Pathogenesis and control of the Chinese highly pathogenic porcine reproductive and respiratory syndrome virus

Han, Jun; Zhou, Lei; Ge, Xinna; Guo, Xin; Yang, Hanchun

doi:10.1016/j.vetmic.2017.02.020

Cited by 136 publications

(88 citation statements)

References 208 publications

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“…Since 2013, several field PRRSV isolates in China have been found to share high nucleotide similarity to a group of strains represented by NADC30, a type 2 PRRSV that was previously reported in USA in 2008 (Brockmeier et al 2012;Zhou et al 2015;Li et al 2016). Although the virulence of NADC30-like strains is relatively mild, they are now starting to recombine with the HP-PRRSV, making the PRRSV control in China more complex (Han et al 2017;Tian 2017).…”

Section: Introductionmentioning

confidence: 90%

“…Porcine reproductive and respiratory syndrome (PRRS) is an economically important swine disease characterized by severe reproductive failure in sows and respiratory distress in piglets and growing pigs and represents a major threat to the worldwide swine industry (Corzo et al 2010;Han et al 2017). It is estimated to cost the pork producers at least $600 million annually in North America with comparative losses in most other countries (Neumann et al 2005).…”

Section: Introductionmentioning

confidence: 99%

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Identification of Nonstructural Protein 8 as the N-Terminus of the RNA-Dependent RNA Polymerase of Porcine Reproductive and Respiratory Syndrome Virus

Liu

Chai

et al. 2018

Virol. Sin.

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Porcine reproductive and respiratory syndrome virus (PRRSV) is a member within the family Arteriviridae of the order Nidovirales. Replication of this positive-stranded RNA virus within the host cell involves expression of viral replicase proteins encoded by two ORFs, namely ORF1a and ORF1b. In particular, translation of ORF1b depends on a -1-ribosomal frameshift strategy. Thus, nonstructural protein 9 (nsp9), the first protein within ORF1b that specifies the function of the viral RNA-dependent RNA polymerase, is expressed as the C-terminal extension of nsp8, a small nsp that is encoded by ORF1a. However, it has remained unclear whether the mature form of nsp9 in virus-infected cells still retains nsp8, addressing which is clearly critical to understand the biological function of nsp9. By taking advantage of specific antibodies to both nsp8 and nsp9, we report the following findings. (1) In infected cells, PRRSV nsp9 was identified as a major product with a size between 72 and 95 kDa (72-95 KDa form), which exhibited the similar mobility on the gel to the in vitro expressed nsp8-9 ORF1b , but not the ORF1b-coded portion (nsp9 ORF1b ). (2) The antibodies to nsp8, but not to nsp7 or nsp10, could detect a major product that had the similar mobility to the 72-95 KDa form of nsp9. Moreover, nsp9 could be co-immunoprecipitated by antibodies to nsp8, and vice versa. (3) Neither nsp4 nor nsp2 PLP2 was able to cleave nsp8-nsp9 in vitro. Together, our studies provide experimental evidence to suggest that nsp8 is an N-terminal extension of nsp9. Our findings here paves way for further charactering the biological function of PRRSV nsp9.

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Section: Introductionmentioning

confidence: 90%

Section: Introductionmentioning

confidence: 99%

Identification of Nonstructural Protein 8 as the N-Terminus of the RNA-Dependent RNA Polymerase of Porcine Reproductive and Respiratory Syndrome Virus

Liu

Chai

et al. 2018

Virol. Sin.

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“…The serum, lung and lymph gland were used to detect the viral loads Y. Chen, et al Veterinary Microbiology 231 (2019) 226-231 (Han et al, 2017). In this experiment, the serum of every piglet was collected at 3, 7, 10, 14 and 21 dpi.…”

