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The Hemagglutinating Action of Vibrio vulnificus Metalloprotease
Author(s) -
Miyoshi Shinichi,
Kawata Koji,
Tomochika Kenichi,
Shinoda Sumio
Publication year - 1999
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1999.tb02376.x
Subject(s) - metalloproteinase , vibrio vulnificus , protease , biology , biochemistry , hemagglutination , zinc , enzyme , bacteria , chemistry , virus , virology , genetics , organic chemistry
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 CuCl 2 or NiCl 2 , 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.