scholarly journals Crystallization and preliminary crystallographic study ofPorcine epidemic diarrhea virusmain protease in complex with an inhibitor

2014 ◽  
Vol 70 (12) ◽  
pp. 1608-1611
Author(s):  
Yusheng Tan ◽  
Fenghua Wang ◽  
Xia Chen ◽  
Jinshan Wang ◽  
Qi Zhao ◽  
...  
Keyword(s):  
Porcine Epidemic Diarrhea Virus ◽  
Antiviral Drug ◽  
Proteolytic Processing ◽  
Genome Replication ◽  
Virus Shedding ◽  
Cell Parameters ◽  
Diarrhea Virus ◽  
Main Protease ◽  
Porcine Epidemic Diarrhea ◽  
Complex Crystals

Porcine epidemic diarrhea virus(PEDV) mainly infects neonatal pigs, resulting in significant morbidity and mortality. Owing to problems such as long periods of virus shedding, existing vaccines cannot provide complete protection from PEDV infection. The PEDV genome encodes two polyprotein precursors required for genome replication and transcription. Each polyprotein undergoes extensive proteolytic processing, resulting in functional subunits. This process is mainly mediated by its genome-encoded main protease, which is an attractive target for antiviral drug design. In this study, the main protease ofPorcine epidemic diarrhea virusin complex with a Michael acceptor was crystallized. The complex crystals diffracted to 2.5 Å resolution and belonged to space groupR3, with unit-cell parametersa= 175.3,b= 175.3,c= 58.7 Å. Two molecules were identified per asymmetric unit.

scholarly journals Crystallization and preliminary crystallographic study of human coronavirus NL63 main protease in complex with an inhibitor

2014 ◽  
Vol 70 (8) ◽  
pp. 1068-1071 ◽  
Author(s):  
Fenghua Wang ◽  
Yusheng Tan ◽  
Huiyan Li ◽  
Xia Chen ◽  
Jinshan Wang ◽  
...  
Keyword(s):  
Antiviral Drug ◽  
Proteolytic Processing ◽  
Genome Replication ◽  
Asymmetric Unit ◽  
Unit Cell Parameters ◽  
Human Coronavirus ◽  
Cell Parameters ◽  
Crystallographic Study ◽  
Main Protease ◽  
Complex Crystals

Human coronavirus NL63 mainly infects younger children and causes cough, fever, rhinorrhoea, bronchiolitis and croup. It encodes two polyprotein precursors required for genome replication and transcription. Each polyprotein undergoes extensive proteolytic processing, resulting in functional subunits. This process is mainly mediated by its genome-encoded main protease, which is an attractive target for antiviral drug design. In this study, the main protease of human coronavirus NL63 was crystallized in complex with a Michael acceptor. The complex crystals diffracted to 2.85 Å resolution and belonged to space groupP41212, with unit-cell parametersa=b= 87.2,c= 212.1 Å. Two molecules were identified per asymmetric unit.

scholarly journals Crystallization and preliminary crystallographic study ofFeline infectious peritonitis virusmain protease in complex with an inhibitor

2014 ◽  
Vol 70 (12) ◽  
pp. 1612-1615 ◽  
Author(s):  
Jinshan Wang ◽  
Fenghua Wang ◽  
Yusheng Tan ◽  
Xia Chen ◽  
Qi Zhao ◽  
...  
Keyword(s):  
Antiviral Drug ◽  
Proteolytic Processing ◽  
Genome Replication ◽  
Domestic Cats ◽  
Unit Cell Parameters ◽  
Feline Infectious Peritonitis ◽  
Cell Parameters ◽  
Crystallographic Study ◽  
Main Protease ◽  
Complex Crystals

