Snake venomics and antivenomics of Protobothrops mucrosquamatus and Viridovipera stejnegeri from Taiwan: keys to understand the variable immune response in horses.
Abstract: The proteomes of the venoms of the snakes Viridovipera stejnegeri and Protobothrops mucrosquamatus from Taiwan were characterized by N-terminal sequencing, MALDI-TOF mass fingerprinting, and collision-induced dissociation tandem mass spectrometry of in-gel generated tryptic peptides. Proteins belonging to the following toxin classes were identified: metalloproteinase, phospholipase A(2) (PLA(2)), serine proteinase, C-type lectin-like, CRISP, l-amino acid oxidase, disintegrin, and peptides (vasoactive and inhibitors of SVMPs). Nine horses were immunized with a mixture of these venoms. All horses developed a satisfactory immune response against lethality of the venom of V. stejnegeri, whereas only three horses reached the accepted neutralizing potency against the venom of P. mucrosquamatus. Antivenoms were prepared from pools of 'good responder' (GR) and 'poor responder' (PR) horses and compared by antivenomics and neutralization tests. A similar neutralizing response was observed between the GR and PR antivenoms against the venom of V. stejnegeri, whereas antivenom from PR had a lower neutralizing activity against effects of P. mucrosquamatus venom than antivenom from GR. The low potency of the plasma of some horses against this venom is a consequence of the low immunogenicity of the neurotoxic PLA(2) trimucrotoxin. Our results provide clues for innovating the immunization scheme to generate improved antivenoms.
Copyright © 2012 Elsevier B.V. All rights reserved.
Publication Date: 2012-08-18 PubMed ID: 22906718DOI: 10.1016/j.jprot.2012.08.008Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research investigated the venom properties of two snake species in Taiwan and the variability in immune response in horses when immunized with these venoms. The study further explored ways to improve the production of antivenoms.
Characterization of Snake Venom Proteins
- The researchers studied the venomous properties of two snake species – Viridovipera stejnegeri and Protobothrops mucrosquamatus – from Taiwan.
- Through techniques such as N-terminal sequencing, MALDI-TOF mass fingerprinting, and collision-induced dissociation tandem mass spectrometry, they identified proteins from eight distinct toxin classes present in the venoms of these snakes. These toxins included metalloproteinase, phospholipase A2 (PLA2), and others.
Immune Response in Horses
- Nine horses were immunized with these venoms to test their immune response.
- All the horses exhibited an effective immune response against V. stejnegeri venom, but only three showed a satisfactory neutralizing potency against P. mucrosquamatus venom.
Development and Evaluation of Antivenoms
- Following the trial, the researchers prepared antivenoms from both ‘good responder’ (GR) and ‘poor responder’ (PR) horses.
- Comparative analysis using antivenomics and neutralization tests showed a similar efficacy for both GR and PR antivenoms against V. stejnegeri venom. In contrast, PR antivenom had less neutralizing activity against P. mucrosquamatus venom compared to the GR antivenom.
Understanding the Variation in Response
- The study concluded that the lower potency in PR horses’ plasma against P. mucrosquamatus venom could be attributed to the low immunogenicity of the neurotoxic PLA2 called trimucrotoxin in the venom.
Implication for Antivenom Production
- The study provides theoretical insights that can be used to innovate the immunization scheme for producing improved and more effective antivenoms.
Cite This Article
APA
Villalta M, Pla D, Yang SL, Sanz L, Segura A, Vargas M, Chen PY, Herrera M, Estrada R, Cheng YF, Lee CD, Cerdas M, Chiang JR, Angulo Y, León G, Calvete JJ, Gutiérrez JM.
(2012).
Snake venomics and antivenomics of Protobothrops mucrosquamatus and Viridovipera stejnegeri from Taiwan: keys to understand the variable immune response in horses.
J Proteomics, 75(18), 5628-5645.
https://doi.org/10.1016/j.jprot.2012.08.008 Publication
Researcher Affiliations
- Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica.
MeSH Terms
- Amino Acid Sequence
- Animals
- Antivenins / immunology
- Horses / immunology
- Humans
- Mice
- Neutralization Tests
- Proteome / analysis
- Taiwan
- Viper Venoms / chemistry
- Viper Venoms / immunology
- Viperidae
Citations
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