ArticleNature communications2022
Structures of a deltacoronavirus spike protein bound to porcine and human receptors.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 66 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
66 citing papers in PubMed, 98 citations in OpenAlex.
- Neutralizing epitope mapping for deltacoronavirus receptor-binding domain and seroepidemiological survey across different animal species.Virulence · 2026Article
- The essential role of heparan sulfate in the entry of PDCoV and other porcine coronaviruses.Virulence · 2026Article
- Molecular characterization and pathogenicity of a novel Chinese porcine deltacoronavirus strain CH/HLJ/20 isolated from diarrheic piglets.Virulence · 2026Article
- Aminopeptidase N is a receptor for hedgehog merbecoviruses.Nature microbiology · 2026Article
- Convergent use of aminopeptidase N receptor by hedgehog merbecoviruses.Nature microbiology · 2026Article
- Engineering a dimeric porcine deltacoronavirus S-RBD subunit vaccine for enhanced immunogenicity and neutralizing antibody responses.BMC veterinary research · 2026Article
- GTPase domain of porcine Mx1 protein interacts with the N protein of porcine deltacoronavirus to inhibit viral replication.The Journal of general virology · 2026Article
- Identification of GRP78 as a novel host factor that facilitates zoonotic porcine deltacoronavirus internalization and replication via clathrin-mediated endocytosis.Journal of virology · 2026Article
- Article
- O-GlcNAcylation licenses RNF166 to degrade the M protein of porcine coronaviruses.PLoS pathogens · 2026Article
- Swine GBP1 restricts PDCoV replication via disrupting the replication and transcription complex formation.Journal of virology · 2026Article
- Computational design of an ultrapotent deltacoronavirus miniprotein inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Alkaline mineral complex water protects piglets against viral infection by driving cholesterol consumption through the GPAT2/SULT2A1 axis.Science China. Life sciences · 2026Article
- Quantifying and combating zoonotic viruses poised for emergence: Using multiplex receptor screening and decoy engineering technologies.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Cetacean coronavirus spikes highlight S glycoprotein structural plasticity.PLoS pathogens · 2026Article
- Cell entry mechanisms of porcine enteric coronaviruses.The Journal of biological chemistry · 2026Review
- Identification of two immunodominant and neutralizing linear B-cell epitopes exposed on the surface of the porcine deltacoronavirus spike protein.Veterinary research · 2026Article
- Detection of ongoing asymptomaticFrontiers in microbiology · 2026Article
- RNA G-Quadruplexes in the Porcine Deltacoronavirus Genome: Structural Regulation and Therapeutic Targeting for Antiviral Strategies.Transboundary and emerging diseases · 2026Article
- Double-antigen sandwich ELISA based on S1 for cross-species detection of Porcine deltacoronavirus antibodies.Applied microbiology and biotechnology · 2025Article
6 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
14 authors at 4 institutions in 3 countries.
Funding
Abstract
Porcine deltacoronavirus (PDCoV) can experimentally infect a variety of animals. Human infection by PDCoV has also been reported. Consistently, PDCoV can use aminopeptidase N (APN) from different host species as receptors to enter cells. To understand this broad receptor usage and interspecies transmission of PDCoV, we determined the crystal structures of the receptor binding domain (RBD) of PDCoV spike protein bound to human APN (hAPN) and porcine APN (pAPN), respectively. The structures of the two complexes exhibit high similarity. PDCoV RBD binds to common regions on hAPN and pAPN, which are different from the sites engaged by two alphacoronaviruses: HCoV-229E and porcine respiratory coronavirus (PRCoV). Based on structure guided mutagenesis, we identified conserved residues on hAPN and pAPN that are essential for PDCoV binding and infection. We report the detailed mechanism for how a deltacoronavirus recognizes homologous receptors and provide insights into the cross-species transmission of PDCoV.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.