TY - JOUR
T1 - Bacterial proteases as pathogenic factors, with special emphasis on vibrio proteases
AU - Shinoda, Sumio
AU - Miyoshi, Shin Ichi
AU - Wakae, Hitoshi
AU - Rahman, Monzur
AU - Tomochika, Ken Ichi
PY - 1996
Y1 - 1996
N2 - Bacterial proteases play various pathogenic roles in infection. Pathogenic species of the genus Vibrio, such as V. cholerae, V. parahaemolyticus or V. vulnificus also produce exocellular proteases, and almost of them are metalloproteases having a zinc atom. V. vulnificus is an opportunistic human pathogen causing septicemia or wound infections characterized by the formation of edema, necrotic ulcer and cellulitis on the skin. The protease produced by the vibrio (VVP) enhanced vascular permeability through activation of the Hageman factor-plasma kallikrein-kinin cascade and/or exocytotic histamine release from mast cells, and formed hemorrhagic lesions which subsequently provoke severe dermonecrosis. Thus, VVP is the most probable candidate for edema formation in the infection. Other pathogenic roles of VVP were also demonstrated. The VVP gene was cloned, and the amino acid sequence was deduced from the nucleotide sequence. The mature protein was demonstrated to be composed of 413 amino acid residues and showed 69 to 74% homology with other vibrio proteases.
AB - Bacterial proteases play various pathogenic roles in infection. Pathogenic species of the genus Vibrio, such as V. cholerae, V. parahaemolyticus or V. vulnificus also produce exocellular proteases, and almost of them are metalloproteases having a zinc atom. V. vulnificus is an opportunistic human pathogen causing septicemia or wound infections characterized by the formation of edema, necrotic ulcer and cellulitis on the skin. The protease produced by the vibrio (VVP) enhanced vascular permeability through activation of the Hageman factor-plasma kallikrein-kinin cascade and/or exocytotic histamine release from mast cells, and formed hemorrhagic lesions which subsequently provoke severe dermonecrosis. Thus, VVP is the most probable candidate for edema formation in the infection. Other pathogenic roles of VVP were also demonstrated. The VVP gene was cloned, and the amino acid sequence was deduced from the nucleotide sequence. The mature protein was demonstrated to be composed of 413 amino acid residues and showed 69 to 74% homology with other vibrio proteases.
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U2 - 10.3109/15569549609064086
DO - 10.3109/15569549609064086
M3 - Article
AN - SCOPUS:0030453064
SN - 0731-3837
VL - 15
SP - 327
EP - 339
JO - Journal of Toxicology - Toxin Reviews
JF - Journal of Toxicology - Toxin Reviews
IS - 4
ER -