期刊
JOURNAL OF PROTEOMICS
卷 75, 期 8, 页码 2442-2453出版社
ELSEVIER
DOI: 10.1016/j.jprot.2012.02.021
关键词
Snake venomics; Antivenomics; Cerastes cerastes; Ceraste vipera; Mass spectrometry; Venom proteome
资金
- Ministerio de Economia y Competitividad, Madrid, Spain [BFU2010-17373]
- Programa de Cooperacion Interuniversitaria e Investigacion Cientifica [C/032069/10]
- Generalitat Valenciana (Valencia, Spain) [PROMETEO/2010/005]
We report the proteomic analysis of the venom of the medically relevant snake, Cerastes cerastes, from Morocco, and the immunoreactivity profile of an experimental monospecific (CcMo_AV against Moroccan C. cerastes venom) and a commercial (Gamma-VIP against Tunisian C. cerastes and M. lebetina venoms) F(ab')(2) antivenoms towards geographic variants of C. cerastes and C. vipera venoms. The venom of C. cerastes is a low-complexity proteome composed of 25-30 toxins belonging to 6 protein families, mainly targetting the hemostatic system. This toxin arsenal explains the clinical picture observed in C. cerastes envenomings. Despite geographic compositional variation, the monospecific CcMo_AV and the Gamma-VIP divalent antivenom produced at Institut Pasteur de Tunis, showed similar immunocapturing capability towards Moroccan, Tunisian, and Egyptian C. cerastes venom proteins. Proteins partially escaping immunorecognition were all identified as PLA(2) molecules. Antivenomic analysis showed low degree of cross-reactivity of Moroccan CcMo_AV and Tunisian Gamma-VIP antivenoms towards C. vipera venom toxins. This study indicates that a more complete therapeutic cover could be achieved by including C. vipera venom in the formulation of venom immunization mixtures, thereby generating a pan-Cerastes antivenom. (C) 2012 Elsevier B.V. All rights reserved.
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