Feline infectious peritonitis virus(FIPV) causes a lethal systemic granulomatous disease in wild and domestic cats around the world. Currently, no effective vaccines or drugs have been developed against it. As a member of the genusAlphacoronavirus, FIPV encodes two polyprotein precursors required for genome replication and transcription. Each polyprotein undergoes extensive proteolytic processing, resulting in functional subunits. This process is mainly mediated by its genome-encoded main protease, which is an attractive target for antiviral drug design. In this study, the main protease of FIPV in complex with a Michael acceptor-type inhibitor was crystallized. The complex crystals diffracted to 2.5 Å resolution and belonged to space groupI422, with unit-cell parametersa= 112.3,b= 112.3,c= 102.1 Å. There is one molecule per asymmetric unit.

scholarly journals Structural Basis for Inhibiting Porcine Epidemic Diarrhea Virus Replication with the 3C-Like Protease Inhibitor GC376

Viruses ◽  
2020 ◽  
Vol 12 (2) ◽  
pp. 240 ◽  
Author(s):  
Gang Ye ◽  
Xiaowei Wang ◽  
Xiaohan Tong ◽  
Yuejun Shi ◽  
Zhen F. Fu ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Porcine Epidemic Diarrhea Virus ◽  
Catalytic Mechanism ◽  
Antiviral Drug ◽  
Structural Basis ◽  
Transmissible Gastroenteritis Virus ◽  
Diarrhea Virus ◽  
Porcine Epidemic Diarrhea ◽  
Transmissible Gastroenteritis ◽  
Viral Polyprotein

Porcine epidemic diarrhea virus (PEDV), being highly virulent and contagious in piglets, has caused significant damage to the pork industries of many countries worldwide. There are no commercial drugs targeting coronaviruses (CoVs), and few studies on anti-PEDV inhibitors. The coronavirus 3C-like protease (3CLpro) has a conserved structure and catalytic mechanism and plays a key role during viral polyprotein processing, thus serving as an appealing antiviral drug target. Here, we report the anti-PEDV effect of the broad-spectrum inhibitor GC376 (targeting 3Cpro or 3CLpro of viruses in the picornavirus-like supercluster). GC376 was highly effective against the PEDV 3CLpro and exerted similar inhibitory effects on two PEDV strains. Furthermore, the structure of the PEDV 3CLpro in complex with GC376 was determined at 1.65 Å. We elucidated structural details and analyzed the differences between GC376 binding with the PEDV 3CLpro and GC376 binding with the transmissible gastroenteritis virus (TGEV) 3CLpro. Finally, we explored the substrate specificity of PEDV 3CLpro at the P2 site and analyzed the effects of Leu group modification in GC376 on inhibiting PEDV infection. This study helps us to understand better the PEDV 3CLpro substrate specificity, providing information on the optimization of GC376 for development as an antiviral therapeutic against coronaviruses.

scholarly journals Porcine Epidemic Diarrhea Virus Shedding and Antibody Response in Swine Farms: A Longitudinal Study

2016 ◽  
Vol 7 ◽  
Author(s):  
Cristina Bertasio ◽  
Enrico Giacomini ◽  
Massimiliano Lazzaro ◽  
Simona Perulli ◽  
Alice Papetti ◽  
...  
Keyword(s):  
Longitudinal Study ◽  
Antibody Response ◽  
Porcine Epidemic Diarrhea Virus ◽  
Virus Shedding ◽  
Diarrhea Virus ◽  
Swine Farms ◽  
Porcine Epidemic Diarrhea

Michael Acceptor-Based Peptidomimetic Inhibitor of Main Protease from Porcine Epidemic Diarrhea Virus

2017 ◽  
Vol 60 (7) ◽  
pp. 3212-3216 ◽  
Author(s):  
Fenghua Wang ◽  
Cheng Chen ◽  
Kailin Yang ◽  
Yang Xu ◽  
Xiaomei Liu ◽  
...  
Keyword(s):  
Porcine Epidemic Diarrhea Virus ◽  
Diarrhea Virus ◽  
Main Protease ◽  
Michael Acceptor ◽  
Porcine Epidemic Diarrhea

Use of an internal control in a quantitative RT-PCR assay for quantitation of porcine epidemic diarrhea virus shedding in pigs

