| Literature DB >> 35699567 |
Line Ledsgaard1, Andreas H Laustsen1, Urska Pus1, Jack Wade1, Pedro Villar2, Kim Boddum3, Peter Slavny2, Edward W Masters2, Ana S Arias4, Saioa Oscoz1, Daniel T Griffiths2, Alice M Luther2, Majken Lindholm2, Rachael A Leah2, Marie Sofie Møller1, Hanif Ali5, John McCafferty2, Bruno Lomonte4, José M Gutiérrez4, Aneesh Karatt-Vellatt2.
Abstract
The monocled cobra (Naja kaouthia) is among the most feared snakes in Southeast Asia due to its toxicity, which is predominantly derived from long-chain α-neurotoxins. The only specific treatment for snakebite envenoming is antivenom based on animal-derived polyclonal antibodies. Despite the lifesaving importance of these medicines, major limitations in safety, supply consistency, and efficacy create a need for improved treatments. Here, we describe the discovery and subsequent optimization of a recombinant human monoclonal immunoglobulin G antibody against α-cobratoxin using phage display technology. Affinity maturation by light chain-shuffling resulted in a significant increase in in vitro neutralization potency and in vivo efficacy. The optimized antibody prevented lethality when incubated with N. kaouthia whole venom prior to intravenous injection. This study is the first to demonstrate neutralization of whole snake venom by a single recombinant monoclonal antibody, thus providing a tantalizing prospect of bringing recombinant antivenoms based on human monoclonal or oligoclonal antibodies to the clinic.Entities:
Keywords: Recombinant antivenom; affinity maturation; antibody discovery; monoclonal antibodies; snake neurotoxins; venom neutralization
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Year: 2022 PMID: 35699567 PMCID: PMC9225616 DOI: 10.1080/19420862.2022.2085536
Source DB: PubMed Journal: MAbs ISSN: 1942-0862 Impact factor: 6.440