Abstract

BackgroundThe relative influence of diet and phylogeny on snake venom activity is a poorly understood aspect of snake venom evolution. We measured the activity of two enzyme toxin groups – phospholipase A2 (PLA2), and L-amino acid oxidase (LAAO) – in the venom of 39 species of Australian elapids (40% of terrestrial species diversity) and used linear parsimony and BayesTraits to investigate any correlation between enzyme activity and phylogeny or diet.ResultsPLA2 activity ranged from 0 to 481 nmol/min/mg of venom, and LAAO activity ranged from 0 to 351 nmol/min/mg. Phylogenetic comparative methods, implemented in BayesTraits showed that enzyme activity was strongly correlated with phylogeny, more so for LAAO activity. For example, LAAO activity was absent in both the Vermicella and Pseudonaja/Oxyuranus clade, supporting previously proposed relationships among these disparate taxa. There was no association between broad dietary categories and either enzyme activity. There was strong evidence for faster initial rates of change over evolutionary time for LAAO (delta parameter mean 0.2), but no such pattern in PLA2 (delta parameter mean 0.64). There were some exceptions to the phylogenetic patterns of enzyme activity: different PLA2 activity in the ecologically similar sister-species Denisonia devisi and D. maculata; large inter-specific differences in PLA2 activity in Hoplocephalus and Austrelaps.ConclusionsWe have shown that phylogeny is a stronger influence on venom enzyme activity than diet for two of the four major enzyme families present in snake venoms. PLA2 and LAAO activities had contrasting evolutionary dynamics with the higher delta value for PLA2 Some species/individuals lacked activity in one protein family suggesting that the loss of single protein family may not incur a significant fitness cost.

Highlights

  • Venomous snakes in Australia belong almost entirely to the front-fanged family Elapidae

  • We aimed to investigate the evolution of two protein families, phospholipase A2 (PLA2) and L-amino acid oxidase (LAAO), in Australasian elapid venoms, by measuring their enzymatic activity, and analysing this with respect to phylogeny and snake diet

  • Phospholipase A2 PLA2 activity was measured in 90 individual snakes from 37 different species (Fig. 2)

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Summary

Introduction

Venomous snakes in Australia belong almost entirely to the front-fanged family Elapidae. Australasian elapid venoms contain all four major protein families; three-finger toxins (3FTx), phospholipase A2 (PLA2), snake venom serine protease (SVSP), and snake venom metalloprotease (SVMP) – and all six secondary protein families; disintegrin (DIS), L-amino acid oxidase (LAAO), natriuretic peptides (NP), kunitz peptides (KUN) cysteine-rich secretary proteins (CRiSP) and C-type lectins (CTL) [3]. These protein families are typically unevenly (2020) 20:9. We measured the activity of two enzyme toxin groups – phospholipase A2 (PLA2), and L-amino acid oxidase (LAAO) – in the venom of 39 species of Australian elapids (40% of terrestrial species diversity) and used linear parsimony and BayesTraits to investigate any correlation between enzyme activity and phylogeny or diet

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