Vibrio cholerae hemagglutinin/protease nicks cholera enterotoxin

Booth, Barbara A.; Boesman-Finkelstein, Mary; Finkelstein, Richard A.

doi:10.1128/iai.45.3.558-560.1984

Cited by 132 publications

(44 citation statements)

References 12 publications

(14 reference statements)

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“…Metalloproteases may also be related to virulence by activation of other extracellular toxins. This has been shown with proteases from Staphylococcus aureus and Vibrio cholerae (Drapeau 1978;Booth, Boesman-Finkelstein & Finkelstein 1984). However, activation of the lethal toxin (GCAT) is performed with the serine protease in A. salmonicida (Eggset et al 1994).…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterisation of two extracellular metalloproteases from Aeromonas salmonicida ssp. salmonicida

Arnesen

Eggset

1999

Journal of Fish Diseases

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Two extracellular metalloproteases were purified from a culture filtrate derived from Aeromonas salmonicida ssp. salmonicida. One enzyme, leucine aminopeptidase (LAP), which had a molecular mass 37 kDa, hydrolysed aminoterminal l‐leucine and l‐phenylalanine. The activity was inhibited by 1,10‐o‐phenanthroline, but not by EDTA. The addition of excess Zn2+ to an o‐phenanthroline‐inhibited enzyme restored most of its activity. The peptidase was temperature stable, and had an optimum temperature and pH of 60 °C and 8, respectively. The other enzyme, metalloprotease 3 (MP3), which had a molecular mass 20 kDa, was an endoprotease, and hydrolysed azocoll and hide powder‐azure, but not gelatine. The MP3 enzyme had an optimum temperature and pH of ≈40 °C and 7.5, respectively, and a cationic isoelectrical point.

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Section: Discussionmentioning

confidence: 99%

Isolation and characterisation of two extracellular metalloproteases from Aeromonas salmonicida ssp. salmonicida

Arnesen

Eggset

1999

Journal of Fish Diseases

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“…The HA/P of V. chokrue 01 is recognized as a virulence factor in pathogenesis of cholera [14]. It has been reported that HA/P contributes to pathogenesis by degrading several physiologically important substances of host 1193, including mucin, fibronectin and secretory IgA, and by activating the cholera enterotoxin (CT) with nicking A subunit of the toxin [20]. Recently, Finkelstein et al [14] have reported HA/P works as detachase which facilitate detaching of the V. choterue organism from host epithelial cells.…”

Section: Discussionmentioning

confidence: 99%

Vibrio cholerae O139 produces a protease which is indistinguishable from the haemagglutinin/protease of Vibrio cholerae O1 and non-O1

Naka¹,

Yamamoto²,

Albert³

et al. 1995

FEMS Immunology and Medical Microbiology

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Haemaglutinin/protease (HA/P) is one of the virulence factors of Vibrio cholerae O1 and pathogenic strains of V. cholerae non-O1. In this study, we examined protease activity of a new serogroup of Vibrio cholerae recently designated as O139 synonym Bengal. The protease activity was produced by all eight isolates of V. cholerae O139 from Bangladeshi patients. Purification and partial characterization of the protease from V. cholerae O139 demonstrated the purified protease (O139-P) was indistinguishable from that previously reported for HA/P of V. cholerae non-O1 (NAG-HA/P) and V. cholerae O1 (Vc-HA/P). These results prove that V. cholerae O139 produces a protease belonging to HA/P, and suggest that the protease is another virulence factor found in newly emerged V. cholerae O139, as in V. cholerae O1.

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“…Young and Broadbent reported the purification of three types of protease from V. cholerae O1: phenylmethylsulfonyl fluoride inhibitable type 1, metalloprotease and serine protease inhibitor resistant type II, and EDTA inhibitable type III [2]. Booth et al [3,4] reported that soluble HA/protease is a metalloenzyme that can be inhibited by a variety of chelating agents and inhibitors of zinc * Corresponding author. metalloprotease, and that it nicks cholera enterotoxin.…”

Section: Introductionmentioning

confidence: 99%

The effect on enterotoxicity of protease purified from Vibrio cholerae O1

Ichinose

1994

FEMS Microbiology Letters

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The effect on enterotoxicity of protease purified from Vibrio cholerae O1 was investigated by the inoculation of live vibrio cells into protease-treated loops of the ileal loop model. Fluid accumulation ratios in the protease-treated loops were elevated in a dose-dependent manner by challenge with live vibrio cells but not by that with toxin. An enhancement effect of protease on enterotoxicity was observed in both serotypes of V. cholerae O1 and V. cholerae non-O1. It is suggested, therefore, that the enterotoxicity was enhanced by treatment with protease when live vibrio cells were inoculated into the ileal loops of rabbits.

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Vibrio cholerae hemagglutinin/protease nicks cholera enterotoxin

Cited by 132 publications

References 12 publications

Isolation and characterisation of two extracellular metalloproteases from Aeromonas salmonicida ssp. salmonicida

Isolation and characterisation of two extracellular metalloproteases from Aeromonas salmonicida ssp. salmonicida

Vibrio cholerae O139 produces a protease which is indistinguishable from the haemagglutinin/protease of Vibrio cholerae O1 and non-O1

The effect on enterotoxicity of protease purified from Vibrio cholerae O1

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