Evidence for two haemolytic activities from Aeromonas salmonicida

Titball, Richard W.

doi:10.1016/0378-1097(81)90031-8

Cited by 30 publications

(45 citation statements)

References 4 publications

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“…The cell envelope protein (7,15,36) and the extracellular products (2, 6, 21) of the bacterium have been investigated as the virulent factors causing the disease symptoms. The extracellular products include proteolytic (3, 25,27,28,30), glycerophospholipid-cholesterol acyltransferase (1,18), leukocytolytic (8), and hemolytic (14,22,33) activities. They reproduce the histopathological effects associated with furunculosis infection in rainbow trout.…”

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confidence: 99%

Purification and characterization of salmolysin, an extracellular hemolytic toxin from Aeromonas salmonicida

et al. 1988

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An extracellular hemolytic toxin of Aeromonas salmonicida, termed salmolysin, was purified 945-fold by ammonium sulfate precipitation, anion-exchange chromatography on DEAE-cellulose, and gel filtration chromatography on Sephadex G-100 and Sepharose 2B. Salmolysin appeared homogeneous upon cellulose acetate membrane electrophoresis and immunodiffusion analysis. The molecular weight of the toxin was estimated to be approximately 200,000 by the sedimentation equilibrium method. The UV absorption spectrum showed a maximum at 275 nm and a minimum at 262 nm. The isoelectric point was found to be at pl 5.4. Carbohydrate and protein analyses and other biochemical data indicated that salmolysin is a glycoprotein, containing approximately 62% carbohydrates. The toxin is a heat-labile substance and is stable at a neutral pH value. Ferrous ion inhibited the activity, whereas metal-chelating agents did not affect the activity. Sulfhydryl reagents did not inhibit the toxin, whereas reducing agents, such as L-cysteine and reduced glutathione, inhibited the toxin to a certain extent. Salmolysin was inactivated by a nonionic detergent but was stimulated by an anionic detergent, sodium deoxycholate, at a low concentration. The toxin was also inactivated by subtilisin and trypsin but was not inhibited by papain and pepsin. Salmolysin, with a remarkable hemolytic activity against salmonid erythrocytes, was lethal to rainbow trout when it was injected intramuscularly.

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confidence: 99%

Purification and characterization of salmolysin, an extracellular hemolytic toxin from Aeromonas salmonicida

et al. 1988

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“…Thus, it may have some practical application, in either crude or purified form, through conjugation to other non-immunogenic antigens to produce immunogenic vaccines. 26.…”

Section: Discussionmentioning

confidence: 99%

“…salmoninarum in water and sediment of 56 freshwater fish farms in England and Wales, which had a history of BKD, and could not demonstrate the presence of the organisms using a fluorescent antibody technique (26).…”

Section: Diseasementioning

confidence: 99%

“…The two major factors associated with this pathology were the serine protease and trout cell specific hemolysin (18,19) but other factors have been identified which may contribute more subtly to the pathogenic process. These include other proteases (20,21,22,23) and cytolysins (24,25,26,27). Extracellular factors have been used as immunogens with successful results.…”

Section: Acknowiedgemen'ismentioning

confidence: 99%

“…Concentrations of V. anguillarum lipopolysaccharide were expressed as ug/ml carbohydrate as determined by the phenol/sulfuric acid method (26).…”

Section: Vibrio Anguillarum O-antigen Extract and Lipopolysaccharidementioning

confidence: 99%

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Development of a Vaccine for Bacterial Kidney Disease in Salmon, 1988 Final Report.

Kaattari¹

1989

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Virulence of Photobacterium damselae subsp. piscicida in cultured cobia Rachycentron canadum

Liu

Lin

Lee

2003

J. Basic Microbiol.

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An outbreak of serious mortality among the cultured cobia Rachycentron canadum (weighing 3 kg) characterized by the presence of whitish granulomatous deposits on the kidney, liver and spleen occurred in July of 2000 in Taiwan. A non-motile strain CP1 was isolated from kidney and/or liver on tryptic soy agar and/or brain heart infusion agar plates (both supplemented with 1% NaCl, w/v). This strain was characterized and identified as Photobacterium damselae subsp. piscicida using biochemical characteristics and Bionor mono-Pp tests. The bacterium and its extracellular products (ECP) were lethal to the cobia (weighing 10 g) with LD50 values of 1.03 x 10(4) colony forming units and 1.26 microg protein/g fish body weight, respectively. All the moribund/dead fish exhibited darkness in color with no gross or internal leasions. However, the bacteria could be reisolated from kidney and liver after bacterial challenge. The present results reveal that Ph. damselae subsp. piscicida is the causative agent of fish photobacteriosis in the cobia and the bacterium isolated from sub-adult cobia (chronic form) is virulent to young cobia causing acute form of the disease.

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Evidence for two haemolytic activities from Aeromonas salmonicida

Cited by 30 publications

References 4 publications

Purification and characterization of salmolysin, an extracellular hemolytic toxin from Aeromonas salmonicida

Purification and characterization of salmolysin, an extracellular hemolytic toxin from Aeromonas salmonicida

Development of a Vaccine for Bacterial Kidney Disease in Salmon, 1988 Final Report.

Virulence of Photobacterium damselae subsp. piscicida in cultured cobia Rachycentron canadum

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