Abstract

Variability in snake venom composition has been frequently reported and correlated to the adaptability of snakes to environmental conditions. Previous studies report plasticity for the venom phenotype. However, these observations are not conclusive, as the results were based on pooled venoms, which present high individual variability. Here we tested the hypothesis of plasticity by influence of confinement and single diet type in the venom composition of 13 adult specimens of Bothrops atrox snakes, maintained under captivity for more than three years. Individual variability in venom composition was observed in samples extracted just after the capture of the snakes. However, composition was conserved in venoms periodically extracted from nine specimens, which presented low variability restricted to the less abundant components. In a second group, composed of four snakes, drastic changes were observed in the venom samples extracted at different periods, mostly related to snake venom metalloproteinases (SVMPs), the core function toxins of B. atrox venom, which occurred approximately between 400 and 500 days in captivity. These data show plasticity in the venom phenotype during the lifetime of adult snakes maintained under captive conditions. Causes or functional consequences involved in the phenotype modification require further investigations.

Highlights

  • Venoms are considered trophic adaptations that enable venomous snakes to use potent toxins as a chemical means to subdue their prey [1]

  • Venom composition was analyzed in each individual sample according to the chromatographic profile in reverse-phase C18 HPLC columns (RP-HPLC), which is a well-accepted method to screen and compare venom composition in a large number of samples [37,45,47,48,49]

  • This is the protocol we used to perform proteomic analyses from pools or individual venom samples from B. atrox snakes collected in the same areas, in which we characterized the toxins present in each of the RP-HPLC fractions [50], which allows for inferences in venom components present in each chromatographic fraction discussed here

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Summary

Introduction

Venoms are considered trophic adaptations that enable venomous snakes to use potent toxins as a chemical means to subdue their prey [1]. Toxins 2019, 11, 294 snake venom serine proteases (SVSPs), C-type lectin-like toxins (CTLs), and phospholipases A2 (PLA2 s) are the most abundant toxin families and are commonly related to impacts on prey hemostasis [4]. Other toxin families, such as cysteine-rich secretory proteins (CRISPs), L-amino acid oxidases (LAAOs), and other components, are included in the venom composition, but generally in lower abundance and have not yet been related to serious disturbances in the coagulation system or tissue damage. Following SVMPs, CTLs are the second most abundant toxin family in B. atrox venom (~20%) and PLA2 s and SVSPs are present in in lower amounts in venom proteome (6–9% and 4–7%, respectively) [5]

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