Ontology highlight
ABSTRACT:
SUBMITTER: Shime H
PROVIDER: S-EPMC130396 | biostudies-literature | 2002 Nov
REPOSITORIES: biostudies-literature
Shime Hiroaki H Ohnishi Takahiro T Nagao Kaori K Oka Kiyomasa K Takao Toshifumi T Horiguchi Yasuhiko Y
Infection and immunity 20021101 11
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. ...[more]