The hemagglutinating action of Vibrio vulnificus metalloprotease.
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.
Miyoshi
S
S
Faculty of Pharmaceutical Sciences, Okayama University, Okayama, Japan.
Kawata
K
K
Tomochika
K
K
Shinoda
S
S
D000818:Animals; D001426:Bacterial Proteins; D020134:Catalytic Domain; D004910:Erythrocyte Membrane / Q000378:metabolism; D006384:Hemagglutination; D006801:Humans; D008666:Metalloendopeptidases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D011817:Rabbits; D014733:Vibrio / Q000201:enzymology*
D001426:Bacterial Proteins; D008666:Metalloendopeptidases; C070101:vvP protein, Vibrio vulnificus