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The present study was aimed at determining changes in chosen elements of phagocytosis in rabbits infected with 3 antigenic variants of RHD – Hartmannsdorf, Pv97 and 9905, which differed in haemagglutination ability. The animals were tested for phagocytosis parameters, and the results revealed that the examined strains showed the differences. These variations regarded mainly Pv97 strain, as the intensity of the changes were 5 times stronger in comparison to strain Hartmannsdorf and 9905. As all of the strains examined are signified as antigenic variants, we have stated that this feature does not determine their immunological picture. The results suggest the existence of immunological dissimilarities among strains of the RHD virus, which was revealed for the first time in antigenic variants.
The presence and type of adhesins occurring in Pseudomonas aeruginosa strains were determined by hemagglutination test with a 3% suspension of normal and trypsin-treated human group A erythrocytes, with or without the addition of sugar inhibitors (D-mannose, D-glucose, L-fucose, D-galactose, D-fructose, lactose, N-acetylneuraminic acid, N-acetylglucosamine and N-acetylgalactosamine). This study showed that a low percentage of Pseudomonas aeruginosa strains caused the agglutination of normal erythrocytes. Trypsin treatment of erythrocytes did not affect the hemagglutinating properties, indicating that hemagglutination was not dependent upon a trypsin-sensitive protein on the erythrocytes surface. Most of the studied strains agglutinated RBCs at 37°C. A great variability in the inhibiting activity on studied strains was observed among the carbohydrates tested. These results demonstrated the predominant role of N-acetylglucosamine, N-acetylgalactosamine and N-acetylneuraminic acid for Pseudomonas aeruginosa adhesion to RBCs.
It has been recently recognized that lectins exhibit other activities besides hemagglutination. Previously we have found that purified lectin from Chelidonium majus showed DNase activity (Fik, Gozdzicka-Jozefiak & Kedzia, 1995, Herba Polon. 41, 84-95). Comparison of lectin and DNase from the sap from leaves and roots of Chelidonium majus proved that both these compounds are composed of 24kDa monomer subunits which have an identical N-terminal sequence but differ in amino-acid composition and degree of glycosylation. Possible interrelationship between lectin and DNase is discussed.
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