Contextual Constraints: Dynamic Evolution of Snake Venom Phospholipase A<sub>2</sub>

Venom is a dynamic trait that has contributed to the success of numerous organismal lineages. Predominantly composed of proteins, these complex cocktails are deployed for predation and/or self-defence. Many non-toxic physiological proteins have been convergently and recurrently recruited by venomous...

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Main Authors: Vivek Suranse, Timothy N. W. Jackson, Kartik Sunagar
Format: Article
Language:English
Published: MDPI AG 2022-06-01
Series:Toxins
Subjects:
Online Access:https://www.mdpi.com/2072-6651/14/6/420
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author Vivek Suranse
Timothy N. W. Jackson
Kartik Sunagar
author_facet Vivek Suranse
Timothy N. W. Jackson
Kartik Sunagar
author_sort Vivek Suranse
collection DOAJ
description Venom is a dynamic trait that has contributed to the success of numerous organismal lineages. Predominantly composed of proteins, these complex cocktails are deployed for predation and/or self-defence. Many non-toxic physiological proteins have been convergently and recurrently recruited by venomous animals into their toxin arsenal. Phospholipase A<sub>2</sub> (PLA<sub>2</sub>) is one such protein and features in the venoms of many organisms across the animal kingdom, including snakes of the families Elapidae and Viperidae. Understanding the evolutionary history of this superfamily would therefore provide insight into the origin and diversification of venom toxins and the evolution of novelty more broadly. The literature is replete with studies that have identified diversifying selection as the sole influence on PLA<sub>2</sub> evolution. However, these studies have largely neglected the structural/functional constraints on PLA<sub>2</sub>s, and the ecology and evolutionary histories of the diverse snake lineages that produce them. By considering these crucial factors and employing evolutionary analyses integrated with a schema for the classification of PLA<sub>2</sub>s, we uncovered lineage-specific differences in selection regimes. Thus, our work provides novel insights into the evolution of this major snake venom toxin superfamily and underscores the importance of considering the influence of evolutionary and ecological contexts on molecular evolution.
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spelling doaj.art-6e858471cb524756b236846de878641d2023-11-23T19:17:38ZengMDPI AGToxins2072-66512022-06-0114642010.3390/toxins14060420Contextual Constraints: Dynamic Evolution of Snake Venom Phospholipase A<sub>2</sub>Vivek Suranse0Timothy N. W. Jackson1Kartik Sunagar2Evolutionary Venomics Laboratory, Centre for Ecological Sciences, Indian Institute of Science, Bangalore 560012, IndiaAustralian Venom Research Unit, Department of Pharmacology and Therapeutics, The University of Melbourne, Parkville, VIC 3010, AustraliaEvolutionary Venomics Laboratory, Centre for Ecological Sciences, Indian Institute of Science, Bangalore 560012, IndiaVenom is a dynamic trait that has contributed to the success of numerous organismal lineages. Predominantly composed of proteins, these complex cocktails are deployed for predation and/or self-defence. Many non-toxic physiological proteins have been convergently and recurrently recruited by venomous animals into their toxin arsenal. Phospholipase A<sub>2</sub> (PLA<sub>2</sub>) is one such protein and features in the venoms of many organisms across the animal kingdom, including snakes of the families Elapidae and Viperidae. Understanding the evolutionary history of this superfamily would therefore provide insight into the origin and diversification of venom toxins and the evolution of novelty more broadly. The literature is replete with studies that have identified diversifying selection as the sole influence on PLA<sub>2</sub> evolution. However, these studies have largely neglected the structural/functional constraints on PLA<sub>2</sub>s, and the ecology and evolutionary histories of the diverse snake lineages that produce them. By considering these crucial factors and employing evolutionary analyses integrated with a schema for the classification of PLA<sub>2</sub>s, we uncovered lineage-specific differences in selection regimes. Thus, our work provides novel insights into the evolution of this major snake venom toxin superfamily and underscores the importance of considering the influence of evolutionary and ecological contexts on molecular evolution.https://www.mdpi.com/2072-6651/14/6/420phospholipase A<sub>2</sub>snake venomvenom evolutionvenom ecologyElapidaeViperidae
spellingShingle Vivek Suranse
Timothy N. W. Jackson
Kartik Sunagar
Contextual Constraints: Dynamic Evolution of Snake Venom Phospholipase A<sub>2</sub>
Toxins
phospholipase A<sub>2</sub>
snake venom
venom evolution
venom ecology
Elapidae
Viperidae
title Contextual Constraints: Dynamic Evolution of Snake Venom Phospholipase A<sub>2</sub>
title_full Contextual Constraints: Dynamic Evolution of Snake Venom Phospholipase A<sub>2</sub>
title_fullStr Contextual Constraints: Dynamic Evolution of Snake Venom Phospholipase A<sub>2</sub>
title_full_unstemmed Contextual Constraints: Dynamic Evolution of Snake Venom Phospholipase A<sub>2</sub>
title_short Contextual Constraints: Dynamic Evolution of Snake Venom Phospholipase A<sub>2</sub>
title_sort contextual constraints dynamic evolution of snake venom phospholipase a sub 2 sub
topic phospholipase A<sub>2</sub>
snake venom
venom evolution
venom ecology
Elapidae
Viperidae
url https://www.mdpi.com/2072-6651/14/6/420
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