Epitope specificity of hemagglutinating monoclonal anti-B antibodies
O. E. Galanina, E. I. Deryugina, N. I. Olovnikova, A. E. Nosyrev, M. I. Lapenkov, N. B. Cheknyova, T. V. Zemlyanukhina, E. Yu. Korchagina, N. V. Bovin
M. M. Shemyakin Institute of Bioorganic Chemistry, Academy of Sciences of the USSR. Moscow, *National Hematological Scientific Centre, Ministry of Health of the USSR, Moscow
Abstract: Fine epitope specificity of ten monoclonal antibodies (MA) agglutinating red blood cells B was studied. Three methods were used: 1) inhibition of MA binding to natural antigen by synthetic oligosaccharides (OS) and their polyacrylamide conjugates, 2) direct MA binding to a series of synthetic OS-polyacrylamido conjugates differing in carbohydrate epitope density, 3) direct MA binding to the affinity sorbents. It is shown that all antibodies studied prefer trisaccharide B determinant Galα1-3(Fucα1-2) Gal independently of their ability to discriminate sorological subgroups of B erythrocytes (B, Bweak, B3). The correlation of the MAs epitope specificity with their ability to agglutinate red blood cells B subgroups is discussed. Of an interest is that MAs which are able to agglutinate any B subgroups also bing the synthetic tetrasaccharide Galα1-3(Fucα1l-2)Galβ1-3GalNAc, a B type 3 determinant.
Russian Journal of Bioorganic Chemistry 1991, 17 (9):1177-1187