Insights into the structural features of a feline CD8αα homodimer

文献类型： 外文期刊

第一作者： Liang, Rui Ying

作者： Liang, Rui Ying;Liang, Rui Ying;Cao, Yu Die;Li, Hai Yang;Sang, Chen Jun;Xiu, Yu He;Li, Dan;Liu, Da Zhong;Gao, Feng Shan;Bin Li, Zi;Gao, Yong Yu;Gao, Feng Shan;Bin Li, Zi

作者机构：

关键词： Feline; CD8 alpha alpha; Crystal structure; MHC I; Evolution

期刊名称：DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY （ 影响因子：2.4； 五年影响因子：2.7 ）

ISSN： 0145-305X

年卷期： 2025 年 169 卷

页码：

收录情况： SCI

摘要： Cat ownership enjoys widespread popularity across the globe, with over 50 % of households in certain countries owning feline companions. Besides providing outstanding emotional support for humans, cats occupy a distinctive niche in scientific research, with their unique biological attributes and disease susceptibilities establishing them as a preferred model species across multiple disciplines. However, structural features and biological role of feline immune-related molecules remain largely unknown. In the current study, we crystallized feline CD8 alpha alpha (fCD8 alpha alpha) ectodomain and analyze its structural features. The fCD8 alpha alpha ectodomain adopts canonical fold of the CD8 alpha alpha homodimer immunoglobulin variable (Ig-V) domain and shares a common feature of CD8 alpha also is a symbolic alpha-helix located on the E-F loop. In line with the known CD8 alpha alpha, the homodimer formation of fCD8 alpha alpha relies upon the conserved hydrophobic core,and conserved as well as species-specific residues provide additional hydrogen bonds. Compared with other known CD8 alpha monomers, the structural differences of the fCD8 alpha monomer focus on the loop regions linking different strands, which also show low sequence similarity in alignment analyses. Further, we generate an fCD8 alpha alpha/FLA-E*01801 model with high pLDDT and ipTM scores using AlphaFold3. Regardless of the spatial conformations of conserved or similar residues and possible interactions, the binding manner between fCD8 alpha alpha and FLA-E*01801 complex closely resembles that of the known hCD8 alpha alpha/HLA-A*0201 complex. Overall, our results provide structural and immunological knowledge for studying CD8 alpha alpha function in the feline model and reveal the potential immunomodulatory roles of feline CD8 and its binding partners, deepening our understanding of the structural and functional mechanisms underlying feline immune responses.

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