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

  • Libia Sanz
  • , Davinia Pla
  • , Alicia Pérez
  • , Yania Rodríguez
  • , Alfonso Zavaleta
  • , Maria Salas
  • , Bruno Lomonte
  • , Juan J. Calvete
  • CSIC - Instituto de Biomedicina de Valencia (IBV)
  • Mental Honorio Delgado-Hideyo Noguchi
  • Universidad Peruana Cayetano Heredia
  • University of Costa Rica

Research output: Contribution to journalArticlepeer-review

49 Scopus citations

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.

Original languageEnglish
Article number178
JournalToxins
Volume8
Issue number6
DOIs
StatePublished - Jun 2016

Keywords

  • Mass spectrometry
  • Micrurus tschudii tschudii venom
  • Snake venom phospholipase A
  • Snake venom proteome
  • Three-finger toxin
  • Venomics

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