The structural biology of PRRSV

Abstract

Porcine reproductive and respiratory syndrome virus (PRRSV) is an enveloped, positive-sense single-stranded RNA virus belonging to the Arteriviridae family. Arteriviruses and coronaviruses are grouped together in the order Nidovirales, based on similarities in genome organization and expression strategy. Over the past decade, crystal structures of several viral proteins, electron microscopic studies of the virion, as well as biochemical and in vivo studies on protein-protein interactions have led to a greatly increased understanding of PRRSV structural biology. At this point, crystal structures are available for the viral proteases NSP1α, NSP1β and NSP4 and the nucleocapsid protein, N. The NSP1α and NSP1β structures have revealed additional non-protease domains that may be involved in modulation of host functions. The N protein forms a dimer with a novel fold so far only seen in PRRSV and other nidoviruses. Cryo-electron tomographic studies have shown the three-dimensional organization of the PRRSV virion and suggest that the viral nucleocapsid has an asymmetric, linear arrangement, rather than the isometric core previously described. Together, these studies have revealed a closer structural relationship between arteri- and coronaviruses than previously anticipated.

An infectious clone of the highly pathogenic porcine reproductive and respiratory syndrome virus: Topology of glycoprotein 3 (GP3) addressing the intrachain disulfide bonds

“…Transmembrane regions were also predicted using the TMHMM server (http://www.cbs. dtu.dk/services/TMHMM/), and two transmembrane regions were identified on the basis of our prediction results and previous report [31]. Models to reveal the interaction between the structural proteins were constructed based on reports [31,32] and our findings (Figure 6(a)) and the topological alteration of GP3 was constructed as shown in Figure 6(b) and (c).…”

“…dtu.dk/services/TMHMM/), and two transmembrane regions were identified on the basis of our prediction results and previous report [31]. Models to reveal the interaction between the structural proteins were constructed based on reports [31,32] and our findings (Figure 6(a)) and the topological alteration of GP3 was constructed as shown in Figure 6(b) and (c). For wild type GP3, the secondary structure prediction showed that 106 aa out of 254 aa in GP3 formed coils in the structure, which indicated that GP3 might be very flexible especially in ectodomain of the protein.…”

“…Particularly, numerous adult pigs and some pregnant sows have died as a result of infection, while in the previous occurrences of PRRSV infection, most of the fatal cases had Figure 6 The interaction model for structural proteins in the surface-protein complex and the topology prediction of GP3. (a) The preliminary model of GP3 interacted with other structural proteins summarized according to references [31,32]. For the sake of simplicity and convenience, the GPs were depicted as globular structures with the same colored lines spanning the viral membrane.…”

Expression of peptide nanoparticles containing a porcine reproductive and respiratory syndrome (PRRS) virus epitope in plants

“…The nucleocapsid protein (N) is encoded by ORF7. N is the major structural element within the PRRSV virion and forms disulfide-linked homodimers; It functions to package the viral genomic RNA and is the only known structural protein, which does not encode a transmembrane domain (Dokland, 2010).…”

Expression of porcine reproductive and respiratory syndrome virus (PRRSV) ORF7 gene and monoclonal antibody production

“…ORF1a와 ORF1b는 바이러스 복제와 전사에 필요한 14개의 비구조단백질을 coding한다 (Dokland, 2010). 피막을 가지고 있는 바이러스 입자 에는 3개의 중요한 단백, 즉 glycosylated envelope protein (GP5, 25 kDa), unglycosylated membrane protein (M, 18 kDa), 그리고 nucleocapsid protein (N, 15 kDa)…”