Isolation and identification of a cDNA clone corresponding to an HLA-DR antigen beta chain.

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Abstract
The HLA-D locus in the major histocompatibility complex controls the expression of the genetically polymorphic HLA-DR antigens. mRNA coding for the .beta. chains of these antigens was partially purified from the human lymphoblastoid cell line Raji. The mRNA was copied into double-stranded c[complementary]DNA and cloned in Escherichia coli. One clone, pDR-.beta.-1, obtained by hybrid selection, carries a 1070-base-pair insert comprising all of the coding region except the signal sequence and a substantial portion of the untranslated region. To identify pDR-.beta.-1, highly purified HLA-DR antigen .beta. chains derived from Raji cells were subjected to NH2-terminal amino acid sequence determination. This sequence displayed extensive homology with that deduced from the nucleotide sequence at the 5'' end of the pDR-.beta.-1 coding region. Taken together, the amino acid and nucleotide sequences strongly argue in favor of Raji cells containing at least 2 .beta.-chain loci.