Anti-id sera to Rh antibodies were produced by injecting rabbits with purified Rh antibodies. These sera were shown to agglutinate O Rh+ RBC coated by the immunizing antibody and--in some cases--by other anti-D antibodies. Id and cross-reactive id were shown to be located in the antigen-binding and in the non-antigen binding regions of Rh antibodies. An unique example of evolution of idiotypic specificities on human antibodies has been reported. Lastly, we have demonstrated by rosette assay, presence on some PBL of receptors for Fab'2 anti-Rh coating O Rh+ red cells. Rosettes could not be obtained with lymphocytes of a donor and Fab'2 anti-Rh of another individual. Rosettes appeared at a period of time in which the amount of antibody was decreasing.
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http://dx.doi.org/10.1016/s0338-4535(84)80127-0 | DOI Listing |
Anti-id sera to Rh antibodies were produced by injecting rabbits with purified Rh antibodies. These sera were shown to agglutinate O Rh+ RBC coated by the immunizing antibody and--in some cases--by other anti-D antibodies. Id and cross-reactive id were shown to be located in the antigen-binding and in the non-antigen binding regions of Rh antibodies.
View Article and Find Full Text PDFRev Fr Transfus Immunohematol
December 1983
Evolution of idiotypic determinants on lymphocytes membrane and presence of other lymphocytes carrying anti-idiotypic determinants, were studied in Rh negative human volunteer blood donors during immunization towards Rh factor. For this purpose E-Rh Rosettes, direct immunofluorescence, inhibition of E-Rh Rosettes by anti-idiotypic sera as well as EA-Rh Rosettes--induced with Fab'2 fragments from anti-Rh antibodies and lymphocytes from the same subject--were examined and compared to the evolution of circulating antibodies. E-Rh Rosettes preceded or accompanied production of anti-Rh antibodies; their frequency decreased after the fifth month following immunization, meanwhile EA-Rh Rosettes increased in parallel with antibody decrease.
View Article and Find Full Text PDFClin Exp Immunol
November 1978
To study the possible heterogeneity of human lymphocyte Fc receptors, isolated human peripheral blood lymphocytes (PBL) were enzymatically altered (`stripped') by exposure to pronase or papain. Pronase treatment markedly increased the percentages of PBL binding IgG-sensitized erythrocytes (EA), while simultaneously removing or inactivating their receptors for heat-aggregated IgG (aggG). Papain treatment markedly diminished the ability of PBL to bind both EA and aggG.
View Article and Find Full Text PDFHuman peripheral blood lymphocytes (PBL) were incubated (stripped) with pronase or papain and compared with unstripped lymphocytes for their ability to mediate antibody-dependent, cell-mediated cytotoxicity (ADCC). Despite marked removal or inactivation of receptors for heat-aggregated IgG (aggG) by proteolytic digestion, and pronounced changes in the percentages of cells rosetting with IgG-sensitized erythrocytes (EA) (decreased by papain, increased by pronase), stripped PBL functioned normally in ADCC. Stripped and unstripped lymphocytes were pre-treated with aggG to determine the role of aggG receptors in ADCC.
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