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Epitope Specificity of Blood‐Group‐A‐Reactive Murine Monoclonal Antibodies
Author(s) -
Lubenko A.,
Ivanyi J.
Publication year - 1986
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1986.tb00230.x
Subject(s) - epitope , monoclonal antibody , hapten , antibody , chemistry , trisaccharide , microbiology and biotechnology , oligosaccharide , antigen , abo blood group system , biochemistry , biology , immunology
Abstract. Monoclonal antibodies (MABs) towards blood group A manifested three broad patterns of binding distinguished on the basis of affinities for A 1 or A 2 B phenotype red blood cells and blood group substances. Competitive inhibition of binding of radiolabelled MABs by other unlabelled antibodies and absorption studies with synthetic haptens suggested that GpA specificity was expressed as two topographically related structures, one being the terminal GpA trisaccharide and the second probably involving part of the oligosaccharide backbone. The enhancement of binding of an extremely low‐affinity antibody by higher affinity antibodies recognising either epitope indicated a topographic, possibly conformational relationship between these epitopes. It is suggested that only those antibodies that recognise terminal GpA trisaccharides can agglutinate weak A 2 B cells.