Vibrio furnissii
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ABSTRACT:
PROVIDER: PRJNA40619 | ENA |
REPOSITORIES: ENA
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Project description:We recently reported the genome sequence of a free-living strain of Vibrio furnissii (NCTC 11218) harvested from an estuarine environment. V. furnissii is a widespread, free-living proteobacterium and emerging pathogen that can cause acute gastroenteritis in humans and lethal zoonoses in aquatic invertebrates, including farmed crustaceans and molluscs. Here we present the analyses to assess the potential pathogenic impact of V. furnissii. We compared the complete genome of V. furnissii with 8 other emerging and pathogenic Vibrio species. We selected and analyzed more deeply 10 genomic regions based upon unique or common features, and used 3 of these regions to construct a phylogenetic tree. Thus, we positioned V. furnissii more accurately than before and revealed a closer relationship between V. furnissii and V. cholerae than previously thought. However, V. furnissii lacks several important features normally associated with virulence in the human pathogens V. cholera and V. vulnificus. A striking feature of the V. furnissii genome is the hugely increased Super Integron, compared to the other Vibrio. Analyses of predicted genomic islands resulted in the discovery of a protein sequence that is present only in Vibrio associated with diseases in aquatic animals. We also discovered evidence of high levels horizontal gene transfer in V. furnissii. V. furnissii seems therefore to have a dynamic and fluid genome that could quickly adapt to environmental perturbation or increase its pathogenicity. Taken together, these analyses confirm the potential of V. furnissii as an emerging marine and possible human pathogen, especially in the developing, tropical, coastal regions that are most at risk from climate change.
| S-EPMC4139957 | biostudies-literature
Project description:Alginate lyases show great potential for industrial and medicinal applications, especially as an attractive biocatalyst for the production of oligosaccharides with special bioactivities. A novel alginate lyase, AlyH1, from the marine bacterium Vibrio furnissii H1, which has been newly isolated from rotten seaweed, was purified and characterized. The purified enzyme showed the specific activity of 2.40 U/mg. Its molecular mass was 35.8 kDa. The optimal temperature and pH were 40 °C and pH 7.5, respectively. AlyH1 maintained stability at neutral pH (7.0-8.0) and temperatures below 30 °C. Metal ions Na⁺, Mg2+, and K⁺ increased the activity of the enzyme. With sodium alginate as the substrate, the Km and Vmax values of AlyH1 were 2.28 mg/mL and 2.81 U/mg, respectively. AlyH1 exhibited activities towards both polyguluronate and polymannuronate, and preferentially degraded polyguluronate. Products prepared from sodium alginate by AlyH1 were displayed to be di-, tri-, and tetra-alginate oligosaccharides. A partial amino acid sequence (190 aa) of AlyH1 analysis suggested that AlyH1 was an alginate lyase of polysaccharide lyase family 7. The sequence showed less than 77% identity to the reported alginate lyases. These data demonstrated that AlyH1 could be as a novel and potential candidate in application of alginate oligosaccharides production with low polymerization degrees.
| S-EPMC5793078 | biostudies-literature
Project description:We found a new qnr gene, qnrVF1, carried by a multidrug resistance plasmid in a clinical Vibrio furnissii isolate. QnrVF1 exhibits 44.6% to 72.5% similarity in identity with other Qnr family proteins. QnrVF alleles are mainly encoded by chromosomes of V. furnissii and Vibrio fluvialis. Phylogenic analysis showed that QnrVF1 and QnrVF2 form a distinct clade in Qnr proteins. Thus, qnrVF represents a new qnr family. In addition, the qnrVF1 gene is often flanked by the mobile element ISCR1. Thus, it is likely that qnrVF1 is mobilized by ISCR1 from chromosome to plasmid in V. furnissii. IMPORTANCE Quinolones are widely used drugs. Bacteria contain a quinolone resistance gene, which mediates resistance to quinolones. Currently, seven families of Qnr proteins, QnrVC, QnrA, QnrB, QnrC, QnrD, QnrE, and QnrS, have been identified. However, it is unclear whether there are any other qnr families. In this study, we identified a new qnr family, qnrVF. We found many V. furnissii and V. fluvialis strains that possess chromosomal qnrVF alleles, suggesting that V. furnissii and V. fluvialis are the reservoirs of qnrVF. We also found that QnrVF1 confers low-level resistance to quinolones. ISCR1 may facilitate the spread of qnrVF1. The emergence and spread of qnrVF may pose a considerable threat to public health.
| S-EPMC9927268 | biostudies-literature
Project description:Vibrio furnissii in the blood is rarely reported, which may explain why clinical features of bloodstream infections with this organism have not been described. We describe a patient who developed skin lesions and V. furnissii bacteremia and was successfully treated with fluoroquinolones. V. furnissii may be a serious pathogen in patients with underlying comorbidities who are exposed to seafood.
| S-EPMC3122773 | biostudies-literature
Project description: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.
| S-EPMC2168660 | biostudies-literature
Project description:Vibrio furnissii M1 was recently reported to biosynthesize n-alkanes when grown on biopolymers, sugars, or organic acids (M. O. Park, J. Bacteriol. 187:1426-1429, 2005). In the present study, V. furnissii M1 was subjected to genomic analysis and studied biochemically. The sequence of the 16S rRNA gene and repetitive PCR showed that V. furnissii M1 was not identical to other V. furnissii strains tested, but the level of relatedness was consistent with its assignment as a V. furnissii strain. Pulsed-field gel electrophoresis showed chromosomal bands at approximately 3.2 and 1.8 Mb, similar to other Vibrio strains. Complete genomic DNA from V. furnissii M1 was sequenced with 21-fold coverage. Alkane biosynthetic and degradation genes could not be identified. Moreover, V. furnissii M1 did not produce demonstrable levels of n-alkanes in vivo or in vitro. In vivo experiments were conducted by growing V. furnissii M1 under different conditions, extracting with solvent, and analyzing extracts by gas chromatography-mass spectrometry. A highly sensitive assay was used for in vitro experiments with cell extracts and [(14)C]hexadecanol. The data are consistent with the present strain being a V. furnissii with properties similar to those previously described but lacking the alkane-producing phenotype. V. furnissii ATCC 35016, also reported to biosynthesize alkanes, was found in the present study not to produce alkanes.
| S-EPMC2168193 | biostudies-literature
Project description:Vibrio furnissii NCTC 11218 genome sequencing project
| PRJNA53247 | ENA
Project description:Vibrio furnissii CIP 102972 genome sequencing project
| PRJNA40497 | ENA