Academic Journal
Generation and epitope mapping of two distinct neutralizing mAb subsets targeting BVDV E2: a pan-pestivirus cross-reactive linear epitope and a BVDV-specific conformational epitope.
| Τίτλος: | Generation and epitope mapping of two distinct neutralizing mAb subsets targeting BVDV E2: a pan-pestivirus cross-reactive linear epitope and a BVDV-specific conformational epitope. |
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| Συγγραφείς: | Bao F; State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, College of Veterinary Medicine, Jilin University, Changchun, 130062, China., Mi S; Key Laboratory of Jilin Province for Zoonoses Prevention and Control, State Key Laboratory of Pathogen and Biosecurity, Academy of Military Medical Sciences, Changchun, 130122, China., Liu Z; State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, College of Veterinary Medicine, Jilin University, Changchun, 130062, China., Zhang S; State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, College of Veterinary Medicine, Jilin University, Changchun, 130062, China., Wu M; Chongqing Academy of Animal Sciences, Chongqing, 402460, China., Zhang Y; State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, College of Veterinary Medicine, Jilin University, Changchun, 130062, China., Tu C; State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, College of Veterinary Medicine, Jilin University, Changchun, 130062, China. changchun_tu@hotmail.com.; Key Laboratory of Jilin Province for Zoonoses Prevention and Control, State Key Laboratory of Pathogen and Biosecurity, Academy of Military Medical Sciences, Changchun, 130122, China. changchun_tu@hotmail.com.; Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou University, Yangzhou, 225009, China. changchun_tu@hotmail.com., Gong W; State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, College of Veterinary Medicine, Jilin University, Changchun, 130062, China. gong@jlu.edu.cn. |
| Πηγή: | Veterinary research [Vet Res] 2026 Oct 07; Vol. 57 (1). Date of Electronic Publication: 2026 Oct 07. |
| Τύπος έκδοσης: | Journal Article |
| Γλώσσα: | English |
| Στοιχεία περιοδικού: | Publisher: BioMed Central Country of Publication: England NLM ID: 9309551 Publication Model: Electronic Cited Medium: Internet ISSN: 1297-9716 (Electronic) Linking ISSN: 09284249 NLM ISO Abbreviation: Vet Res Subsets: MEDLINE |
| Imprint Name(s): | Publication: 2011- : London : BioMed Central Original Publication: Paris : Editions Scientifiques Elsevier ; INRA, c1993- |
| Ιατρικοί όροι (MeSH): | Epitope Mapping*/veterinary , Antibodies, Monoclonal*/immunology , Diarrhea Viruses, Bovine Viral*/immunology , Epitopes*/immunology , Antibodies, Neutralizing*/immunology , Viral Envelope Proteins*/immunology , Antibodies, Viral*/immunology, Animals ; Cattle ; Cross Reactions |
| Περίληψη: | Bovine viral diarrhea virus (BVDV) is an important infectious pathogen responsible for substantial economic losses in the global cattle industry. The structural protein E2 serves as a major protective antigen of BVDV and is the main target for host neutralizing immune responses. However, its antigenic structure and epitope distribution remain poorly understood. Here, five novel monoclonal antibodies (mAbs) against the E2 protein of BVDV-1 were generated using hybridoma technology, and their reactivity patterns, biological properties, and recognized epitopes were systematically characterized. As a result, one mAb, TBH033, specifically reacted with BVDV, while four mAbs, TBH002, TBH004, TBH008, and TBH009, exhibited broad-spectrum reactivity against different subgenotypes of classical swine fever virus (CSFV) and BVDV, as well as E2 proteins from eight pestivirus species (BVDV-1, BVDV-2, BVDV-3, CSFV, BDV, PPeV, GPeV, and ovIT PeV). All five mAbs exhibited high binding affinity to the E2 protein and potent cross-neutralizing activity against BVDV strains of different subgenotypes. Epitope mapping with chimeric recombinant and site-mutated E2 proteins revealed that TBH002, TBH004, TBH008, and TBH009 recognized a linear epitope in the DA domain, comprising 70H, 72R, 74L and 76T as critical residues; TBH033 targeted a BVDV-specific conformational epitope in the DB domain, defined by the conserved amino acid motifs 103LCP105, 123GP124. These findings enrich our understanding of the antigenic structure of the E2 protein and may facilitate the design of E2-based diagnostic tools and vaccines. (© 2026. The Author(s).) |
| Competing Interests: | Declarations. Ethics approval and consent to participate: All animal experiments were conducted in accordance with protocols approved by the Animal Welfare and Ethics Committee of the Academy of Military Medical Sciences (approval no.: IACUC of AMMS-11-2025-120). Consent for publication: Not applicable. Competing interests: The authors declare no competing interests. |
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| Grant Information: | 32372987 National Natural Science Foundation of China |
| Contributed Indexing: | Keywords: Bovine viral diarrhea virus; E2 protein; cross-neutralizing mAb; epitope mapping |
| Substance Nomenclature: | 0 (Antibodies, Monoclonal) 0 (Epitopes) 0 (Antibodies, Neutralizing) 0 (Viral Envelope Proteins) 0 (Antibodies, Viral) |
| Entry Date(s): | Date Created: 20261008 Date Completed: 20261008 Latest Revision: 20261008 |
| Update Code: | 20261008 |
| DOI: | 10.1186/s13567-026-01852-5 |
| PMID: | 42844638 |
| Βάση Δεδομένων: | MEDLINE |
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