{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["11(4)"],"submitter":["Hu N"],"pubmed_abstract":["Botulinum neurotoxin (BoNT) is a highly lethal toxin produced by the anaerobic bacterium Clostridium botulinum, which leads to nerve paralysis following poisoning. At present, there is no specific drug officially approved. Antibodies, particularly single-domain antibodies, represent safe and effective candidates for specific drugs against BoNT. In this study, the receptor-binding domain of botulinum toxin (BoNT/AHC<sub>C</sub>) was utilized to immunize Bactrian camels, resulting in the generation of a nanobody phage library. From this library, a high-affinity binding antibody, designated A1, and a neutralizing antibody, named HM, were successfully obtained through SPR-based screening. The affinity constant of HM for botulinum toxin is 1.08E-11 M. Results from computer simulations indicate that HM binds at the same site as SV2C. Furthermore, experimental findings demonstrate that HM exhibits significant blocking activity at both the <i>in vitro</i> binding level and the cellular level. In mouse toxicity experiments, HM has been shown to offer protection against a 20 LD<sub>50</sub> dose of BoNT/A. Consequently, HM mitigates botulinum toxin poisoning in mice by obstructing the binding of AHC<sub>C</sub> to SV2C."],"journal":["Heliyon"],"pagination":["e42616"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11891721"],"repository":["biostudies-literature"],"pubmed_title":["A novel single-domain antibody obtained from immune Bactrian camels against botulinum toxin type A using SPR-based screening method."],"pmcid":["PMC11891721"],"pubmed_authors":["Qiao C","Peng S","Xing C","Chen G","Yu J","Wang J","Jiang Z","Liu Y","Li X","Peng F","Feng J","Luo L","Xiao H","Hu N","Liu C","Wang Z"],"additional_accession":[]},"is_claimable":false,"name":"A novel single-domain antibody obtained from immune Bactrian camels against botulinum toxin type A using SPR-based screening method.","description":"Botulinum neurotoxin (BoNT) is a highly lethal toxin produced by the anaerobic bacterium Clostridium botulinum, which leads to nerve paralysis following poisoning. At present, there is no specific drug officially approved. Antibodies, particularly single-domain antibodies, represent safe and effective candidates for specific drugs against BoNT. In this study, the receptor-binding domain of botulinum toxin (BoNT/AHC<sub>C</sub>) was utilized to immunize Bactrian camels, resulting in the generation of a nanobody phage library. From this library, a high-affinity binding antibody, designated A1, and a neutralizing antibody, named HM, were successfully obtained through SPR-based screening. The affinity constant of HM for botulinum toxin is 1.08E-11 M. Results from computer simulations indicate that HM binds at the same site as SV2C. Furthermore, experimental findings demonstrate that HM exhibits significant blocking activity at both the <i>in vitro</i> binding level and the cellular level. In mouse toxicity experiments, HM has been shown to offer protection against a 20 LD<sub>50</sub> dose of BoNT/A. Consequently, HM mitigates botulinum toxin poisoning in mice by obstructing the binding of AHC<sub>C</sub> to SV2C.","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Feb","modification":"2026-06-01T20:12:42.687Z","creation":"2025-04-07T07:50:15.411Z"},"accession":"S-EPMC11891721","cross_references":{"pubmed":["40066047"],"doi":["10.1016/j.heliyon.2025.e42616"]}}