Molecular structure of human histocompatibility antigens: the HLA‐C series

D. Snary, C. J. Barnstable, W. F. Bodmer, M. J. Crumpton

Research output: Contribution to journalArticlepeer-review

156 Scopus citations


The HLA‐CW2 antigen of the B lymphoblastoid cell line BRI 8 is structurally homologous to the HLA‐A and B antigens as judged by various criteria. Each antigen comprised a glycosylated polypeptide of 43 000 molecular weight that is noncovalently associated with β2–microglobulin (β2 m). Some small differences in molecular parameters were, however, revealed. Thus, the deoxycholate‐solubilized HLA‐CW2 antigen sedimented at the same rate as the HLA‐A antigens but at a slightly faster rate than the HLA‐B antigens. This variation is apparently due to different amounts of bound deoxy‐cholate. Also, whereas essentially all of the HLA‐A and B antigens and about half of the HLA‐CW2 antigen were adsorbed Strongly by Lens culinaris lectin‐Sepharose, the remaining HLA‐CW2 antigen was bound much more weakly and did not require sugar for elution. This difference reflects some structural heterogeneity in the carbohydrate moiety of the HLA‐CW2 antigen. The results of various studies suggest that the HLA‐CW2 antigen is expressed to a lower extent than the HLA‐A or B antigens and that essentially all of the β2 m of the BRI 8 plasma membrane is associated with the HLA‐A, B and C alloantigenic polypeptides.

Original languageEnglish (US)
Pages (from-to)580-585
Number of pages6
JournalEuropean Journal of Immunology
Issue number8
StatePublished - Aug 1977

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Immunology


Dive into the research topics of 'Molecular structure of human histocompatibility antigens: the HLA‐C series'. Together they form a unique fingerprint.

Cite this