Annexin A2 binds to vimentin and contributes to porcine reproductive and respiratory syndrome virus multiplication

文献类型： 外文期刊

第一作者： Chang, Xiao-Bo

作者： Chang, Xiao-Bo;Yang, Yong-Qian;Gao, Jia-Cong;Zhao, Kuan;Guo, Jin-Chao;Ye, Chao;Jiang, Cheng-Gang;Tian, Zhi-Jun;Cai, Xue-Hui;An, Tong-Qing;Tong, Guang-Zhi

作者机构：

期刊名称：VETERINARY RESEARCH （ 影响因子：3.683； 五年影响因子：4.106 ）

ISSN： 0928-4249

年卷期： 2018 年 49 卷

页码：

收录情况： SCI

摘要： Porcine reproductive and respiratory syndrome virus (PRRSV) is an important globally distributed and highly contagious pathogen that has restricted cell tropism in vivo and in vitro. In the present study, we found that annexin A2 (ANXA2) is upregulated expressed in porcine alveolar macrophages infected with PRRSV. Additionally, PRRSV replication was significantly suppressed after reducing ANXA2 expression in Marc-145 cells using siRNA. Bioinformatics analysis indicated that ANXA2 may be relevant to vimentin, a cellular cytoskeleton component that is thought to be involved in the infectivity and replication of PRRSV. Co-immunoprecipitation assays and confocal analysis confirmed that ANXA2 interacts with vimentin, with further experiments indicating that the B domain (109-174 aa) of ANXA2 contributes to this interaction. Importantly, neither ANXA2 nor vimentin alone could bind to PRRSV and only in the presence of ANXA2 could vimentin interact with the N protein of PRRSV. No binding to the GP2, GP3, GP5, nor M proteins of PRRSV was observed. In conclusion, ANXA2 can interact with vimentin and enhance PRRSV growth. This contributes to the regulation of PRRSV replication in infected cells and may have implications for the future antiviral strategies.

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