S100A9 regulates porcine reproductive and respiratory syndrome virus replication by interacting with the viral nucleocapsid protein
文献类型： 外文期刊
作者： Song, Zhongbao 1 ; Bai, Juan 1 ; Liu, Xuewei 1 ; Nauwynck, Hans 2 ; Wu, Jiaqiang 3 ; Liu, Xing 4 ; Jiang, Ping 1 ;
作者机构： 1.Nanjing Agr Univ, Coll Vet Med, MOE Int Joint Collaborat Res Lab Anim Hlth & Food, Key Lab Anim Dis Diagnost & Immunol,Minist Agr, Nanjing 210095, Jiangsu, Peoples R China
2.Univ Ghent, Fac Vet Med, Lab Virol, Salisburylaan 133, B-9820 Merelbeke, Belgium
3.Shandong Acad Agr Sci, Inst Anim Husb & Vet Med, Jinan 250100, Shandong, Peoples R China
4.Minist Agr, Jiangsu Acad Agr Sci, Natl Ctr Engn Res Vet Bioprod, Key Lab Vet Biol Engn & Technol,Inst Vet Med, Nanjing 210014, Jiangsu, Peoples R China
5.Jiangsu Coinnovat Ctr Prevent & Control Important, Yangzhou, Jiangsu, Peoples R China
关键词： PRRSV; S100A9; Inhibit; Nucleocapsid protein
期刊名称：VETERINARY MICROBIOLOGY （ 影响因子：3.293； 五年影响因子：3.599 ）
ISSN： 0378-1135
年卷期： 2019 年 239 卷
页码：
收录情况： SCI
摘要： Porcine reproductive and respiratory syndrome virus (PRRSV) has caused huge economic losses to the pig industry worldwide over the last 30 years, yet the associated viral-host interactions remain poorly understood. S100A9 is a damage-associated molecular pattern of the 5100 protein family. Here, we found that PRRSV infection stimulated S100A9 expression in porcine alveolar macrophages (PAMs) and Marc-145 cells. S100A9 inhibited PRRSV replication via cellular Ca2+ dependent manner. The viral nucleocapsid (N) protein co-localized with S100A9 in the cytoplasm, and directly interacted at amino acid 78 of S100A9 and amino acids 36-37 of N protein. Moreover, we also found that the mutant S100A9 (E78Q) protein exhibited decreased antiviral activity against PRRSV compared with the parent S100A9. Recombinant PRRSV rBB (36/37) with two mutations in amino acid 36-37 in the N protein exhibited greater replication than the parent PRRSV BB0907 in S100A9-overexpressed PAM and Marc-145 cells. Thus, S100A9 may restrict PRRSV proliferation by interacting with the viral N protein.
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