scholarly journals Molecular Characterization of Porcine Epidemic Diarrhea Virus and Its New Genetic Classification Based on the Nucleocapsid Gene

Viruses ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 790
Author(s):  
Sung-Jae Kim ◽  
Van-Giap Nguyen ◽  
Thi-My-Le Huynh ◽  
Yong-Ho Park ◽  
Bong-Kyun Park ◽  
...  
Keyword(s):  
B Cell ◽  
Porcine Epidemic Diarrhea Virus ◽  
Cell Epitope ◽  
N Gene ◽  
Swine Industry ◽  
Genetic Classification ◽  
Nucleocapsid Gene ◽  
Diarrhea Virus ◽  
B Cell Epitope ◽  
Porcine Epidemic Diarrhea

Porcine epidemic diarrhea virus (PEDV) causes continuous, significant damage to the swine industry worldwide. By RT-PCR-based methods, this study demonstrated the ongoing presence of PEDV in pigs of all ages in Korea at the average detection rate of 9.92%. By the application of Bayesian phylogenetic analysis, it was found that the nucleocapsid (N) gene of PEDV could evolve at similar rates to the spike (S) gene at the order of 10−4 substitutions/site/year. Based on branching patterns of PEDV strains, three main N gene-base genogroups (N1, N2, and N3) and two sub-genogroups (N3a, N3b) were proposed in this study. By analyzing the antigenic index, possible antigenic differences also emerged in both the spike and nucleocapsid proteins between the three genogroups. The antigenic indexes of genogroup N3 strains were significantly lower compared with those of genogroups N1 and N2 strains in the B-cell epitope of the nucleocapsid protein. Similarly, significantly lower antigenic indexes in some parts of the B-cell epitope sequences of the spike protein (COE, S1D, and 2C10) were also identified. PEDV mutants derived from genetic mutations of the S and N genes may cause severe damage to swine farms by evading established host immunities.

scholarly journals Identification of a novel B-cell epitope in the spike protein of porcine epidemic diarrhea virus

2020 ◽  
Vol 17 (1) ◽  
Author(s):  
Ning Kong ◽  
Qiong Meng ◽  
Yajuan Jiao ◽  
Yongguang Wu ◽  
Yewen Zuo ◽  
...  
Keyword(s):  
B Cell ◽  
Porcine Epidemic Diarrhea Virus ◽  
Cell Epitope ◽  
Spike Protein ◽  
Diarrhea Virus ◽  
B Cell Epitope ◽  
Porcine Epidemic Diarrhea

scholarly journals Identification of a conserved linear B-cell epitope in the M protein of porcine epidemic diarrhea virus

2012 ◽  
Vol 9 (1) ◽  
pp. 225 ◽  
Author(s):  
Zhibang Zhang ◽  
Jianfei Chen ◽  
Hongyan Shi ◽  
Xiaojin Chen ◽  
Da Shi ◽  
...  
Keyword(s):  
B Cell ◽  
Porcine Epidemic Diarrhea Virus ◽  
Cell Epitope ◽  
M Protein ◽  
Diarrhea Virus ◽  
B Cell Epitope ◽  
Porcine Epidemic Diarrhea ◽  
Linear B

scholarly journals The interactome of porcine epidemic diarrhea virus nucleocapsid protein

2019 ◽  
Author(s):  
Min Tan ◽  
Guofei Ding ◽  
Xinna Cai ◽  
Shengliang Cao ◽  
Fangyuan Cong ◽  
...  
Keyword(s):  
Porcine Epidemic Diarrhea Virus ◽  
Cellular Proteins ◽  
Economic Losses ◽  
N Gene ◽  
Effective Vaccine ◽  
Label Free ◽  
Swine Industry ◽  
N Protein ◽  
Diarrhea Virus ◽  
Porcine Epidemic Diarrhea

Abstract Background Many viral proteins specifically interact with cellular proteins to facilitate virus replication. Understanding these interactions can decipher the viral infection mechanism and provide potential targets for antiviral therapy. Porcine epidemic diarrhea virus (PEDV), the agent of PED, causes numerous economic losses for the swine industry each year. Till now, no effective vaccine or drugs are available to contain this disease. As a result, it is critical urgent to elucidate the PEDV interactome. The nucleocapsid (N) of PEDV plays an important role in viral replication. Results In this study, the N gene was cloned into pEGFP-C1 and transfected into 293T cells. The interactome of N was elucidated by label-free mass spectrometry. A total of 125 cellular proteins interacting with PEDV N protein were discovered, of which 4 cellular proteins, DHX9, NCL, KAP1, TCEA1, were confirmed by pull down, immunoprecipitation, and co-localization. Conclusions The interactome of N protein supplied a powerful tool to explore the role of N in PEDV infection and therapeutic targets.

