Cysteine residues of the porcine reproductive and respiratory syndrome virus ORF5a protein are not essential for virus viability
文献类型: 外文期刊
第一作者: Sun, Lichang
作者: Sun, Lichang;Zhou, Yan;Liu, Runxia;Li, Yanhua;Gao, Fei;Wang, Xiaomin;Yuan, Shishan;Wei, Zuzhang;Tong, Guangzhi;Fan, Hongjie;Wei, Zuzhang
作者机构:
关键词: PRRSV;ORF5a;Cysteine;Replication
期刊名称:VIRUS RESEARCH ( 影响因子:3.303; 五年影响因子:3.445 )
ISSN:
年卷期:
页码:
收录情况: SCI
摘要: ORF5a protein was recently identified as a novel structural protein in porcine reproductive and respiratory syndrome virus (PRRSV). The ORF5a protein possesses two cysteines at positions 29 and 30 that are highly conserved among type 2 PRRSV. In this study, the significance of the ORF5a protein cysteine residues on virus replication was determined based on a type 2 PRRSV cDNA clone (pAJXM). Each cysteine was substituted by serine or glycine and the mutations were introduced into pAJXM. We found that the replacement of cysteine to glycine at position 30 was lethal for virus viability, but all serine mutant clones produced infectious progeny viruses. This data indicated that cysteine residues in the ORF5a protein were not essential for replication of type 2 PRRSV. The bimolecular fluorescence complementation (BiFC) and Co-immunoprecipitation (Co-IP) assay were used to study ORF5a protein interacted with other enveloped proteins. These results showed that ORF5a protein interacted non-covalently with itself and interacted with GP4 and 2b protein. The replacement of cysteine to glycine at position 30 affected the ORF5a protein interacted non-covalently with itself, which may account for the lethal phenotype of mutants carrying substitution of cysteine to glycine at position 30. (C) 2014 Elsevier B.V. All rights reserved.
分类号: R37
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