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Venomic analysis of the poorly studied desert coral snake, Micrurus tschudii tschudii, supports the 3FTx/PLA2 dichotomy across Micrurus venoms

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Sanz, Libia
Pla Ferrer, Davinia
Pérez, Alicia
Rodríguez, Yania
Zavaleta Martínez Vargas, Alfonso
Salas Arruz, María
Lomonte, Bruno
Calvete Chornet, Juan José

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Abstract

The venom proteome of the poorly studied desert coral snake Micrurus tschudii tschudii was unveiled using a venomic approach, which identified ¥38 proteins belonging to only four snake venom protein families. The three-finger toxins (3FTxs) constitute, both in number of isoforms (~30) and total abundance (93.6% of the venom proteome), the major protein family of the desert coral snake venom. Phospholipases A2 (PLA2s; seven isoforms, 4.1% of the venom proteome), 1–3 Kunitz-type proteins (1.6%), and 1–2 L-amino acid oxidases (LAO, 0.7%) complete the toxin arsenal of M. t. tschudii. Our results add to the growing evidence that the occurrence of two divergent venom phenotypes, i.e., 3FTx- and PLA2-predominant venom proteomes, may constitute a general trend across the cladogenesis of Micrurus. The occurrence of a similar pattern of venom phenotypic variability among true sea snake (Hydrophiinae) venoms suggests that the 3FTx/PLA2 dichotomy may be widely distributed among Elapidae venoms.

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Micrurus, Venom, Proteome, Venomics, Three-finger toxin, Snake venom phospholipase A 2, Mass spectrometry, Micrurus tschudii tschudii

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http://www.mdpi.com/2072-6651/8/6/178

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