NDLI: An extracellular oligopeptide permease may be a potential virulence factor of Vibrio harveyi

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An extracellular oligopeptide permease may be a potential virulence factor of Vibrio harveyi

Content Provider	Springer Nature Link
Author	He, Qingfang Chen, Jixiang Li, Caifeng
Copyright Year	2011
Abstract	An oligopeptide permease A (OppA) was purified from the extracellular product of Vibrio harveyi SF-1. The molecular weight of the purified protein was estimated to be 58 kDa on SDS-PAGE. The purified protein showed phospholipase C activity at the optimal values of temperature 50°C and pH 8.0. The enzymatic activity decreased when the temperature increased to 40 °C. The N-terminal sequence of the purified protein was determined as ADVPAGTKLA, which is similar to that of OppA. The OppA precursor gene was cloned from the genome of V. harveyi SF-1. The gene consisted of 1665 base pairs and encoded a 554 amino acid polypeptide, which showed a high similarity to those of the OppAs of V. harveyi and other Vibrio species. The gene was subcloned into pET-28a (+) and expressed in Escherichia coli. The expressed recombinant protein was purified by Ni-NTA metal affinity chromatography. The expressed recombinant protein showed a 58 kDa band on SDS-PAGE and exhibited phospholipase C activity with the optima of temperature 50°C and pH 8.0. The purified protein was toxic to the flounder gill cells. An OppA mutant of V. harveyi SF-1 was constructed by homologous recombination. The mutant strain was less virulent when it was intraperitoneally inoculated to zebra fish, with the LD$_{50}$ of 5.46×10$^{5}$ CFU fish$^{−1}$, compared to 3.11×10$^{4}$ CFU fish$^{−1}$ of the wild-type strain, which indicated that the OppA might play an important role in the pathogenicity of V. harveyi.
Starting Page	343
Ending Page	350
Page Count	8
File Format	PDF
ISSN	16725182
Journal	Journal of Ocean University of China
Volume Number	10
Issue Number	4
e-ISSN	19935021
Language	English
Publisher	SP Science Press
Publisher Date	2011-11-06
Publisher Place	Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Vibrio harveyi oligopeptide permease phospholipase C pathogenicity Oceanography
Content Type	Text
Resource Type	Article
Subject	Oceanography Ocean Engineering

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