Identification of the strain-specifically truncated nonstructural protein 10 of porcine reproductive and respiratory syndrome virus in infected cells

• Published in: Journal of Integrative Agriculture Vol. 17; no. 5; pp. 1171 - 1180
• Main Authors: ZHANG, Zhi-bang, XU, Lei, WEN, Xue-xia, DONG, Jian-guo, ZHOU, Lei, GE, Xin-na, YANG, Han-chun, GUO, Xin
• Format: Journal Article
• Language: English
• Published: China Key Laboratory of Animal Epidemiology and Zoonosis, Ministry of Agriculture/College of Veterinary Medicine, China Agricultural University/State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, P.R.China 01.05.2018; CAAS. Publishing services by Elsevier B.V. Published by Elsevier B.V; KeAi Communications Co., Ltd
• Subjects: amino acids; enzymes; growth models; mass spectrometry; mutagenesis; nonstructural protein 10 (nsp10); Porcine reproductive and respiratory syndrome virus; porcine reproductive and respiratory syndrome virus (PRRSV); viral nonstructural proteins; viral replication; virus replication; viruses; viral replication; nonstructural protein 10 (nsp10); porcine reproductive and respiratory syndrome virus (PRRSV)
• ISSN: 2095-3119; 2095-3119
• DOI: 10.1016/S2095-3119(17)61896-3

The nonstructural protein 10 (nsp10) of porcine reproductive and respiratory syndrome virus (PRRSV) encodes for helicase which plays a vital role in viral replication. In the present study, a truncated form of nsp10, termed nsp10a, was found in PRRSV-infected cells and the production of nsp10a was strain-specific. Mass spectrometric analysis and deletion mutagenesis indicated that nsp10a may be short of about 70 amino acids in the N terminus of nsp10. Further studies by rescuing recombinant viruses showed that the Glu-69 in nsp10 was the key amino acid for nsp10a production. Finally, we demonstrated that nsp10a exerted little influence on the growth kinetics of PRRSV