ArticleBMC veterinary research2026
Identification of a novel N-terminal linear B-cell epitope on the FIPV nucleocapsid protein by a monoclonal antibody.
Article in BMC veterinary research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
backgroundFeline infectious peritonitis (FIP) is difficult to diagnose in clinical practice and has a high mortality rate, which underscores the need for reliable and standardized diagnostic tools. The nucleocapsid (N) protein, a major viral structural component, is a preferred target for serological and pathological assays because it is highly abundant in infected cells and has strong immunogenicity.
resultsIn this study, a monoclonal antibody, designated mAb 4F3, was generated by immunizing mice with purified recombinant FIPV N protein fused with a His tag (His-N) and screening hybridomas via ELISA utilizing purified recombinant N protein fused with a glutathione S-transferase tag (GST-N). Characterization via ELISA, western blot, and indirect immunofluorescence assay (IFA) confirmed that mAb 4F3 binds effectively to the recombinant antigen and specifically recognizes the native N protein within FIPV-infected cells. Furthermore, the antibody exhibited no cross-reactivity with heterologous coronaviruses, including porcine epidemic diarrhea virus (PEDV), transmissible gastroenteritis virus (TGEV), and porcine deltacoronavirus (PDCoV). Fine epitope mapping identified the minimal linear epitope recognized by mAb 4F3 as 105FKDKIDGVFW114, located within the N-terminal domain (NTD) of the N protein. Sequence alignment further verified that this epitope is highly conserved (> 90%) among FCoV strains while sharing low homology with non-FCoV coronaviruses, demonstrating excellent viral specificity.
conclusionsWe successfully generated and characterized mAb 4F3, an anti-FIPV N protein monoclonal antibody that is suitable for multiple detection platforms. We also precisely mapped its minimal linear epitope. These findings provide a valuable antibody resource and a molecular basis for the development of standardized FIP diagnostic techniques and for studies of the immunological functions of the N protein.
Indexed as
Identifiers
What OpenQuestion holds
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 OpenQuestion graph.