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 cDNA 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 two beta-chain loci.
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Wiman K, Larhammar D, Claesson L, Gustafsson K, Schenning L, Bill P, Bohme J, Denaro M, Dobberstein B, Hammerling U, Kvist S, Servenius B, Sundelin J, Peterson PA, Rask L (1982) Isolation and identification of a cDNA clone corresponding to an HLA-DR antigen beta chain Proc Natl Acad Sci U S A79: 1703-7
Wiman K, Larhammar D, Claesson L, Gustafsson K, Schenning L, Bill P, Bohme J, Denaro M, Dobberstein B, Hammerling U, Kvist S, Servenius B, Sundelin J, Peterson PA, Rask L (1982) Proc Natl Acad Sci U S A79: 1703-7
