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ANALYSIS OF GENETIC DIFFERENCES IN EARLY VERSUS LATE AGGLUTINABILITY WITH H‐2 ANTIBODIES OF NEONATAL MOUSE ERYTHROCYTES
Author(s) -
Boubelík M.,
Lengerová Alena
Publication year - 1977
Publication title -
international journal of immunogenetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.41
H-Index - 47
eISSN - 1744-313X
pISSN - 1744-3121
DOI - 10.1111/j.1744-313x.1977.tb00917.x
Subject(s) - antibody , agglutination (biology) , biology , trypsin , phenotype , receptor , trypsinization , microbiology and biotechnology , gene , biochemistry , immunology , enzyme
SUMMARY Neonatal red blood cells (RBC) of some mouse strains are agglutinable by H‐2 antibodies immediately after birth (early strains, E) while others only on day 3 (late strains, L). Previous genetic analysis led to the conclusion that there are at least three ‘temporal’ genes controlling the timing of agglutinability. In the present study, we attempted to throw some light on the way in which these genes function by defining the phenotypic difference(s) between H‐2 agglutinable (E) and non‐agglutinable (L) neonatal RBC. We found that the E vs L difference was not manifested in two other assays, for in agglutination with lectins (Con A and PHA) both cell types behaved as E while in formation of alloclusters with H‐2 specific lymphocytes both behaved as L. Unlike H‐2 a E, H‐2 a L (native) neonatal RBC had virtually no detectable antibody‐absorbing capacity, however, following digestion with trypsin or neuraminidase (NANAse) they acquired both antibody‐absorbing capacity and agglutinability. In contrast to it, adult RBC lost agglutinability following GA‐fixation, but this could not be counteracted by trypsinization. Neonatal H‐2 a L RBC could be made agglutinable by the action of dimethylsulphoxide (DMSO) or by an admixture of adult H‐2 a RBC. The results are thus compatible with a hypothesis that the H‐2 receptors on neonatally non‐agglutinable (L) RBC are not absent, but in a state interfering with agglutinability; a poor accessibility to antibody may be due to a rigid integration of H‐2 sites with the cell membrane which prevents their antibody‐mediated juxtaposition to similarly rigid receptors on other cells. The possible nature of the allelic difference between E and L H‐2 receptors is discussed.