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MOV10 inhibits replication of porcine reproductive and respiratory syndrome virus by retaining viral nucleocapsid protein in the cytoplasm of Marc-145 cells
- Zhao, Kuan, Li, Li-Wei, Zhang, Yu-Jiao, Jiang, Yi-Feng, Gao, Fei, Li, Guo-Xin, Yu, Ling-Xue, Zhao, Wen-Ying, Shan, Tong-Ling, Zhou, Yan-Jun, Tong, Guang-Zhi
- Biochemical and biophysical research communications 2018 v.504 no.1 pp. 157-163
- Porcine reproductive and respiratory syndrome virus, adsorption, control methods, cytoplasm, drugs, fluorescent antibody technique, leukemia, livestock production, nucleocapsid, nucleocapsid proteins, physiological transport, precipitin tests, protein content, swine, virus replication, viruses
- Porcine reproductive and respiratory syndrome virus (PRRSV) has been a major threat to global industrial pig farming ever since its emergence in the late 1980s. Identification of sustainable and effective control measures against PRRSV transmission is a pressing problem. The nucleocapsid (N) protein of PRRSV is specifically localized in the cytoplasm and nucleus of virus-infected cells which is important for PRRSV replication. In the current study, a new host restricted factor, Moloney leukemia virus 10-like protein (MOV10), was identified as an inhibitor of PRRSV replication. N protein levels and viral replication were significantly reduced in Marc-145 cells stably overexpressing MOV10 compared with those in wild-type Marc-145 cells. Adsorption experiments revealed that MOV10 did not affect the attachment and internalization of PRRSV. Co-immunoprecipitation and immunofluorescence co-localization analyses showed that MOV10 interacted and co-localized with the PRRSV N protein in the cytoplasm. Notably, MOV10 affected the distribution of N protein in the cytoplasm and nucleus, leading to the retention of N protein in the former. Taken together, these findings demonstrate for the first time that MOV10 inhibits PRRSV replication by restricting the nuclear import of N protein. These observations have great implications for the development of anti-PRRSV drugs and provide new insight into the role of N protein in PRRSV biology.