Open AccessEvidence for tryosine peptide homologies in the HLA antigens system.
Author(s) -
Charlotte CunninghamRundles,
C Jersild,
A. Svejgaard,
Bo Dupont,
Robert A. Good
Publication year - 1975
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.72.12.5081
Subject(s) - antigen , biology , human leukocyte antigen , antiserum , antibody , epitope , tyrosine , peptide sequence , homologous chromosome , genetics , amino acid , biochemistry , gene
The tetrameric HLA antigens are composed of two heavier chains which carry the alloantigenic determinants and two lighter chains identified as beta2-microglobulin. Although at least 40 different antisera are required to define the varying HLA specificities, it appears that these antigens may be closely related to each other and to the immunoglobulins. Through the use of a new electrophoretic technique, which is able to compare simultaneously the tyrosine peptides produced from radioiodinated cell surface proteins, this report gives evidence that HLA antigens of the three chromosomal loci may have similar amino-acid sequences. Since the retention of homologous tyrosine residues and a tendency for sequence preservation surrounding these residues are features of immunoglobulin structure, this may indicate that similarly conservative evolutionary mechanisms have been operative in the HLA allelelic proteins or that immunoglobulins and HLA antigens may indeed have a common evolutionary origin.