The hemagglutinating action of Vibrio vulnificus metalloprotease

Shin Ichi Miyoshi, Koji Kawata, Ken Ichi Tomochika, Sumio Shinoda

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)79-82
Number of pages4
Issue number1
Publication statusPublished - Jan 1 1999


  • Protease
  • Vibrio vulnificus

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Virology


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