Dec, 2001
The C-terminal domain promotes the hemorrhagic damage caused by Vibrio vulnificus metalloprotease
TOXICON
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- Volume
- 39
- Number
- 12
- First page
- 1883
- Last page
- 1886
- Language
- English
- Publishing type
- Research paper (scientific journal)
- DOI
- 10.1016/S0041-0101(01)00171-4
- Publisher
- PERGAMON-ELSEVIER SCIENCE LTD
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 alpha (2)-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. (C) 2001 Elsevier Science Ltd. All rights reserved.
- Link information
- ID information
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- DOI : 10.1016/S0041-0101(01)00171-4
- ISSN : 0041-0101
- Web of Science ID : WOS:000171790500011