ArticleInternational journal of biological macromolecules2018
Characterization of the interaction between recombinant porcine aminopeptidase N and spike glycoprotein of porcine epidemic diarrhea virus.
Article in International journal of biological macromolecules, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- FUT8-mediated core fucosylation of receptor APN drives entry of multiple alphacoronaviruses.PLoS pathogens · 2026Article
- PEDV Nsp14 induces mitophagy-mediated degradation of MAVS to antagonize host innate immunity and facilitate viral proliferation.Journal of virology · 2025Article
- IFITM proteins are key entry factors for porcine epidemic diarrhea coronavirus.Journal of virology · 2025Article
- Palmitoylation enhances the stability of porcine epidemic diarrhea virus spike protein by antagonizing its degradation via chaperone-mediated autophagy to facilitate viral proliferation.Journal of virology · 2025Article
- The Alpha-1 Subunit of the NaInternational journal of molecular sciences · 2023Article
- Development of an enzyme-linked immunosorbent assay based on viral antigen capture by anti-spike glycoprotein monoclonal antibody for detecting immunoglobulin A antibodies against porcine epidemic diarrhea virus in milk.BMC veterinary research · 2023Article
- CCR4-NOT Complex 2-A Cofactor in Host Cell for Porcine Epidemic Diarrhea Virus Infection.Genes · 2022Article
- Transferrin receptor 1 levels at the cell surface influence the susceptibility of newborn piglets to PEDV infection.PLoS pathogens · 2020Article
- A Bibliometric Analysis of Corona Pandemic in Social Sciences: A Review of Influential Aspects and Conceptual Structure.IEEE access : practical innovations, open solutions · 2020Article
- Preparation and characterization of a single-domain antibody specific for the porcine epidemic diarrhea virus spike protein.AMB Express · 2019Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Porcine epidemic diarrhea (PED) has caused huge economic losses to the global pork industry. Infection by its causative agent PED virus (PEDV), an Alpha-coronavirus, was previously proven to be mediated by its spike (S) glycoprotein and a cellular receptor porcine aminopeptidase N (pAPN). Interestingly, some recent studies have indicated that pAPN is not a functional receptor for PEDV. To date, there is a lack of a direct evidence for the interaction between pAPN and PEDV S protein in vitro. Here, we prepared pAPN ectodomain and the truncated variants of PEDV S protein in Drosophila S2 cells. These recombinant proteins were homogeneous after purification by metal-affinity and size-exclusion chromatography. We then assayed the purified target proteins through immunogenicity tests, PEDV binding interference assays, circular dichroism (CD) measurements, pAPN activity assay and structural determination, demonstrating that they were biologically functional. Finally, we characterized their interactions by gel filtration chromatography, native-polyacrylamide gel electrophoresis (PAGE) and surface plasmon resonance (SPR) analyses. The results showed that their affinities were too low to form complexes, which suggest that pAPN may be controversial as the genuine receptor for PEDV. Therefore, further research needs to be carried out to elucidate the interaction between PEDV and its genuine receptor.
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