Biophysical characterisation of the nucleocapsid protein from a highly pathogenic porcine reproductive and respiratory syndrome virus strain.
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.
Institute of Molecular and Cellular Biology, Faculty of Biological Sciences, Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 6JP, UK.
Stefanie S
SS
Jourdan
Fernando A
FA
Osorio
Julian A
JA
Hiscox
D000409:Alanine / Q000235:genetics / Q000378:metabolism; D019943:Amino Acid Substitution; D000818:Animals; D003545:Cysteine / Q000235:genetics / Q000378:metabolism*; D019590:Nucleocapsid Proteins / Q000235:genetics / Q000378:metabolism*; D019318:Porcine Reproductive and Respiratory Syndrome / Q000821:virology*; D019316:Porcine respiratory and reproductive syndrome virus / Q000235:genetics / Q000472:pathogenicity*; D012367:RNA, Viral / Q000378:metabolism*; D013552:Swine
D019590:Nucleocapsid Proteins; D012367:RNA, Viral; D003545:Cysteine; D000409:Alanine