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Author Report for: Servenius B

Title: Isolation and identification of a cDNA clone corresponding to an HLA-DR antigen beta chain
Wiman K, Larhammar D, Claesson L, Gustafsson K, Schenning L, Bill P, Bohme J, Denaro M, Dobberstein B and Rask L <5 more author(s)> 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 (- 5)
Ref: Proc Natl Acad Sci U S A, 79:1703, 1982 : PubMed
Abstract


ESTHER: Wiman_1982_Proc.Natl.Acad.Sci.U.S.A_79_1703
PubMedSearch: Wiman 1982 Proc.Natl.Acad.Sci.U.S.A 79 1703
PubMedID: 6952222

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 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.