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Polymorphic analysis of peptide binding domain of major histocompatibility complex class I in domestic ducks

文献类型： 外文期刊

作者： Yu, S. 1 ; Wu, J. 1 ; Bai, J. 1 ; Ding, Y. 4 ; Qiu, W. 2 ; Zhang, L. 1 ;

作者机构： 1.Shandong Acad Agr Sci, Inst Anim Sci & Vet Med, Shandong Key Lab Dis Control & Breeding, 8 Sangyuan Rd, Jinan 250100, Shandong, Peoples R China

2.Shandong Normal Univ, Coll Life Sci, 88 Wenhua East Rd, Jinan 250014, Shandong, Peoples R China

3.Hebei Univ Engn, Coll Life Sci & Food Engn, 199 Guangming South Rd, Handan 056038, Peoples R China

4.Qilu Anim Hlth Co Ltd, 243 Gongye North Rd, Jinan 250100, Shandong, Peoples R China

关键词： domestic duck; highly variably sites; MHC class I; peptide binding domain; phylogenetic tree; polymorphism

期刊名称：POLISH JOURNAL OF VETERINARY SCIENCES （ 影响因子：0.821； 五年影响因子：1.005 ）

ISSN： 1505-1773

年卷期： 2019 年 22 卷 2 期

页码：

收录情况： SCI

摘要： Function of duck (Anas platyrhynchos) major histocompatibility complex class I (Anpl-MHC I) molecules in binding peptides is through the peptide binding groove (PBG), which is thought to be influenced by the high polymorphism of alpha 1 and alpha 2 domains. However, little is known about the polymorphism of Anpl-MHC I peptide binding domain (PBD), especially in the domestic duck. Here, we analyzed the polymorphism of forty-eight Anpl-MHC I alpha 1 and alpha 2 domains from domestic duck breeds previously reported. All sequences were analyzed through multiple sequence alignment and a phylogenetic tree was constructed. The coefficient of variance of the peptide binding domains (PBDs) from WS, CV, JD, and SX duck breeds was estimated based on the Wu-Kabat variability index, followed by the location of the highly variable sites (HVSs) on reported crystal structure models. Analysis of alpha 1 and alpha 2 domains showed common features of classical MHC class I and high polymorphism, especially in alpha 1 domain. The constructed phylogenetic tree showed that PBDs of domestic ducks did not segregate based on breeds and had a close phylogenetic relationship, even with wild ducks. In each breed, HVSs were mostly located in the PBG, suggesting that they might determine peptide-binding characteristics and subsequently influence peptide presentation and recognition. The combined results of sequence data and crystal structure provide novel valuable insights into the polymorphism and diversity of Anpl-MHC I PBDs that will facilitate further studies on disease resistance differences between duck breeds and the development of cytotoxic T-lymphocyte (CTL) epitope vaccines suited for preventing diseases in domestic ducks.

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