Section: The Phosphorylation Of the N Protein Affected Prrsv Replicatmentioning

confidence: 99%

The phosphorylation of the N protein could affect PRRSV virulence in vivo

Yao

et al. 2019

Veterinary Microbiology

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A B S T R A C TThe porcine respiratory and reproductive syndrome virus (PRRSV) nucleocapsid (N) protein is a multiphosphorylated protein.It has been proved that the phosphorylation of N protein could regulate the growth ability of PRRSV in Marc-145 cells. However, further investigation is needed to determine whether phosphorylation of the N protein could affect PRRSV virulence in piglets. In this study, we confirmed that the mutations could impair PRRSV replication ability in porcine primary macrophages (PAMs) as they did in Marc-145 cells. The animal experiments suggested that the pathogenicity of the mutated virus (A105-120) was significantly reduced compared with parent strain (XH-GD). Our results suggested that the phosphorylation of the N protein contributes to virus replication and virulence. This study is the first to identify a specific modification involved in PRRSV pathogenicity. Mutation of PTMs sites is also a novel way to attenuate PRRSV virulence. The mutations could be a marker in a vaccine. In conclusion, our study will improve our understanding of the molecular mechanisms of PRRSV pathogenicity.

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“…In 2006, a highly pathogenic porcine reproductive and respiratory syndrome virus (HP-PRRSV) emerged and prevailed in mainland China, resulting in devastating damage to swine production (Tian et al, 2007). Currently, HP-PRRSV causes high morbidity and high mortality in infected pigs of all ages and has remained a major threat to the swine producers in China and surrounding countries (Han et al, 2017). Porcine epidemic diarrhea virus (PEDV), a member of the genus Alpha-coronavirus (Song and Park, 2012), was first identified in the 1980s in China (Xuan et al, 1984).…”

Section: Introductionmentioning

confidence: 99%

“…As RNA viruses, PRRSV and PEDV are prone to mutation under selective pressures in the field, and this may cause the frequent appearances of new variant strains Han et al, 2017). Moreover, current commercial vaccination approaches against PRRSV and PEDV are only partially effective Du et al, 2017a,b).…”

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confidence: 99%

Identification of two antiviral inhibitors targeting 3C-like serine/3C-like protease of porcine reproductive and respiratory syndrome virus and porcine epidemic diarrhea virus

Shi

Lei

et al. 2018

Veterinary Microbiology

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Porcine reproductive and respiratory syndrome virus (PRRSV) and porcine epidemic diarrhea virus (PEDV) are highly virulent and contagious porcine pathogens that cause tremendous economic losses to the swine industry worldwide. Currently, there is no effective treatment for PRRSV and PEDV, and commercial vaccines do not induce sterilizing immunity. In this study, we screened a library of 1000 compounds and identified two specific inhibitors, designated compounds 2 and 3, which target the PRRSV 3C-like serine protease (3CLSP). First, we evaluated the inhibitory effects of compounds 2 and 3 on PRRSV 3CLSP activity. Next, we determined the anti-PRRSV capacity of compounds 2 and 3 in MARC-145 cells and obtained EC and CC values of 57μM (CC=479.9μM) and 56.8μM (CC=482.8μM), respectively. Importantly, compounds 2 and 3 also targeted the PEDV 3C-like protease (3CL protease) and inhibited PEDV replication, showing EC and CC values of 100μM (CC=533.8μM) and 57.9μM (CC=522.3μM), respectively. Finally, our results indicated that the active sites (His39 in 3CLSP and His41 in 3CL protease) were conservative, and contacted compounds 2 and 3 via hydrogen bonds and hydrophobic forces in the putative substrate-binding models. In summary, compounds 2 and 3 exhibit broad-spectrum antiviral activity and may facilitate the development of antiviral drugs against PRRSV and PEDV.

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Pathogenesis and control of the Chinese highly pathogenic porcine reproductive and respiratory syndrome virus

Cited by 136 publications

References 208 publications

Identification of Nonstructural Protein 8 as the N-Terminus of the RNA-Dependent RNA Polymerase of Porcine Reproductive and Respiratory Syndrome Virus

Identification of Nonstructural Protein 8 as the N-Terminus of the RNA-Dependent RNA Polymerase of Porcine Reproductive and Respiratory Syndrome Virus

The phosphorylation of the N protein could affect PRRSV virulence in vivo

Identification of two antiviral inhibitors targeting 3C-like serine/3C-like protease of porcine reproductive and respiratory syndrome virus and porcine epidemic diarrhea virus

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