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The major histocompatibility class II DQ molecules are dimeric glycoproteins involved in antigen presentation to CD4 + T cells. In the current work, we have performed the molecular analysis of the goat Cahi-DQA1 gene. Sequencing of the Cahi-DQA1 cDNA revealed a single 768 bp open reading frame. The alignment of this sequence with its bovine and ovine DQA1 counterparts revealed a remarkable degree of nucleotide identity (92–93% for the most similar bovine and ovine sequences). Moreover, we amplified a region including the 3′-end of intron 1, exon 2 and the 5′-end of intron 2. We identified seven Cahi-DQA1 alleles that likely correspond to four different allelic lineages. The alignment of these seven Cahi-DQA1 alleles revealed the existence of 23 amino acid polymorphic sites, seven of which (α 10 , α 55 , α 56 , α 68 , α 69 , α 71 and α 76 ) are highly polymorphic with at least three amino acid substitutions. Ten of the 23 polymorphic amino acid sites were included in the peptide binding region and consequently they might play a crucial role in immunological processes modulating disease pathogenesis. |
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