Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 1883-1886 |
| Number of pages | 4 |
| Journal | Toxicon |
| Volume | 39 |
| Issue number | 12 |
| DOIs | |
| Publication status | Published - 2001 |
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Keywords
- Functional domain
- Hemorrhage
- Protease
- Vibrio vulnificus
ASJC Scopus subject areas
- Toxicology
Cite this
The C-terminal domain promotes the hemorrhagic damage caused by Vibrio vulnificus metalloprotease. / Miyoshi, Shin-ichi; Kawata, K.; Tomochika, K.; Shinoda, S.; Yamamoto, S.
In: Toxicon, Vol. 39, No. 12, 2001, p. 1883-1886.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The C-terminal domain promotes the hemorrhagic damage caused by Vibrio vulnificus metalloprotease
AU - Miyoshi, Shin-ichi
AU - Kawata, K.
AU - Tomochika, K.
AU - Shinoda, S.
AU - Yamamoto, S.
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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UR - http://www.scopus.com/inward/citedby.url?scp=0034797999&partnerID=8YFLogxK
U2 - 10.1016/S0041-0101(01)00171-4
DO - 10.1016/S0041-0101(01)00171-4
M3 - Article
VL - 39
SP - 1883
EP - 1886
JO - Toxicon
JF - Toxicon
SN - 0041-0101
IS - 12
ER -