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Murine monoclonal antibodies against a unique determinant of erythrocytes, related to Rh and U antigens: expression on normal and malignant erythrocyte precursors and Rh null red cells
Author(s) -
Kr. vondem Borne Albert E. G.,
Bos Marjolein J. E.,
Lomas Christine,
Tippett Patricia,
Bloy Christian,
Hermand Patricia,
Cartron Jean Pierre,
Admiraal Lucia G.,
Van de Graaf Jettie,
Overbeeke Marijke A. M.
Publication year - 1990
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1990.tb02659.x
Subject(s) - glycophorin , epitope , monoclonal antibody , microbiology and biotechnology , glycoprotein , antigen , rh blood group system , antibody , red blood cell , biology , membrane glycoproteins , band 3 , chemistry , membrane protein , biochemistry , immunology , membrane
Summary Three murine monoclonal antibodies (Mabs) MB‐2D10, LA‐18.18 and LA‐23.40 were prepared. They reacted with red cells of all common and most rare blood‐group phenotypes, with the exception of those of the Rh null U negative and Rh mod U negative phenotypes. So far, only a single example of an alloantibody (Duclos or anti‐Rh38) of a similar specificity has been found. Serological studies indicated that the Mabs were probably not directed against an antigenic determinant of Rh polypeptides, the LW ab glycoprotein or glycophorin B, all structures absent from or aberrantly expressed on Rh null red cells. The antigen was found to be erythrocyte‐specific, and was also present on pro‐erythroblasts, erythroblasts and malignant erythroblastoid cells but not on erythroid progenitors in the bone marrow. The Mabs were found to block each other in an immune rosette method and are thus probably directed against the same epitope or against neighbouring epitopes on the same structure. In immunochemical studies, MB‐2D10 precipitated the 30–32 kDa Rh polypeptides from red cell membranes and a protein or proteins which formed diffuse and overlapping bands in SDS–polyacrylamide gel electrophoresis, with M r s of 40–200 kDa (probably the Rh‐related glycoproteins). Under certain experimental conditions glycophorin B appeared to be coprecipitated. The 2D10 structure, detected by the Mabs, seems to be part of a complex of proteins and/or glycoproteins, which includes Rh polypeptides, the LW ab glycoprotein and glycoproteins recognized by various Mabs with Rh‐related specificities. In the red cell membrane, the complex may be associated with glycophorin B.