scholarly journals Structural Analysis of Porcine Reproductive and Respiratory Syndrome Virus Non-structural Protein 7α (NSP7α) and Identification of Its Interaction with NSP9

2017 ◽  
Vol 8 ◽  
Author(s):  
Jiaping Chen ◽  
Xiaodong Xu ◽  
Hu Tao ◽  
Yuan Li ◽  
Hao Nan ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Respiratory Syndrome Virus ◽  
Structural Protein

scholarly journals A 10-kDa Structural Protein of Porcine Reproductive and Respiratory Syndrome Virus Encoded by ORF2b

Virology ◽  
2001 ◽  
Vol 287 (1) ◽  
pp. 183-191 ◽  
Author(s):  
Wai-Hong Wu ◽  
Ying Fang ◽  
Rachel Farwell ◽  
Melissa Steffen-Bien ◽  
Raymond R.R Rowland ◽  
...  
Keyword(s):  
Respiratory Syndrome Virus ◽  
Structural Protein

scholarly journals Antiviral Mechanism of Tea Polyphenols on Porcine Reproductive and Respiratory Syndrome Virus

2020 ◽  
Author(s):  
Wenjuan Dong ◽  
Xun Wang ◽  
Xiaoxiao Zhang ◽  
Zhenbang Zhu ◽  
Yaosheng Chen ◽  
...  
Keyword(s):  
Antiviral Agent ◽  
Tea Polyphenols ◽  
Respiratory Syndrome Virus ◽  
Structural Protein ◽  
Viral Attachment ◽  
New Horizons ◽  
Pre Treatment ◽  
Transcription Complexes ◽  
Main Components ◽  
And Control

Abstract Background: Neither inactivated vaccine nor attenuated vaccine can effectively prevent and control the infection and spread of porcine reproductive and respiratory syndrome virus (PRRSV). Therefore, it is necessary to broaden new horizons and to conceive effective preventive strategies. Tea polyphenols (TPP) are polyphenol in tea. The main components of TPP are catechins and their derivatives. TPP has many physiological activities and has certain antiviral and antifungal effects. But whether TPP owns anti-PRRSV activity remains unclear. Results: We found that TPP effectively inhibited PRRSV replication in Marc-145 cells by suppressing viral attachment and internalization. TPP exhibited a potent anti-PRRSV effect regardless of its pre-treatment or post-treatment. In addition, we demonstrated that TPP restrained PRRSV-induced p65 entry into the nucleus to suppress the activation of the NF-κB signaling pathway, which ultimately leads to the inhibition of the expression of inflammatory cytokines. Furthermore, TPP limited the synthesis of viral non-structural protein 2 (nsp2), the core component of viral replication transcription complexes, which may contribute to the inhibition of viral RNA replication. Conclusions: TPP has the potential to develop into an effective antiviral agent for PRRSV prevention and control in the future.

scholarly journals Understanding COVID-19 Pathogenesis: A Drug-Repurposing Effort to Disrupt Nsp-1 Binding to Export Machinery Receptor Complex

Pathogens ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 1634
Author(s):  
Sona Vasudevan ◽  
James N. Baraniuk
Keyword(s):  
Structural Analysis ◽  
Nuclear Export ◽  
Messenger Rna ◽  
Drug Repurposing ◽  
Nuclear Pore ◽  
Receptor Complex ◽  
Structural Protein ◽  
Gonadotropin Secretion ◽  
Approved Drugs ◽  
Nuclear Rna Export

Non-structural protein 1 (Nsp1) is a virulence factor found in all beta coronaviruses (b-CoVs). Recent studies have shown that Nsp1 of SARS-CoV-2 virus interacts with the nuclear export receptor complex, which includes nuclear RNA export factor 1 (NXF1) and nuclear transport factor 2-like export factor 1 (NXT1). The NXF1–NXT1 complex plays a crucial role in the transport of host messenger RNA (mRNA). Nsp1 interferes with the proper binding of NXF1 to mRNA export adaptors and its docking to the nuclear pore complex. We propose that drugs targeting the binding surface between Nsp1 and NXF1–NXT1 may be a useful strategy to restore host antiviral gene expression. Exploring this strategy forms the main goals of this paper. Crystal structures of Nsp1 and the heterodimer of NXF1–NXT1 have been determined. We modeled the docking of Nsp1 to the NXF1–NXT1 complex, and discovered repurposed drugs that may interfere with this binding. To our knowledge, this is the first attempt at drug-repurposing of this complex. We used structural analysis to screen 1993 FDA-approved drugs for docking to the NXF1–NXT1 complex. The top hit was ganirelix, with a docking score of −14.49. Ganirelix competitively antagonizes the gonadotropin releasing hormone receptor (GNRHR) on pituitary gonadotrophs, and induces rapid, reversible suppression of gonadotropin secretion. The conformations of Nsp1 and GNRHR make it unlikely that they interact with each other. Additional drug leads were inferred from the structural analysis of this complex, which are discussed in the paper. These drugs offer several options for therapeutically blocking Nsp1 binding to NFX1–NXT1, which may normalize nuclear export in COVID-19 infection.

scholarly journals Identification of amino acid residues important for anti-IFN activity of porcine reproductive and respiratory syndrome virus non-structural protein 1

Virology ◽  
2012 ◽  
Vol 433 (2) ◽  
pp. 431-439 ◽  
Author(s):  
Lalit K. Beura ◽  
Sakthivel Subramaniam ◽  
Hiep L.X. Vu ◽  
Byungjoon Kwon ◽  
Asit K. Pattnaik ◽  
...  
Keyword(s):  
Amino Acid ◽  
Respiratory Syndrome Virus ◽  
Amino Acid Residues ◽  
Structural Protein
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