ArticleScientific reports2016
The Identification and Characterization of Two Novel Epitopes on the Nucleocapsid Protein of the Porcine Epidemic Diarrhea Virus.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 40 citations in OpenAlex.
- Identification of Novel B Cell Epitopes on the Nucleocapsid Protein of Porcine Epidemic Diarrhea Virus.Viruses · 2026Article
- Precise mapping of two conserved minimal epitopes on the nucleocapsid protein of porcine epidemic diarrhea virus.Frontiers in microbiology · 2026Article
- Identification and characterization of a novel linear B-cell epitope on nucleocapsid protein of porcine epidemic diarrhea virus.BMC veterinary research · 2025Article
- The integrin protein ITGβ1 effectively suppresses porcine epidemic diarrhea virus replication through facilitating MDA5 oligomerization and subsequent activation of the type I interferon signaling pathway.Journal of virology · 2025Article
- Clofazimine targeting the spike protein and RdRp exhibits highly efficient antiviral activity against porcine epidemic diarrhea virus in vitro.Virologica Sinica · 2025Article
- Whole-Genome Analysis of Porcine Epidemic Diarrhea Virus from Yunnan, China.Veterinary sciences · 2024Article
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- Correlation between the IgG/IgA Antibody Response against PEDV Structural Protein and Virus Neutralization.Microbiology spectrum · 2023Article
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- Antigen epitopes of animal coronaviruses: a mini-review.Animal diseases · 2023Review
- Visual and Ultrasensitive Detection of a Coronavirus Using a Gold Nanorod Probe under Dark Field.Biosensors · 2022Article
- Current State of Molecular and Serological Methods for Detection of Porcine Epidemic Diarrhea Virus.Pathogens (Basel, Switzerland) · 2022Review
- Characterisation of ORF3, M, N and E Gene Sequences of Porcine Epidemic Diarrhoea Virus from Domestic Pigs in Poland.Journal of veterinary research · 2022Article
- Generation and functional analysis of single chain variable fragments (scFvs) targeting the nucleocapsid protein of Porcine epidemic diarrhea virus.Applied microbiology and biotechnology · 2022Article
- Porcine epidemic diarrhea virus strain FJzz1 infection induces type I/III IFNs production through RLRs and TLRs-mediated signaling.Frontiers in immunology · 2022Article
- A Virulent PEDV Strain FJzz1 with Genomic Mutations and Deletions at the High Passage Level Was Attenuated in Piglets via Serial Passage In Vitro.Virologica Sinica · 2021Article
- Identification of a novel B cell epitope on the nucleocapsid protein of porcine deltacoronavirus.Virus research · 2021Article
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Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Porcine epidemic diarrhea virus (PEDV) is a highly contagious coronavirus that causes severe diarrhea and death, particularly in neonatal piglets. The nucleocapsid protein (N protein) of PEDV presents strong immunogenicity and contributes to the cross-reactivity between PEDV and TGEV. However, the characterization of epitopes on the PEDV N protein remains largely unknown. Here, two monoclonal antibodies (MAbs) specific to the N protein of a PEDV strain, FJzz1/2011, were generated and screened against a partially overlapping library of 24 GST-fusion N protein-truncated constructs. We confirmed that residues 18-133 (designated NEP-D4) and residues 252-262 (designated NEP-D6) were the epitopes targeted by MAbs PN-D4 and PN-D6, respectively. Sequence analysis revealed that these two epitopes were highly conserved among PEDV strains but were significantly different from other members of the Coronavirinae subfamily. Western blot analysis showed that they could be specifically recognized by PEDV antisera but could not be recognized by TGEV hyperimmune antisera. Indirect immunofluorescence (IFA) assays confirmed no cross-reaction between these two MAbs and TGEV. In addition, the freeze-thaw cycle and protease treatment results indicated that NEP-D4 was intrinsically disordered. All these results suggest that these two novel epitopes and their cognate MAbs could serve as the basis for the development of precise diagnostic assays for PEDV.
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