The impact of micropolymorphism in Anpl-UAA on structural stability and peptide presentation
文献类型： 外文期刊
作者： Tang, Ziche 1 ; Wang, Suqiu 1 ; Du, Liubao 1 ; Hu, Dongmei 1 ; Chen, Xiaoming 1 ; Zheng, Hanyin 1 ; Ding, Han 1 ; Chen, Shiwen 1 ; Zhang, Lin 2 ; Zhang, Nianzhi 1 ;
作者机构： 1.China Agr Univ, Coll Vet Med, Natl Key Lab Vet Publ Hlth Secur, Key Lab Anim Epidemiol,Minist Agr & Rural Affairs, Beijing 100193, Peoples R China
2.Shandong Acad Agr Sci, Inst Anim Sci & Vet Med, Shandong Key Lab Anim Dis Control & Breeding, Jinan 250100, Shandong, Peoples R China
3.Key Lab Livestock & Poultry Multi MARA, Jinan 251000, Peoples R China
关键词： Micropolymorphism; Peptide presentation; RPLD-MS; Crystal structure
期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.2； 五年影响因子：7.8 ）
ISSN： 0141-8130
年卷期： 2024 年 267 卷
页码：
收录情况： SCI
摘要： Micropolymorphism significantly shapes the peptide-binding characteristics of major histocompatibility complex class I (MHC-I) molecules, affecting the host's resistance to pathogens, which is particularly pronounced in avian species displaying the "minimal essential MHC" expression pattern. In this study, we compared two duck MHC-I alleles, Anpl-UAA*77 and Anpl-UAA*78, that exhibit markedly different peptide binding properties despite their high sequence homology. Through mutagenesis experiments and crystallographic analysis of complexes with the influenza virus-derived peptide AEAIIVAMV (AEV9), we identified a critical role for the residue at position 62 in regulating hydrogen-bonding interactions between the peptide backbone and the peptide-binding groove. This modulation affects the characteristics of the B pocket and the stability of the loop region between the 310 helix and the alpha 1 helix, leading to significant changes in the structure and stability of the peptide-MHC-I complex (pMHC-I). Moreover, the proportion of different residues at position 62 among Anpl-UAAs may reflect the correlation between pAnpl-UAA stability and duck body temperature. This research not only advances our understanding of the Anpl-UAA structure but also deepens our insight into the impact of MHC-I micropolymorphism on peptide binding.
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