural and Functional Proteomics, Institute for Protein Research, Osaka University, Suita, Osaka 565-0871,3 Division of Microbiology, National Institute of Health Sciences, Setagaya, Tokyo 158-8501, Japan2
Received 14 May 2002/ Returned for modification 10 July 2002/ Accepted 29 July 2002
To help understand the molecular mechanisms of Pasteurella multocida toxin (PMT) action, we searched for a cellular protein interacting with PMT. The ligand overlay assay revealed a 60-kDa cellular protein that binds to a region from the 840th to 985th amino acids of the toxin. This protein was identified as vimentin by peptide mass fingerprinting. The N-terminal head domain of vimentin was further found to be responsible for the binding to the toxin.
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