scholarly journals Immunodominant and neutralizing linear B cell epitopes spanning the spike and membrane proteins of Porcine Epidemic Diarrhea Virus

2021 ◽  
Author(s):  
Kanokporn Polyiam ◽  
Marasri Ruengjitchatchawalya ◽  
Phenjun Mekvichitsaeng ◽  
Kampon Kaeoket ◽  
Tawatchai Hoonsuwan ◽  
...  
Keyword(s):  
B Cell ◽  
Porcine Epidemic Diarrhea Virus ◽  
M Protein ◽  
B Cell Epitopes ◽  
Diarrhea Virus ◽  
M Proteins ◽  
Porcine Epidemic Diarrhea ◽  
Neutralizing Epitopes ◽  
Immunodominant Epitopes ◽  
Linear B

AbstractPorcine Epidemic Diarrhea Virus (PEDV) is the causative agent of PED, an enteric disease that causes high mortality rates in piglets. PEDV is an alphacoronavirus that has high genetic diversity. Insights into neutralizing B cell epitopes of all genetically diverse PEDV strains are of importance, particularly for designing a vaccine that can provide broad protection against PEDV. In this work, we aimed to explore the landscape of linear B cell epitopes on the spike (S) and membrane (M) proteins of global PEDV strains. All amino acid sequences of the PEDV S and M proteins were retrieved from the NCBI database and grouped. Immunoinformatics-based methods were next developed and used to identify putative linear B cell epitopes from 14 and 5 consensus sequences generated from distinct groups of the S and M proteins, respectively. ELISA testing predicted peptides with PEDV-positive sera revealed 9 novel immunodominant epitopes on the S protein. Importantly, 7 of these novel immunodominant epitopes and other subdominant epitopes were demonstrated to be neutralizing epitopes by neutralization-inhibition assay. Additionally, our study shows the first time that M protein is also the target of neutralizing antibodies as 7 neutralizing epitopes in the M protein were identified. Conservancy analysis revealed that epitopes in the S1 subunit are more variable than those in the S2 subunit and M protein. In this study, we offer the immunoinformatics approach for linear B cell epitope identification and a more complete profile of linear B cell epitopes across the PEDV S and M proteins, which may contribute to the development of a greater PEDV vaccine as well as peptide-based immunoassays.

scholarly journals Pathogenicity and immunogenicity of a new strain of porcine epidemic diarrhea virus containing a novel deletion in the N gene

2020 ◽  
Vol 240 ◽  
pp. 108511 ◽  
Author(s):  
Xian-Wei Wang ◽  
Mi Wang ◽  
Jing Zhan ◽  
Qian-Yu Liu ◽  
Lin-lin Fang ◽  
...  
Keyword(s):  
Porcine Epidemic Diarrhea Virus ◽  
N Gene ◽  
Diarrhea Virus ◽  
Porcine Epidemic Diarrhea

scholarly journals Isolation and Identification of a Recombinant Porcine Epidemic Diarrhea Virus With a Novel Insertion in S1 Domain

2021 ◽  
Vol 12 ◽  
Author(s):  
Dongliang Li ◽  
Yongtao Li ◽  
Yunchao Liu ◽  
Yumei Chen ◽  
Wenqiang Jiao ◽  
...  
Keyword(s):  
Porcine Epidemic Diarrhea Virus ◽  
Driving Forces ◽  
Viral Evolution ◽  
Animal Experiments ◽  
Central China ◽  
N Gene ◽  
Clinical Samples ◽  
Isolation And Identification ◽  
Diarrhea Virus ◽  
Porcine Epidemic Diarrhea

Porcine epidemic diarrhea virus (PEDV) is the major pathogen that causes diarrhea and high mortality in newborn piglets with devastating impact to the pig industry. Recombination and mutation are the main driving forces of viral evolution and genetic diversity of PEDV. In 2016, an outbreak of diarrhea in piglets occurred in an intensive pig farm in Central China. A novel PEDV isolate (called HNAY) was successfully isolated from clinical samples. Sequence analysis and alignment showed that HNAY possessed 21-nucleotide (nt) insertion in its S1 gene, which has never been reported in other PEDV isolates. Moreover, the sequence of the insertion was identical with the sequence fragment in PEDV N gene. Notably, the HNAY strain exhibited two unique mutations (T500A and L521Y) in the neutralizing epitopes of the S1 protein that were different from those of other PEDV variant strains and CV777-based vaccine strains. Additionally, PEDV HNAY might be derived from a natural recombination between two Chinese variant PEDV strains. Animal experiments demonstrated that HNAY displayed higher pathogenicity compared with two other clinical isolates. This study lays the foundation for better understanding of the genetic evolution and molecular pathogenesis of PEDV.

