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A monoclonal antibody against a Burkitt lymphoma associated antigen has an anti‐P k red blood cell specificity
Author(s) -
Fellous Marc,
Cartron JeanPierre,
Wiels Joelle,
Tursz Thomas
Publication year - 1985
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.1365-2141.1985.tb07454.x
Subject(s) - monoclonal antibody , antigen , antibody , microbiology and biotechnology , red blood cell , epitope , biology , monoclonal , lymphoma , chemistry , immunology
S ummary The blood group specificity of a rat IgM monoclonal antibody (38–13) directed against most EBV‐positive or ‐negative Burkitt's lymphoma was investigated. The target antigen was previously identified as the neutral glycolipid ceramide trihexoside (CTH), a substance which accumulates in red cells from very rare individuals of the P k phenotype and which appears as a normal intermediate in the biosynthetic pathway of the P blood group antigen (globoside). The 38–13 antibody agglutinated Pk/1 and Pk/2 red cells at 4°C with a very high titre but was inactive against native P 1 , P 2 and p erythrocytes, although a very weak activity was noticed towards papain‐treated P 1 and P 2 erythrocytes. These results were confirmed by an indirect radio‐binding assay which also demonstrated that the 38–13 antibody reacted with lymphocytes, fibroblasts and EBV‐positive lymphoblastoid cell lines derived from Pk/1 and Pk/2 individuals but not from other donors. These findings demonstrate that the 38–13 monoclonal antibody previously considered as specific of Burkitt cells could be routinely used as an anti‐P k blood group typing reagent. The mechanism of CTH accumulation in Burkitt cells and P k red cells is probably different and might be associated respectively with the activation of an α‐4‐galactosyltransferase or the genetic blockage of a β‐3‐N‐acetylgalactosa‐minyltransferase.