Identification of carbohydrates on the surface membrane of pathogenic and nonpathogenic piscine haemoflagellates, Cryptobia salmositica, C. bullocki and C. catostomi (Kinetoplastida).
نویسندگان
چکیده
Carbohydrates and protein glycoconjugates on the cell membranes of Cryptobia salmositica, C. bullocki and C. catostomi were analyzed using 13 highly purified lectins (unlabelled or digoxigenin/biotin labelled). No agglutinations were observed with C. salmositica, C. bullocki and C. catostomi using lectin TPA (Tetragonolobus purpureas agglutinin, for alpha-L-fucose). C. salmositica was agglutinated by 3 of 12 lectins [Con A, for alpha-man and alpha-D-glc; PSA, for alpha-man; PWM, for (glcNAc)3], while C. bullocki was agglutinated by 8 lectins and C. catostomi was agglutinated by 10 lectins. Glycoconjugate analysis with digoxigenin or biotin labelled lectins showed a species-specific staining pattern in pathogenic and nonpathogenic Cryptobia spp. The nonpathogenic C. catostomi had the strongest reaction. These results indicate that the surface carbohydrate residues and glycoconjugate compositions on Cryptobia spp. are different between species they may be related to the virulence of the parasite.
منابع مشابه
In vitro secretion of metabolic end-products by piscine haemoflagellates Cryptobia salmositica and C. bullocki (Kinetoplastida: Bodonidae) and the relationship of these products to the pH in the medium.
Pathogenic and nonpathogenic strains of Cryptobia salmositica Katz, 1951 and C. bullocki Strout, 1965 produced hydrogen peroxide, pyruvate and lactate under in vitro conditions in Minimum Essential Medium (MEM). As parasite number increased, the phenol red in the medium changed from red to yellow. This change was not associated with a decrease in pH, or an increase in pyruvate or lactate, but w...
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The monoclonal antibody (MAb-001), which was produced against a surface membrane glycoprotein on C. salmositica, significantly inhibited the activities of the intracellular proteases of the parasite. The total activity in the partially purified metallo-protease, and about 80% of activity in the partially purified cysteine protease, were inhibited by the antibody (at 10 μg protein ml–1). The inh...
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عنوان ژورنال:
- Diseases of aquatic organisms
دوره 32 3 شماره
صفحات -
تاریخ انتشار 1998