TY - JOUR
T1 - The C-terminal domain promotes the hemorrhagic damage caused by Vibrio vulnificus metalloprotease
AU - Miyoshi, S.
AU - Kawata, K.
AU - Tomochika, K.
AU - Shinoda, Sumio
AU - Yamamoto, S.
N1 - Funding Information:
This study was supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology, Japan.
PY - 2001
Y1 - 2001
N2 - Vibrio vulnificus, an opportunistic human pathogen, produces a 45-kDa zinc metalloprotease (V. vulnificus protease; VVP) as an important virulence determinant. VVP injected intradermally into the dorsal skin causes the hemorrhagic damage through specific degradation of type IV collage in the vascular basement membrane. The N-terminal 35-kDa polypeptide (VVP-N), the catalytic domain, also evoked the hemorrhagic skin reaction within minutes. However, the hemorrhagic activity of VVP-N was one-third of that of VVP. Besides, the proteolytic activity of VVP-N toward the reconstituted basement membrane or type IV collagen was found to be about 50% of VVP. VVP-N, like VVP, was quickly inactivated by an equimolar amount of α2-macroglobulin, a broad-spectrum plasma protease inhibitor. These findings indicate that the C-terminal 10-kDa polypeptide, the substrate-binding domain mediating the effective binding to protein substrates, functions to augment the hemorrhagic reaction of VVP.
AB - Vibrio vulnificus, an opportunistic human pathogen, produces a 45-kDa zinc metalloprotease (V. vulnificus protease; VVP) as an important virulence determinant. VVP injected intradermally into the dorsal skin causes the hemorrhagic damage through specific degradation of type IV collage in the vascular basement membrane. The N-terminal 35-kDa polypeptide (VVP-N), the catalytic domain, also evoked the hemorrhagic skin reaction within minutes. However, the hemorrhagic activity of VVP-N was one-third of that of VVP. Besides, the proteolytic activity of VVP-N toward the reconstituted basement membrane or type IV collagen was found to be about 50% of VVP. VVP-N, like VVP, was quickly inactivated by an equimolar amount of α2-macroglobulin, a broad-spectrum plasma protease inhibitor. These findings indicate that the C-terminal 10-kDa polypeptide, the substrate-binding domain mediating the effective binding to protein substrates, functions to augment the hemorrhagic reaction of VVP.
KW - Functional domain
KW - Hemorrhage
KW - Protease
KW - Vibrio vulnificus
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U2 - 10.1016/S0041-0101(01)00171-4
DO - 10.1016/S0041-0101(01)00171-4
M3 - Article
C2 - 11600151
AN - SCOPUS:0034797999
VL - 39
SP - 1883
EP - 1886
JO - Toxicon
JF - Toxicon
SN - 0041-0101
IS - 12
ER -