2006 ◽  
Vol 133 (1) ◽  
pp. 27-33 ◽  
Author(s):  
Dae-Sub Song ◽  
Bo-Kyu Kang ◽  
Sang-Sun Lee ◽  
Jeong-Sun Yang ◽  
Hyoung-Joon Moon ◽  
...  
Keyword(s):  
Internal Control ◽  
Porcine Epidemic Diarrhea Virus ◽  
Rt Pcr ◽  
Pcr Assay ◽  
Virus Shedding ◽  
Diarrhea Virus ◽  
Porcine Epidemic Diarrhea

scholarly journals Characteristics and Pathogenicity of the Cell-Adapted Attenuated Porcine Epidemic Diarrhea Virus of the Non-S INDEL Cluster

Pathogens ◽  
2021 ◽  
Vol 10 (11) ◽  
pp. 1479
Author(s):  
Thi Thu Hang Vu ◽  
Minjoo Yeom ◽  
Hyoungjoon Moon ◽  
Thi Nhan Tran ◽  
Van Phan Le ◽  
...  
Keyword(s):  
Porcine Epidemic Diarrhea Virus ◽  
High Titer ◽  
Vaccine Strategy ◽  
Live Attenuated Vaccine ◽  
Virus Shedding ◽  
Diarrhea Virus ◽  
Attenuated Vaccine ◽  
In Vivo Tests ◽  
Porcine Epidemic Diarrhea

The high antigenic diversity of porcine epidemic diarrhea virus (PEDV) means that porcine epidemic diarrhea (PED) is a challenge for the global pig industry. Understanding the circulation of the virus to determine an optimal vaccine strategy is important in controlling the disease. In this study, we describe the genetic diversity of circulating PEDV based on the full sequences of spike genes of eight positive samples collected in Vietnam since 2018. Additionally, we developed a live attenuated vaccine candidate from the cell-adapted PEDV2 strain, which was continuously passaged until level 103 in VERO-CCL81 cells. PEDV2-p103, which belongs to the emerging non-S INDEL cluster, exhibited low virus shedding, did not induce lesions in the small intestine of challenged piglets, and had a high titer in the VERO-CCL81 cell at 48 h post-infection. These results suggest that the PEDV2-p103 strain could be a potential oral attenuated vaccine, and its immunogenicity and efficacy should be further assessed through in vivo tests.

scholarly journals Caerin1.1 Suppresses the Growth of Porcine Epidemic Diarrhea Virus In Vitro via Direct Binding to the Virus

Viruses ◽  
2018 ◽  
Vol 10 (9) ◽  
pp. 507 ◽  
Author(s):  
Nan Guo ◽  
Bingzhou Zhang ◽  
Han Hu ◽  
Shiyi Ye ◽  
Fangzhou Chen ◽  
...  
Keyword(s):  
Antiviral Activity ◽  
Porcine Epidemic Diarrhea Virus ◽  
Antiviral Drug ◽  
Vero Cells ◽  
Economic Losses ◽  
Diarrhea Virus ◽  
Direct Binding ◽  
Porcine Epidemic Diarrhea ◽  
And Control

Porcine epidemic diarrhea (PED) has re-emerged in recent years and has already caused huge economic losses to the porcine industry all over the world. Therefore, it is urgent for us to find out efficient ways to prevent and control this disease. In this study, the antiviral activity of a cationic amphibian antimicrobial peptide Caerin1.1 against porcine epidemic diarrhea virus (PEDV) was evaluated by an in vitro system using Vero cells. We found that even at a very low concentration, Caerin1.1 has the ability to destroy the integrity of the virus particles to block the release of the viruses, resulting in a considerable decrease in PEDV infections. In addition, Caerin1.1 showed powerful antiviral activity without interfering with the binding progress between PEDV and the receptor of the cells, therefore, it could be used as a potential antiviral drug or as a microbicide compound for prevention and control of PEDV.

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