scholarly journals Beyond Cholera: Characterization of zot-Encoding Filamentous Phages in the Marine Fish Pathogen Vibrio anguillarum

Viruses ◽  
2020 ◽  
Vol 12 (7) ◽  
pp. 730 ◽  
Author(s):  
Jesper Juel Mauritzen ◽  
Daniel Castillo ◽  
Demeng Tan ◽  
Sine Lo Svenningsen ◽  
Mathias Middelboe
Keyword(s):  
Vibrio Anguillarum ◽  
Amino Acid Identity ◽  
Exponential Growth Phase ◽  
Fish Pathogen ◽  
Zonula Occludens ◽  
Infection Dynamics ◽  
Putative Toxin ◽  
Pathogenic Vibrios ◽  
Zonula Occludens Toxin

Zonula occludens toxin (Zot) is a conserved protein in filamentous vibriophages and has been reported as a putative toxin in Vibrio cholerae. Recently, widespread distribution of zot-encoding prophages was found among marine Vibrio species, including environmental isolates. However, little is known about the dynamics of these prophages beyond V. cholerae. In this study, we characterized and quantified the zot-encoding filamentous phage VAIϕ, spontaneously induced from the fish pathogen V. anguillarum. VAIϕ contained 6117 bp encoding 11 ORFs, including ORF8pVAI, exhibiting 27%–73% amino acid identity to Inovirus Zot-like proteins. A qPCR method revealed an average of four VAIϕ genomes per host genome during host exponential growth phase, and PCR demonstrated dissemination of induced VAIϕ to other V. anguillarum strains through re-integration in non-lysogens. VAIϕ integrated into both chromosomes of V. anguillarum by recombination, causing changes in a putative ORF in the phage genome. Phylogenetic analysis of the V. anguillarum Inoviridae elements revealed mosaic genome structures related to mainly V. cholerae. Altogether, this study contributes to the understanding of Inovirus infection dynamics and mobilization of zot-like genes beyond human pathogenic vibrios, and discusses their potential role in the evolution of the fish pathogen V. anguillarum.

scholarly journals Purification and Characterization of an Extracellular Protease from the Fish Pathogen Yersinia ruckeri and Effect of Culture Conditions on Production

1999 ◽  
Vol 65 (9) ◽  
pp. 3969-3975 ◽  
Author(s):  
P. Secades ◽  
J. A. Guijarro
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Maximal Activity ◽  
Exchange Chromatography ◽  
Casamino Acid ◽  
Exponential Growth Phase ◽  
Yersinia Ruckeri ◽  
Fish Pathogen ◽  
Sds Page

ABSTRACT A novel protease, hydrolyzing azocasein, was identified, purified, and characterized from the culture supernatant of the fish pathogenYersinia ruckeri. Exoprotease production was detected at the end of the exponential growth phase and was temperature dependent. Activity was detected in peptone but not in Casamino Acid medium. Its synthesis appeared to be under catabolite repression and ammonium control. The protease was purified in a simple two-step procedure involving ammonium sulfate precipitation and ion-exchange chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the purified protein indicated an estimated molecular mass of 47 kDa. The protease had characteristics of a cold-adapted protein, i.e., it was more active in the range of 25 to 42°C and had an optimum activity at 37°C. The activation energy for the hydrolysis of azocasein was determined to be 15.53 kcal/mol, and the enzyme showed a rapid decrease in activity at 42°C. The enzyme had an optimum pH of around 8. Characterization of the protease showed that it required certain cations such as Mg2+ or Ca2+ for maximal activity and was inhibited by EDTA, 1,10-phenanthroline, and EGTA but not by phenylmethylsulfonyl fluoride. TwoN-methyl-N-nitro-N-nitrosoguanidine mutants were isolated and analyzed; one did not show caseinolytic activity and lacked the 47-kDa protein, while the other was hyperproteolytic and produced increased amounts of the 47-kDa protein. Azocasein activity, SDS-PAGE, immunoblotting by using polyclonal anti-47-kDa-protease serum, and zymogram analyses showed that protease activity was present in 8 of 14 strains tested and that two Y. ruckeri groups could be established based on the presence or absence of the 47-kDa protease.

Structural Characterization of Vanchrobactin, a New Catechol Siderophore Produced by the Fish Pathogen Vibrio anguillarum Serotype O2.

ChemInform ◽  
2007 ◽  
Vol 38 (3) ◽  
Author(s):  
Raquel G. Soengas ◽  
Cristina Anta ◽  
Alfonso Espada ◽  
Vanessa Paz ◽  
Isabel R. Ares ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Vibrio Anguillarum ◽  
Fish Pathogen

scholarly journals Characterization of Heme Uptake Cluster Genes in the Fish Pathogen Vibrio anguillarum

2004 ◽  
Vol 186 (18) ◽  
pp. 6159-6167 ◽  
Author(s):  
Susana Mouriño ◽  
Carlos R. Osorio ◽  
Manuel L. Lemos
Keyword(s):  
Gene Cluster ◽  
Genomic Library ◽  
Single Gene ◽  
Vibrio Anguillarum ◽  
Gene Arrangement ◽  
Fish Pathogen ◽  
Heme Uptake ◽  
E Coli ◽  
Iron Source

ABSTRACT Vibrio anguillarum can utilize hemin and hemoglobin as sole iron sources. In previous work we identified HuvA, the V. anguillarum outer membrane heme receptor by complementation of a heme utilization mutant with a cosmid clone (pML1) isolated from a genomic library of V. anguillarum. In the present study, we describe a gene cluster contained in cosmid pML1, coding for nine potential heme uptake and utilization proteins: HuvA, the heme receptor; HuvZ and HuvX; TonB, ExbB, and ExbD; HuvB, the putative periplasmic binding protein; HuvC, the putative inner membrane permease; and HuvD, the putative ABC transporter ATPase. A V. anguillarum strain with an in-frame chromosomal deletion of the nine-gene cluster was impaired for growth with heme or hemoglobin as the sole iron source. Single-gene in-frame deletions were constructed, demonstrating that each of the huvAZBCD genes are essential for utilization of heme as an iron source in V. anguillarum, whereas huvX is not. When expressed in Escherichia coli hemA (strain EB53), a plasmid carrying the gene for the heme receptor, HuvA, was sufficient to allow the use of heme as the porphyrin source. For utilization of heme as an iron source in E. coli ent (strain 101ESD), the tonB exbBD and huvBCD genes were required in addition to huvA. The V. anguillarum heme uptake cluster shows some differences in gene arrangement when compared to homologous clusters described for other Vibrio species.

Structural characterization of vanchrobactin, a new catechol siderophore produced by the fish pathogen Vibrio anguillarum serotype O2

2006 ◽  
Vol 47 (39) ◽  
pp. 7113-7116 ◽  
Author(s):  
Raquel G. Soengas ◽  
Cristina Anta ◽  
Alfonso Espada ◽  
Vanessa Paz ◽  
Isabel R. Ares ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Vibrio Anguillarum ◽  
Fish Pathogen

ChemInform Abstract: Structure of Anguibactin (Ia), a Unique Plasmid-Related Bacterial Siderophore from the Fish Pathogen Vibrio anguillarum

ChemInform ◽  
1989 ◽  
Vol 20 (15) ◽  
Author(s):  
M. A. F. JALAL ◽  
M. B. HOSSAIN ◽  
D. VAN DER HELM ◽  
J. SANDERS-LOEHR ◽  
L. A. ACTIS ◽  
...  
Keyword(s):  
Vibrio Anguillarum ◽  
Fish Pathogen ◽  
Abstract Structure ◽  
Unique Plasmid
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