ArticlePloS one2016
Inhibition of the Myotoxicity Induced by Bothrops jararacussu Venom and Isolated Phospholipases A2 by Specific Camelid Single-Domain Antibody Fragments.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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.
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Who cites it
22 citing papers in PubMed, 51 citations in OpenAlex.
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- Single-Domain Antibody-Gold Nanoparticle Bioconjugates as Immunosensors for the Detection of Hantaviruses.Molecular diagnosis & therapy · 2024Article
- Synthetic development of a broadly neutralizing antibody against snake venom long-chain α-neurotoxins.Science translational medicine · 2024Article
- Towards better antivenoms: navigating the road to new types of snakebite envenoming therapies.The journal of venomous animals and toxins including tropical diseases · 2023Article
- Antibodies as Snakebite Antivenoms: Past and Future.Toxins · 2022Review
- VInternational journal of molecular sciences · 2022Review
- Next-Generation Molecular Discovery: From Bottom-Up In Vivo and In Vitro Approaches to In Silico Top-Down Approaches for Therapeutics Neogenesis.Life (Basel, Switzerland) · 2022Review
- Anti-Metalloprotease P-I Single-Domain Antibodies: Tools for Next-Generation Snakebite Antivenoms.BioMed research international · 2022Article
- Generation of synthetic nanobodies against delicate proteins.Nature protocols · 2020Article
- Development of Nanobodies Against Hemorrhagic and Myotoxic Components ofFrontiers in immunology · 2020Article
- Discrete analysis of camelid variable domains: sequences, structures, and in-silico structure prediction.PeerJ · 2020Article
- Structural basis for phospholipase AScientific reports · 2019Article
- Antibody Cross-Reactivity in Antivenom Research.Toxins · 2018Review
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- Article
- Can anti-bothropstoxin-I antibodies discriminate betweenThe journal of venomous animals and toxins including tropical diseases · 2017Article
- Camelid Single-Domain Antibodies As an Alternative to Overcome Challenges Related to the Prevention, Detection, and Control of Neglected Tropical Diseases.Frontiers in immunology · 2017Review
- Alpha-type phospholipase AThe journal of venomous animals and toxins including tropical diseases · 2017Review
Corrections and comments
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Authors and funding
17 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antivenoms, produced using animal hyperimmune plasma, remains the standard therapy for snakebites. Although effective against systemic damages, conventional antivenoms have limited efficacy against local tissue damage. Additionally, the hypersensitivity reactions, often elicited by antivenoms, the high costs for animal maintenance, the difficulty of producing homogeneous lots, and the instability of biological products instigate the search for innovative products for antivenom therapy. In this study, camelid antibody fragments (VHH) with specificity to Bothropstoxin I and II (BthTX-I and BthTX-II), two myotoxic phospholipases from Bothrops jararacussu venom, were selected from an immune VHH phage display library. After biopanning, 28 and 6 clones recognized BthTX-I and BthTX-II by ELISA, respectively. Complementarity determining regions (CDRs) and immunoglobulin frameworks (FRs) of 13 VHH-deduced amino acid sequences were identified, as well as the camelid hallmark amino acid substitutions in FR2. Three VHH clones (KF498607, KF498608, and KC329718) were capable of recognizing BthTX-I by Western blot and showed affinity constants in the nanomolar range against both toxins. VHHs inhibited the BthTX-II phospholipase A2 activity, and when tested for cross-reactivity, presented specificity to the Bothrops genus in ELISA. Furthermore, two clones (KC329718 and KF498607) neutralized the myotoxic effects induced by B. jararacussu venom, BthTX-I, BthTX-II, and by a myotoxin from Bothrops brazili venom (MTX-I) in mice. Molecular docking revealed that VHH CDRs are expected to bind the C-terminal of both toxins, essential for myotoxic activity, and to epitopes in the BthTX-II enzymatic cleft. Identified VHHs could be a biotechnological tool to improve the treatment for snake envenomation, an important and neglected world public health problem.
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