Purification, characterization and immunochemical properties of a novel 60-kDa protein of Vibrio anguillarum strains

Vibrio anguillarum strains expressed increased amounts of a novel 60-kDa protein when cells were grown at physiologically elevated temperatures. The relative amounts of the 60-kDa protein were unaltered by changes in osmolarity or ionic concentration of the growth medium in cells grown at optimal growth temperatures. The N-terminal amino acid sequence analysis of the V. anguillarum 60-kDa protein showed extensive (94–89%) sequence identity with the 60-kDa heat shock protein of Yersinia enterocolitica and with Serratia rubidaea GroEL protein. Monoclonal antibodies against the Y. enterocolitica chaperonin reacted with the 60-kDa protein from V. anguillarum strains, and with a temperature-induced protein of similar molecular mass in other Gram-negative pathogens of fish.