Precipitating Antibody Against Aeromonas salmonicida in Serums of Inbred Albino Rainbow Trout (Salmo gairdneri)

1970 ◽  
Vol 27 (8) ◽  
pp. 1389-1393 ◽  
Author(s):  
Douglas P. Anderson ◽  
George W. Klontz

Precipitins in albino rainbow trout serums were demonstrated by gel diffusion after a single parenteral exposure to the soluble antigens of Aeromonas salmonicida. The fraction of the serum containing antibody activity against the presented antigens was shown by immunoelectrophoresis to be in the nonmigrating region. This corresponded to the beta-2 fraction of rabbit serum. An antibody-containing component comparable with rabbit gamma globulin was not detected.


1981 ◽  
Vol 38 (11) ◽  
pp. 1322-1326 ◽  
Author(s):  
Rocco C. Cipriano ◽  
Billy R. Griffin ◽  
Burton C. Lidgerding

Extracellular growth products, extracted from culture supernatants of Aeromonas salmonicida by precipitation with ammonium sulfate and ethanol, were resolved into four fractions by ion-exchange chromatography. Although one of these (fraction II) possessed leukocytolytic activity, virulence of the pathogen was not associated with leukocytotoxicity. A positive correlation was established, however, between virulence and the toxicity of extracted material to cultured rainbow trout gonad (RTG-2) cells. The crude material and fractions II and III from virulent isolates were more toxic to RTG-2 cells than were similar preparations from avirulent isolates. Preparations from virulent isolates caused hemorrhaging, lesion development, and mortality when injected intramuscularly into brook trout (Salvelinus fontinalis) and Atlantic salmon (Salmo solar). Rainbow trout (Salmo gairdneri) were more resistant and lesions could be produced only with fraction II. Fraction II also possessed proteolytic activity.Key words: Aeromonas salmonicida, furunculosis, pathogenicity, salmonids, extracellular products, cytotoxicity, leukocytolysis, proteolysis, fishes



1980 ◽  
Vol 37 (4) ◽  
pp. 746-750 ◽  
Author(s):  
C. Michel

With the aid of published information, we have developed a standardized and reproducible experimental model of furunculosis in rainbow trout (Salmo gairdneri). The infective doses (LD50 = 200 to 2000 germs, i.m.) employed strains of Aeromonas salmonicida, the virulence of which was maintained by passage in 15-g fingerlings. The number of viable cells in the dose was conveniently determined using the drop-plate enumeration technique; however, meaningful cell counts could only be obtained if broth cultures used for infecting the fish were harvested early in the exponential growth phase (OD < 1.000 at 525 nm). Better results were obtained with intramuscular injection than with intraperitoneal injection. The infection procedure involved injecting a dose of 10 LD50, intramuscularly, into each of 30 fish held at 15 °C and recording the mortalities for 10 d. Protection tests in which Tribrissen (28 mg sulfadiazine and 5.6 mg trimethoprim/kg fish for 8 d) was fed or tetracycline (1 mg per fish) i.m. injected into the infected fish served to demonstrate the value of the model. Results were in agreement with field observations with no death for treated fish and a mortality of 96%, for untreated fish. Key wordss rainbow trout, Salmo gairdneri; Aeromonas salmonicida, furunculosis, experimental infection



1977 ◽  
Vol 34 (8) ◽  
pp. 1118-1125 ◽  
Author(s):  
D. W. Fuller ◽  
K. S. Pilcher ◽  
J. L. Fryer

A substance characterized as a glycoprotein, isolated from the supernatant fluids of broth cultures of Aeromonas salmonicida by a combination of ammonium sulfate and ethanol precipitations followed by chromatography on DEAE-cellulose, was cytolytic for rainbow trout (Salmo gairdneri) leukocytes, and antigenic when injected into rabbits. The ratio of protein to hexose determined by analysis of the purified fraction was between 0.35 and 0.45, and small amounts of amino sugars were detected. A virulent strain of A. salmonicida produced much more of this factor than an avirulent strain. This factor was cytolytic for leukocytes in vitro and also produced a pronounced leukopenia when injected intravenously in adult rainbow trout. When injected in small coho salmon (Oncorhyncus kisutch) 8–13 cm long together with about one LD50 of live A. salmonicida 36 of 40 fish succumbed to the combination, whereas only 14 of 40 died from an injection of the bacterium alone. Thus, the pathogenicity of the organism was enhanced, presumably by increasing the susceptibility of the host. Hence, this glycoprotein apparently is one of the virulence factors of this bacterium. Key words: leukocytolytic factor, Aeromonas salmonicida, glycoprotein, virulence factor



1966 ◽  
Vol 23 (12) ◽  
pp. 1957-1963 ◽  
Author(s):  
George Post

Rainbow trout serum was shown to be made up of three major protein components. These three major components did not coincide by electrophoretic mobility or by relative salt solubility with the classic albumin, α-, β-, and γ-globulin separation of the sera of higher animals. A component equivalent to γ-globulin of higher animals was found to be completely lacking in the sera of both immunized and non-immunized rainbow trout.Specific humoral antibodies in rainbow trout immune sera were found to be contained in the electrophoretically least mobile proteins. These proteins coincided most nearly to the β-globulins and possibly the least electrophoretically mobile α-globulins of higher animals. Salt solubility of the serum proteins containing the specific antibody assisted in this conclusion. The electrophoretically least mobile major serum protein components were found to contain all of the antibody activity. These proteins could be removed from immune serum by 20% sodium sulfate. The assumption was made that Aeromonas hydrophila antibodies in immunized rainbow trout blood serum may be made up of a complex of serum proteins with a broad range of salt solubility and electrophoretic mobilities.Serum proteins of rainbow trout could also be classified as euglobulins or pseudoglobulins. The serum proteins which contained the A. hydrophila antibodies were found to be euglobulins.



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