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Immunogenetics. 2004 Jul;56(4):304-9. Epub 2004 Jun 8.

cDNA cloning and genomic structure of the duck (Anas platyrhynchos) MHC class I gene.

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The Key Laboratory of Veterinary Molecular Biology, College of Veterinary Medicine, China Agricultural University, 100094 Beijing, PR China.


In order to provide data for studies on disease resistance, duck MHC class I cDNA (Anpl-MHC I) was cloned from a duck cDNA library and the genome structure was investigated. Anpl-MHC I genes encoded 344-355 amino acids. The genomic organization is composed of eight exons and seven introns. Based on the genetic distance, Anpl-MHC I cDNA from six individuals can be classified into four lineages (from Anpl-UAA to Anpl-UDA). A total of 28 amino acid positions in the peptide-binding domain (PBD) showed high scores by Wu-kabat index analysis. The Anpl-MHC amino acid sequence displayed seven critical HLA-A2amino acids that bind with antigen polypeptides, and have an 83.6-88.5% amino acid homology with each lineage, a 55.2-64.6% amino-acid homology with chicken MHC class I (B-FIV21, B-FIV2, Rfp-Y), and a 40.3-42.8% homology with mammalian MHC class I. Nested PCR detected that Anpl-MHC I can be expressed in the brain, heart, kidney, intestines and bursa. Compared with the human HLA-A2 tertiary structure of the PBD, Anpl-MHC I had an insertion or deletion variation in four domains (A-D). The phlyogenetic tree appears to branch in an order consistent with accepted evolutionary pathways.

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