ArticleVeterinary research2026
Identification of two immunodominant and neutralizing linear B-cell epitopes exposed on the surface of the porcine deltacoronavirus spike protein.
Article in Veterinary research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- Engineering a dimeric porcine deltacoronavirus S-RBD subunit vaccine for enhanced immunogenicity and neutralizing antibody responses.BMC veterinary research · 2026Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Porcine deltacoronavirus (PDCoV) is an enteropathogenic virus that causes severe diarrhea in pigs, particularly suckling piglets, and exhibits cross-species transmission with zoonotic potential. The S1 subunit of the viral spike (S) protein mediates cell entry and elicits neutralizing antibodies, making it an ideal target for diagnostics, prophylaxis, and therapeutics. Here, we produced two monoclonal antibodies (mAbs), B8F10 and G10C2, by immunizing BALB/c mice with a recombinant PDCoV S1 protein fused to a human IgG Fc fragment, expressed in an insect baculovirus system and purified using Protein A/G magnetic beads. Both mAbs can specifically recognize native PDCoV S protein in indirect immunofluorescence assays and western blot analyses under denaturing conditions, indicating their binding to linear epitopes. Isotyping classified both as IgG1/κ, and sequence analysis revealed distinct heavy-chain complementarity-determining regions (CDRs) but identical light-chain CDRs. Using truncated S1 proteins coupled with Pepscan ELISA, the B8F10 and G10C2 epitopes were precisely mapped to
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Registered trials
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 Socratic graph.