Abstract
An exocellular metalloprotease produced by Vibrio fluvialis, an enteropathogenic vibrio, was purified and characterized. The metalloprotease (V. fluvialis protease [VFP]) was found to have very similar characteristics to V. vulnificus protease, including a molecular mass of 45 kDa, sensitivity to chelating agents or competitive inhibitors for thermolysin-like metalloproteases, and the substrate specificity. The structural gene for VFP was also cloned, and its nucleotide sequence was determined. The deduced amino acid sequence confirmed that VFP was a member of the thermolysin family. VFP, like V. vulnificus protease, showed the haemagglutinating, permeability-enhancing and haemorrhagic activities in addition to the proteolytic activity toward oligopeptide, casein or elastin.
| Original language | English |
|---|---|
| Pages (from-to) | 127-134 |
| Number of pages | 8 |
| Journal | Microbial Pathogenesis |
| Volume | 33 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2002 |
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Keywords
- Haemagglutinin
- Metalloprotease
- Protease
- Thermolysin
- Vibrio fluvialis
ASJC Scopus subject areas
- Microbiology
- Infectious Diseases
Cite this
An exocellular thermolysin-like metalloprotease produced by Vibrio fluvialis : Purification, characterization, and gene cloning. / Miyoshi, Shin-ichi; Sonoda, Yuka; Wakiyama, Hiroko; Rahman, Md Monzur; Tomochika, Ken Ichi; Shinoda, Sumio; Yamamoto, Shigeo; Tobe, Kazuo.
In: Microbial Pathogenesis, Vol. 33, No. 3, 2002, p. 127-134.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - An exocellular thermolysin-like metalloprotease produced by Vibrio fluvialis
T2 - Purification, characterization, and gene cloning
AU - Miyoshi, Shin-ichi
AU - Sonoda, Yuka
AU - Wakiyama, Hiroko
AU - Rahman, Md Monzur
AU - Tomochika, Ken Ichi
AU - Shinoda, Sumio
AU - Yamamoto, Shigeo
AU - Tobe, Kazuo
PY - 2002
Y1 - 2002
N2 - An exocellular metalloprotease produced by Vibrio fluvialis, an enteropathogenic vibrio, was purified and characterized. The metalloprotease (V. fluvialis protease [VFP]) was found to have very similar characteristics to V. vulnificus protease, including a molecular mass of 45 kDa, sensitivity to chelating agents or competitive inhibitors for thermolysin-like metalloproteases, and the substrate specificity. The structural gene for VFP was also cloned, and its nucleotide sequence was determined. The deduced amino acid sequence confirmed that VFP was a member of the thermolysin family. VFP, like V. vulnificus protease, showed the haemagglutinating, permeability-enhancing and haemorrhagic activities in addition to the proteolytic activity toward oligopeptide, casein or elastin.
AB - An exocellular metalloprotease produced by Vibrio fluvialis, an enteropathogenic vibrio, was purified and characterized. The metalloprotease (V. fluvialis protease [VFP]) was found to have very similar characteristics to V. vulnificus protease, including a molecular mass of 45 kDa, sensitivity to chelating agents or competitive inhibitors for thermolysin-like metalloproteases, and the substrate specificity. The structural gene for VFP was also cloned, and its nucleotide sequence was determined. The deduced amino acid sequence confirmed that VFP was a member of the thermolysin family. VFP, like V. vulnificus protease, showed the haemagglutinating, permeability-enhancing and haemorrhagic activities in addition to the proteolytic activity toward oligopeptide, casein or elastin.
KW - Haemagglutinin
KW - Metalloprotease
KW - Protease
KW - Thermolysin
KW - Vibrio fluvialis
UR - http://www.scopus.com/inward/record.url?scp=0036384304&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036384304&partnerID=8YFLogxK
U2 - 10.1006/mpat.2002.0520
DO - 10.1006/mpat.2002.0520
M3 - Article
VL - 33
SP - 127
EP - 134
JO - Microbial Pathogenesis
JF - Microbial Pathogenesis
SN - 0882-4010
IS - 3
ER -