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The Hemagglutinating Action of Vibrio vulnificus Metalloprotease

1999; Wiley; Volume: 43; Issue: 1 Linguagem: Inglês

10.1111/j.1348-0421.1999.tb02376.x

1348-0421

Shin‐ichi Miyoshi, Koji Kawata, Ken‐ichi Tomochika, Sumió Shinoda,

Vibrio bacteria research studies

Vibrio vulnificus protease (VVP), a 45-kDa zinc metalloprotease, consists of two functional domains: an N-terminal 35-kDa polypeptide having endoproteinase activity, and a C-terminal 10-kDa polypeptide that mediates the binding of VVP to the erythrocyte membrane. Therefore, VVP, but not its N-terminal endoproteinase domain alone, has agglutinating activity to rabbit erythrocytes. When a single zinc atom in the catalytic center was substituted by treatment with CuCl2 or NiCl2, proteolytic and hemagglutinating activities were reduced by Ni substitution but not by Cu substitution. Cu-treated 35-kDa polypeptide showed sufficient affinity of the catalytic center and weak binding ability to the erythrocyte membrane, but the Ni-treated polypeptide did not. These results suggest that the binding of endoproteinase domain to membrane is also necessary for hemagglutination.