標題: Identification of a Vibtio furnissii oligopeptide permease and characterization of its in vitro hemolytic activity
作者: Wu, Tung-Kung
Wang, Yu-Kuo
Chen, Yi-Chin
Feng, Jen-Min
Liu, Yen-Hsi
Wang, Ting-Yi
生物科技學系
Department of Biological Science and Technology
公開日期: 1-Nov-2007
摘要: We describe purification and characterization of an oligopeptide permease protein (Hly-OppA) from Vibrio furnissii that has multifaceted functions in solute binding, in in vitro hemolysis, in antibiotic resistance, and as a virulence factor in bacterial pathogenesis. The solute-binding function was revealed by N-terminal and internal peptide sequences of the purified protein and was confirmed by discernible effects on oligopeptide binding, by accumulation of fluorescent substrates, and by fluorescent substrate-antibiotic competition assay experiments. The purified protein exhibited host-specific in vitro hemolytic activity against various mammalian erythrocytes and apparent cytotoxicity in CHO-K1 cells. Recombinant Hly-OppA protein and an anti-Hly-OppA monoclonal antibody exhibited and neutralized the in vitro hemolytic activity, respectively, which further confirmed the hemolytic activity of the gene product. In addition, a V. furnissii hly-oppA knockout mutant caused less mortality than the wild-type strain when it was inoculated into BALB/c mice, indicating the virulence function of this protein. Finally, the in vitro hemolytic activity was also confirmed with homologous ATP-binding cassette-type transporter proteins from other Vibrio species.
URI: http://dx.doi.org/10.1128/JB.01039-07
http://hdl.handle.net/11536/10186
ISSN: 0021-9193
DOI: 10.1128/JB.01039-07
期刊: JOURNAL OF BACTERIOLOGY
Volume: 189
Issue: 22
起始頁: 8215
結束頁: 8223
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