ArticleVirus research2017
Porcine amino peptidase N domain VII has critical role in binding and entry of porcine epidemic diarrhea virus.
Article in Virus research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Neutralizing activity analysis of mimotopes against porcine epidemic diarrhea virus (PEDV) spike protein.Analytical and bioanalytical chemistry · 2026Article
- Cav1.2 facilitates the binding and internalisation of porcine epidemic diarrhoea virus.Veterinary research · 2025Article
- Resolving the APN controversy in PEDV infection: Comparative kinetic characterization through single-virus tracking.PLoS pathogens · 2025Article
- Research progress of porcine epidemic diarrhea virus S protein.Frontiers in microbiology · 2024Review
- Review
- PEDV: Insights and Advances into Types, Function, Structure, and Receptor Recognition.Viruses · 2022Review
- Improvements in pig agriculture through gene editing.CABI agriculture and bioscience · 2022Review
- Resistance to coronavirus infection in amino peptidase N-deficient pigs.Transgenic research · 2019Article
- Evaluation of the Efficacy of a Recombinant Adenovirus Expressing the Spike Protein of Porcine Epidemic Diarrhea Virus in Pigs.BioMed research international · 2019Article
- Article
- Characterization of influenza A virus pseudotyped with the spike protein of porcine epidemic diarrhea virus.Archives of virology · 2018Article
- Contribution of porcine aminopeptidase N to porcine deltacoronavirus infection.Emerging microbes & infections · 2018Article
- Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Porcine epidemic diarrhea virus (PEDV) infects swine intestinal cells causing enteric disease. Research has shown that the entry into these cells is through porcine aminopeptidase N (pAPN) receptor. To gain insights into mechanisms of PEDV-pAPN interactions, the present study aimed at identifying the domain that is critical for PEDV binding. To this end, NIH3T3 cell lines constitutively expressing pAPN or pAPN mutants were generated. The mutants were; domain VII deletion mutant and domains IV-VI deletion mutant. In the latter, domain VII was linked to the transmembrane segment through domain III. Results showed PEDV infection was restricted to pAPN and pAPN domain VII expressing NIH3T3 cells. Further, reducing PEDV titre 10 fold resulted in 37.8% decrease in foci indicating positive correlation. A time course test at 12, 24, 36, 48 and 60h showed that foci increased 6 fold in the overall time range. Also, PEDV harvested from pAPN or domain VII expressing NIH3T3 cells was induced indirect plaques in Vero cells confirming successful entry and replication. Collectively, our results demonstrate that PEDV recognizes pAPN and that the main interactive point is lodged within domain VII of the pAPN. These findings are important for therapeutic development as well as creating a platform for future studies on PEDV.
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