Molecular Cloning of a Bovine Immunoglobulin Lambda Chain cDNA

Abstract

A cDNA library of the bovine mammary gland constructed in pBR322 was screened by mRNA hybrid-selected translation and by differential hybridization. Several immunoglobulin (Ig) λ light-chain clones were identified and sequenced. Nucleotide sequence comparison of bovine and human Ig λ chains showed a high degree of homology for constant regions and for J regions. The amino acid (aa) sequence encoded by the constant region of the bovine Ig λ chain cDNA contains 107 aa with differences at 24 aa positions from the human Ig A chain. Three complementarity-determining regions (CDR1,2,3) characteristic of the variable region of bovine Ig λ chain cDNA can be distinguished. The bovine and human sequences display good homology in the framework region 3 (FR3) but only patches of homology throughout the FR2 region. The 5′ end of the bovine Ig λ chain cDNA fragment of clone 1-14E contains five stop codons: two in CDR1, one in FR1 and two in the hydrophobic prepeptide region. These data suggest that the Igλ mRNA of clone 1-14E is transcribed from the Vλ pseudogene

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