Biophysical characterisation of the nucleocapsid protein from a highly pathogenic porcine reproductive and respiratory syndrome virus strain

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• 作者：Stefanie S. Jourdan^a ; Fernando A. Osorio^b ; Julian A. Hiscox^a ; ^{j.a.hiscox@leeds.ac.uk}
• 关键词：Porcine reproductive and respiratory syndrome virus ; PRRSV ; Nucleocapsid protein ; Biophysical ; RNA binding
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2012
• 期刊代码：159_0006291x
• 类别：bio
• 出版时间：9 March, 2012
• 卷：419
• 期：2
• 页码：137-141
• 文件大小：527 K

摘要

The arterivirus nucleocapsid (N) protein is a multifunctional protein that binds viral RNA for encapsidation and has potential roles in host cell processes. This study characterised the N protein from a highly virulent North American strain of porcine reproductive and respiratory syndrome virus (PRRSV). The association with viral RNA was mapped to defined motifs on the N protein. The results indicated that disulphide bridge formation played a key role in RNA binding, offering an explanation why infectious virus cannot be rescued if cysteine residues are mutated, and that multiple sites may promote RNA binding.