A further Characterization of Yersinia ruckeri (Enteric Redmouth Bacterium)

1979 ◽  
Vol 14 (2) ◽  
pp. 71-78 ◽  
Author(s):  
P.J. O'LEARY ◽  
J.S. ROHOVEC ◽  
J.L. FRYER
Keyword(s):  
Yersinia Ruckeri

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.

scholarly journals Occurrence and Phenotypic Characterization of Yersinia ruckeri Strains with Biofilm-Forming Capacity in a Rainbow Trout Farm

2002 ◽  
Vol 68 (2) ◽  
pp. 470-475 ◽  
Author(s):  
L. Coquet ◽  
P. Cosette ◽  
L. Quillet ◽  
F. Petit ◽  
G.-A. Junter ◽  
...  
Keyword(s):  
Recurrent Infection ◽  
Pcr Amplification ◽  
Fish Farm ◽  
Phenotypic Characterization ◽  
Yersinia Ruckeri ◽  
Enterobacterial Repetitive Intergenic Consensus ◽  
Solid Supports ◽  
Potential Source ◽  
Sessile Cells

ABSTRACT The presence of Yersinia ruckeri in a French fish farm was investigated. Y. ruckeri was isolated mainly from algae and sediment samples rather than from water. Twenty-two Y. ruckeri isolates were obtained, and three strains were distinguished by enterobacterial repetitive intergenic consensus PCR amplification. These strains were able to adhere to solid supports. This characteristic was correlated with flagellum-mediated motility. Killing experiments showed that sessile cells were more resistant to oxolinic acid than their planktonic counterparts. Our results demonstrate that surface colonization of fish farm tanks by Y. ruckeri biofilms is a potential source of recurrent infection for extended periods of time.

Advancing the fathead minnow (Pimephales promelas) as a model for immunotoxicity testing: Characterization of the renal transcriptome following Yersinia ruckeri infection

2020 ◽  
Vol 103 ◽  
pp. 472-480
Author(s):  
Leah M. Thornton Hampton ◽  
Christopher J. Martyniuk ◽  
Barney J. Venables ◽  
Marlo K. Sellin Jeffries
Keyword(s):  
Fathead Minnow ◽  
Pimephales Promelas ◽  
Yersinia Ruckeri

Antigenic and Molecular Characterization of Yersinia ruckeri Proposal for a New Intraspecies Classification

1993 ◽  
Vol 16 (3) ◽  
pp. 411-419 ◽  
Author(s):  
Jesus L. Romalde ◽  
Beatriz MagariÑos ◽  
Juan L. Barja ◽  
Alicia E. Toranzo
Keyword(s):  
Molecular Characterization ◽  
Yersinia Ruckeri

Isolation and characterization of OmpF-like porin from Yersinia ruckeri

2012 ◽  
Vol 6 (3) ◽  
pp. 235-242 ◽  
Author(s):  
D. K. Chistyulin ◽  
O. D. Novikova ◽  
O. Yu. Portnyagina ◽  
V. A. Khomenko ◽  
T. I. Vakorina ◽  
...  
Keyword(s):  
Yersinia Ruckeri ◽  
Isolation And Characterization

scholarly journals Morphological and biochemical characterization of two fish pathogenic bacteria: Aeromonas salmonicida and Yersinia ruckeri for rapid diagnosis of fish disease

2017 ◽  
Vol 3 (1) ◽  
pp. 44-51
Author(s):  
Tasmina Akter
Keyword(s):  
Pathogenic Bacteria ◽  
Body Shape ◽  
Biochemical Characterization ◽  
Rapid Diagnosis ◽  
Aeromonas Salmonicida ◽  
Yersinia Ruckeri ◽  
Study Results ◽  
Vibrio Mimicus ◽  
Fish Bacteria

Aeromonas salmonicida and Yersinia ruckeri are two common pathogenic fish bacteria responsible for furunculosis and Enteric Red Mouth disease (ERM), respectively. For the characterization of these two pathogens, a series of morphological (pigmentation, hemolyse, motility and body shape), biochemical tests (Gram staining, catalase, oxidase and API 20E strips) and a soft ionization technique (MALDI-TOF/MS) were performed in the laboratory. Pigmentation, motility, hemolysis and body shape was used as a preliminary identification of the bacteria. Both of the species were identified with the entire biochemical test without any doubt except API20E strips test. Although the API profile of A. salmonicida (0006104) was identified with high confidence (99.6%), but Y. ruckeri was misidentified as Vibrio mimicus. There are strong supports against Vibrio mimicus as it is a human pathogen, grow at a temperature more than 20oC, motile and oxidase positive bacteria. The Y. ruckeri is a non-motile fish bacteria and oxidase negative which are consistent with the study results. Agglutination test with Bionor Mono kit was also identified the bacteria as Y. ruckeri. For rapid diagnosis of infectious disease, accurate identification of pathogen is very important for commercial aquaculture.Asian J. Med. Biol. Res. March 2017, 3(1): 44-51

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