Identification and characterization of a zinc metalloprotease associated with invasion by the fish pathogen Vibrio anguillarum.

摘要: An invasiveness-defective mutant of the fish-pathogenic bacterium Vibrio anguillarum was isolated. Compared with wild type, this had a 1,000-fold higher 50% lethal dose after immersion infection rainbow trout, Oncorhynchus mykiss, while intraperitoneal infection, only 10-fold dose. In addition, showed lower level protease activity. Two forms (Pa and Pb) were found sodium dodecyl sulfate-polyacrylamide gel electrophoresis nonheated samples. Pa predominantly in preparations Pb predominant form mutant. Conversion to observed incubation at 4 degrees C. Characterization that it an elastolytic enzyme which required Zn2+ for activity Ca2+ stability. The molecular mass 36 kilodaltons. N-terminal amino acid sequence analysis V. revealed homology elastase Pseudomonas aeruginosa Legionella pneumophila.