Vibrio Cholerae Soluble Hemagglutinin/protease is a Metalloenzyme

Overview

Journal Infect Immun

Publisher American Society for Microbiology

Specialty Allergy & Immunology

Date 1983 Nov 1

PMID 6417020

Citations 35

Authors

B A BOOTH

R A Finkelstein

Affiliations

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Abstract

A soluble hemagglutinin/protease produced by Vibrio cholerae, which has previously been shown to hydrolyze fibronectin and ovomucin and to cleave lactoferrin and the A subunit of the heat-labile enterotoxin of Escherichia coli, appears to be a zinc metalloendopeptidase. Both its hemagglutinative and protease functions are inhibited by chelating agents, including Zincov, a hydroxamic acid derivative specifically designed to inhibit zinc metalloproteases. Thermolysin, a known zinc-containing protease, also causes hemagglutination of responder chicken erythrocytes. This activity is inhibited by Zincov, which does not affect the hemagglutination activity of trypsin and pronase. The hemagglutinin/protease is active on furylacryloyl-Gly-Leu-NH2, a synthetic substrate for thermolysin and other similar proteases. The hemagglutination activity of V. cholerae-infected or cholera toxin-treated infant rabbit intestinal fluid is not inhibited by Zincov, which suggests that this activity is not due to the hemagglutinin/protease, as formerly proposed.

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