Functional polymorphisms among HLA-DR4+ DR beta chains associated with limited peptide diversity.
Tryptic peptide map analysis by high-pressure liquid chromatography of DR4- associated DR beta chains revealed limited structural variation within DR beta polypeptides. Comparison of 3H-leucine-labelled tryptic peptide maps of Dw4 and Dw14 homozygous cells identified distinct peaks corresponding to Dw4 and Dw14-associated DR beta polypeptides. HPLC analysis of cell line 256, heterozygous for two DR4-related specificities, Dw4 and Dw14, displayed both peptides, corresponding to the variable Dw4 and Dw14 chromatograms. This observation was confirmed using a deletion mutant cell line derived from 256 lacking Dw4-associated class II genes. The observed peptide variation correlated precisely with predicted nucleotide-derived amino acid sequences implicating amino acids 66-71 of the DR beta chain as contributing to HLA-D structural and functional polymorphisms.
Seyfried
C E
CE
Virginia Mason Research Center, Seattle, WA 98101.
Gregersen
P K
PK
Nepom
B S
BS
Nepom
G T
GT
D000595:Amino Acid Sequence; D001483:Base Sequence; D002460:Cell Line; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006681:HLA-D Antigens / Q000235:genetics*; D006684:HLA-DR Antigens / Q000235:genetics* / Q000276:immunology; D006239:Haplotypes; D006801:Humans; D010449:Peptide Mapping; D011110:Polymorphism, Genetic; D014357:Trypsin / Q000494:pharmacology
D006681:HLA-D Antigens; D006684:HLA-DR Antigens; D014357:Trypsin