ArticleNature communications2024
Neutralizing antibodies reveal cryptic vulnerabilities and interdomain crosstalk in the porcine deltacoronavirus spike protein.
Article in Nature communications, 2024. 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.
- Neutralizing epitope mapping for deltacoronavirus receptor-binding domain and seroepidemiological survey across different animal species.Virulence · 2026Article
- Monoclonal antibodies target conserved S1mBio · 2026Article
- Review
- Integrated analysis of transcriptome and proteome reveal that PDCoV infection induces autophagy-dependent ferroptosis to facilitate viral replication.Veterinary research · 2026Article
- Computational design of an ultrapotent deltacoronavirus miniprotein inhibitor.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
- Double-antigen sandwich ELISA based on S1 for cross-species detection of Porcine deltacoronavirus antibodies.Applied microbiology and biotechnology · 2025Article
- A novel nanoparticle vaccine, based on S1-CTD, elicits robust protective immune responses against porcine deltacoronavirus.Journal of virology · 2025Article
- A novel neutralizing antibody recognizing a conserved conformational epitope in PDCoV S1 protein and its therapeutic efficacy in piglets.Journal of virology · 2025Article
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Authors and funding
11 authors.
Funding
Abstract
Porcine deltacoronavirus (PDCoV) is an emerging enteric pathogen that has recently been detected in humans. Despite this zoonotic concern, the antigenic structure of PDCoV remains unknown. The virus relies on its spike (S) protein for cell entry, making it a prime target for neutralizing antibodies. Here, we generate and characterize a set of neutralizing antibodies targeting the S protein, shedding light on PDCoV S interdomain crosstalk and its vulnerable sites. Among the four identified antibodies, one targets the S1A domain, causing local and long-range conformational changes, resulting in partial exposure of the S1B domain. The other antibodies bind the S1B domain, disrupting binding to aminopeptidase N (APN), the entry receptor for PDCoV. Notably, the epitopes of these S1B-targeting antibodies are concealed in the prefusion S trimer conformation, highlighting the necessity for conformational changes for effective antibody binding. The binding footprint of one S1B binder entirely overlaps with APN-interacting residues and thus targets a highly conserved epitope. These findings provide structural insights into the humoral immune response against the PDCoV S protein, potentially guiding vaccine and therapeutic development for this zoonotic pathogen.
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