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

Abstract

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.

Resolution of the cellular proteome of the nucleocapsid protein from a highly pathogenic isolate of porcine reproductive and respiratory syndrome virus identifies PARP-1 as a cellular target whose interaction is critical for virus biology

“…N protein was expressed with a C-terminal His-tag ( Jourdan et al, 2012b ) in BL21(DE3)pLyS cells ( Fig. 1 A, left panel).…”

Cecropin P1 inhibits porcine reproductive and respiratory syndrome virus by blocking attachment

“…Previous studies have shown that PRRSV is internalized from the Marc-145 cell surface within 3–6 h [ 14 , 15 ]. Therefore, we investigated whether CP1 also acts at the entry stage of the viral life cycle.…”

Inhibitory Activity and Molecular Mechanism of Protegrin-1 against Porcine Reproductive and Respiratory Syndrome virus in vitro

“…These data suggested that PG-1 could strongly inhibit the early stage of Li10 life cycle. Previous studies showed that PRRSV was internalized from the Marc-145 cells surface in 3-6 h [38,39]. Therefore, we examined whether PG-1 could also block the late stage of virus life cycle by TCID 50 and western blot analysis.…”