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 - 2002/1/1
Y1 - 2002/1/1
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
C2 - 12220989
AN - SCOPUS:0036384304
VL - 33
SP - 127
EP - 134
JO - Microbial Pathogenesis
JF - Microbial Pathogenesis
SN - 0882-4010
IS - 3
ER -
