The impact of micropolymorphism in Anpl-UAA on structural stability and peptide presentation

文献类型： 外文期刊

第一作者： Tang, Ziche

作者： Tang, Ziche;Wang, Suqiu;Du, Liubao;Hu, Dongmei;Chen, Xiaoming;Zheng, Hanyin;Ding, Han;Chen, Shiwen;Zhang, Nianzhi;Zhang, Lin;Zhang, Lin

作者机构：

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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