scholarly journals The trypsin-enhanced infection of porcine epidemic diarrhea virus is determined by the S2 subunit of the spike glycoprotein

2021 ◽  
Author(s):  
Yubei Tan ◽  
Limeng Sun ◽  
Gang Wang ◽  
Yuejun Shi ◽  
Wanyu Dong ◽  
...  
Keyword(s):  
Porcine Epidemic Diarrhea Virus ◽  
Cleavage Site ◽  
Vaccine Development ◽  
Syncytium Formation ◽  
Reverse Genetic System ◽  
Site Mutation ◽  
Swine Industry ◽  
S Protein ◽  
Diarrhea Virus ◽  
Porcine Epidemic Diarrhea

Porcine epidemic diarrhea virus (PEDV) is an enteric pathogen in the swine industry, causing high mortality in neonatal piglets. Efficient PEDV infection usually relies on the presence of trypsin, yet the mechanism of trypsin dependency is ambiguous. Here, we identified two PEDV strains, trypsin-enhanced YN200 and trypsin-independent DR13, in which the spike (S) protein of YN200 exhibits a stronger ability to induce syncytium formation and cleaved by trypsin than that of DR13. Using a full-length infectious YN200 cDNA clone, we confirmed that the S protein is a trypsin dependency determinant by comparison of rYN200 and rYN200-SDR13. To explore the trypsin-associated sites of the YN200 S protein, we then constructed a series of mutations adjacent to the fusion peptide. The results show that the putative S2’ cleavage site (R892G) is not the determinant for virus trypsin dependency. Hence, we generated viruses carrying chimeric S proteins: the S1 subunit, S2 subunit, and S2720∼892 aa domain (NS2’) were individually replaced by the corresponding DR13 sequences. Intriguingly, only the S2 substitution, not the S1 or NS2’ substitutions, provides trypsin-independent growth of YN200. Additionally, the NS2’ recombinant virus significantly abrogated effective infection, indicating a vital role for NS2’ in viral entry. These findings suggest that the trypsin dependency of PEDV is mainly controlled by mutations in the S2 subunit rather than directly trypsin cleavage site. Importance With the emergence of new variants, PEDV remains a major problem in the global swine industry. Efficient PEDV infection usually requires trypsin, while the mechanism of trypsin dependency is complex. Here, we used two PEDV strains, trypsin-enhanced YN200 and trypsin-independent DR13, and results showed that the S protein determined PEDV trypsin dependency by using a reverse genetic system of YN200. The S2 subunit was verified as the main portion of PEDV trypsin dependency, though the putative S2’ site mutation cannot render trypsin-independent growth of YN200. Finally, these results provide some different insight to the PEDV trypsin dependency and might inspire vaccine development.

scholarly journals Single-Particle Tracking Porcine Epidemic Diarrhea Virus Moving along Microtubules in Living Cells

Proceedings ◽  
2020 ◽  
Vol 50 (1) ◽  
pp. 124
Author(s):  
Yangyang Li ◽  
Wei Hou ◽  
Jian Wang ◽  
Fei Liu
Keyword(s):  
Particle Tracking ◽  
Single Particle ◽  
Porcine Epidemic Diarrhea Virus ◽  
Living Cells ◽  
Single Particle Tracking ◽  
Microtubule Organizing Center ◽  
Swine Industry ◽  
Diarrhea Virus ◽  
Organizing Center ◽  
Porcine Epidemic Diarrhea

Porcine epidemic diarrhea virus (PEDV), a member of the genus Alphacoronavirus, has caused severe damage to the swine industry. Although viruses are believed to hijack the microtubule-based transport system, the exact manner of PEDV moving along microtubules has not been fully characterized. In this study, PEDV was labeled with quantum dots which have great brightness and photostability. By using quantum dot-labeled PEDV and single-particle tracking, we were able to systematically dissect the dynamic behaviors of PEDV moving along the microtubules in living cells. We found that PEDVs maintained a restricted motion mode with a relatively stable speed in the cell membrane region while displaying a slow–fast–slow velocity pattern with different motion modes in the cell cytoplasm region and near the microtubule-organizing center. The return movements of small amounts of PEDVs were also observed in living cells. Collectively, our work is crucial for understanding the movement of PEDV in living cells; the proposed work also provides important references for further analysis and studies of the infection mechanism of PEDV.

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