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Rotavirus infection inhibits SLA-I expression on the cell surface by degrading 82 M via ERAD-proteasome pathway

文献类型： 外文期刊

作者： Jing, Zhaoyang;Wu, Ling;Pan, Yudi;Zhang, Liaoyuan;Zhang, Xin;Shi, Da;Shi, Hongyan;Chen, Jianfei;Ji, Zhaoyang;Zhang, Jiyu;Feng, Tingshuai;Tian, Jin;Feng, Li

作者机构：

关键词： RVA;8 2M;ERAD-proteasome pathway;SLA-I;K48-linked ubiquitination

期刊名称： VETERINARY MICROBIOLOGY

ISSN： 0378-1135

年卷期： 2024 年 292 卷

页码：

收录情况： SCIE（2024版）

摘要： Group A Rotavirus (RVA) is a major cause of diarrhea in infants and piglets. 82-microglobulin (82 M), encoded by the B2M gene, serves as a crucial subunit of the major histocompatibility complex class I (MHC-I) molecules. 82 M is indispensable for the transport of MHC-I to the cell membrane. MHC-I, also known as swine leukocyte antigen class I (SLA-I) in pigs, presents viral antigens to the cell surface. In this study, RVA infection downregulated 82 M expression in both porcine intestinal epithelial cells -J2 (IPEC-J2) and MA -104 cells. RVA infection did not down -regulate the mRNA level of the B2M gene, indicating that the down -regulation of 82 M occurred on the protein level. Mechanismly, RVA infection triggered 82 M aggregation in the endoplasmic reticulum (ER) and enhanced the Lys48 (K48) -linked ubiquitination of 82 M, leading to the degradation of 82 M through ERAD-proteasome pathway. Furthermore, we found that RVA infection significantly impeded the level of SLA-I on the surface, and the overexpression of 82 M could recover its expression. In this study, our study demonstrated that RVA infection degrades 82 M via ERAD-proteasome pathway, consequently hampering SLA-I expression on the cell surface. This study would enhance the understanding of the mechanism of how RVA infection induces immune escape.

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