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Immunogenetics. 1993;37(2):95-101.

Different rates of HLA class I molecule assembly which are determined by amino acid sequence in the alpha 2 domain.

Author information

1
Molecular Immunology Group, John Radcliffe Hospital, Oxford, UK.

Abstract

Assembly of HLA class I molecules was studied using pulse-chase labeling of B-lymphoblastoid cell lines with 35S-methionine, immunoprecipitation with antibodies detecting free or beta 2-microglobulin-associated heavy chain and isoelectric focusing. Marked differences between the products of different class I alleles were noted. HLA-B51 assembled very inefficiently, with considerable free heavy chain still detected in an unsialated form after a four hour chase. The closely related molecule HLA-B35 was in contrast rapidly assembled, all newly synthesized heavy chain being detected in a beta 2m-associated sialated form within 30 minutes. Analysis of naturally occurring variants related to HLA-B35 and HLA-B51 localized the region determining assembly efficiency to the alpha 2 domain, in which these molecules differ at eight amino acid residues. The effect was not due to a linked dominant gene, as both patterns of assembly were observed in a single cell line.

PMID:
7678580
DOI:
10.1007/bf00216831
[Indexed for MEDLINE]

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