Exemplar Abstract for Vibrio furnissii Brenner et al. 1984.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
Vibrio Furnissii

scholarly journals Laboratory evaluation on pathogenic potentialities of Vibrio furnissii

1993 ◽  
Vol 88 (4) ◽  
pp. 593-597 ◽  
Author(s):  
Vera Magalhães ◽  
Adauto Castello Filho ◽  
Macelo Magalhães ◽  
Tania T. Gomes
Keyword(s):  
Laboratory Evaluation ◽  
Vibrio Furnissii

scholarly journals Identification of a Vibrio furnissii Oligopeptide Permease and Characterization of Its In Vitro Hemolytic Activity

2007 ◽  
Vol 189 (22) ◽  
pp. 8215-8223 ◽  
Author(s):  
Tung-Kung Wu ◽  
Yu-Kuo Wang ◽  
Yi-Chin Chen ◽  
Jen-Min Feng ◽  
Yen-Hsi Liu ◽  
...  
Keyword(s):  
Hemolytic Activity ◽  
Wild Type Strain ◽  
Knockout Mutant ◽  
Fluorescent Substrate ◽  
Binding Function ◽  
Internal Peptide ◽  
Vibrio Furnissii ◽  
Oligopeptide Permease

ABSTRACT 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.

Genetic analysis of phosphomannomutase/phosphoglucomutase from Vibrio furnissii and characterization of its role in virulence

2003 ◽  
Vol 180 (4) ◽  
pp. 240-250 ◽  
Author(s):  
Sun-Hoi Kim ◽  
Sun-Hee Ahn ◽  
Jong-Hee Lee ◽  
Eun-Mi Lee ◽  
Nam-Hyun Kim ◽  
...  
Keyword(s):  
Genetic Analysis ◽  
Vibrio Furnissii

A case report of Vibrio furnissii bacteremia and cellulitis in a malnourished patient without an apparent site of entry

2018 ◽  
Vol 24 (1) ◽  
pp. 65-67 ◽  
Author(s):  
Takehiro Hashimoto ◽  
Saho Takaya ◽  
Satoshi Kutsuna ◽  
Kayoko Hayakawa ◽  
Daisuke Shiojiri ◽  
...  
Keyword(s):  
Case Report ◽  
Malnourished Patient ◽  
Vibrio Furnissii

Vibrio fluvialis and Vibrio furnissii isolated from a stool sample of one patient.

1984 ◽  
Vol 20 (1) ◽  
pp. 125-127 ◽  
Author(s):  
F W Hickman-Brenner ◽  
D J Brenner ◽  
A G Steigerwalt ◽  
M Schreiber ◽  
S D Holmberg ◽  
...  
Keyword(s):  
Stool Sample ◽  
Vibrio Fluvialis ◽  
Vibrio Furnissii

scholarly journals Reaction mechanism of chitobiose phosphorylase from Vibrio proteolyticus: identification of family 36 glycosyltransferase in Vibrio

2004 ◽  
Vol 377 (1) ◽  
pp. 225-232 ◽  
Author(s):  
Yuji HONDA ◽  
Motomitsu KITAOKA ◽  
Kiyoshi HAYASHI
Keyword(s):  
Reaction Mechanism ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Substrate Inhibition ◽  
Acceptor Substrate ◽  
Vibrio Proteolyticus ◽  
Cellobiose Phosphorylase ◽  
Synthetic Reaction ◽  
Vibrio Furnissii ◽  
High Degree

A family 36 glycosyltransferase gene was cloned from Vibrio proteolyticus. The deduced amino acid sequence showed a high degree of identity with ChBP (chitobiose phosphorylase) from another species, Vibrio furnissii. The recombinant enzyme catalysed the reversible phosphorolysis of (GlcNAc)2 (chitobiose) to form 2-acetamide-2-deoxy-α-d-glucose 1-phosphate [GlcNAc-1-P] and GlcNAc, but showed no activity on cellobiose, indicating that the enzyme was ChBP, not cellobiose phosphorylase. In the synthetic reaction, the ChBP was active with α-d-glucose 1-phosphate as the donor substrate as well as GlcNAc-1-P to produce β-d-glucosyl-(1→4)-2-acetamide-2-deoxy-d-glucose with GlcNAc as the acceptor substrate. The enzyme allowed aryl-β-glycosides of GlcNAc as the acceptor substrate with 10–20% activities of GlcNAc. Kinetic parameters of (GlcNAc)2 in the phosphorolysis and GlcNAc-1-P in the synthetic reaction were determined as follows: phosphorolysis, k0=5.5 s−1, Km=2.0 mM; synthetic reaction, k0=10 s−1, Km=14 mM, respectively. The mechanism of the phosphorolytic reaction followed a sequential Bi Bi mechanism, as frequently observed with cellobiose phosphorylases. Substrate inhibition by GlcNAc was observed in the synthetic reaction. The enzyme was considered a unique biocatalyst for glycosidation.

Sign in / Sign up

Export Citation Format

Share Document