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.
Mutharia
L M
LM
Department of Microbiology, University of Guelph, Ont., Canada. lmuthari@micro.uoguelph.ca
Klinck
J
J
Yamaguchi
H
H
Davey
M
M
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000942:Antigens, Bacterial / Q000276:immunology; D001426:Bacterial Proteins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D005393:Fish Diseases / Q000382:microbiology*; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D013696:Temperature; D014733:Vibrio / Q000254:growth & development / Q000302:isolation & purification* / Q000378:metabolism*; D014735:Vibrio Infections / Q000382:microbiology*
D000911:Antibodies, Monoclonal; D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D006360:Heat-Shock Proteins