PreprintCited by 486Venomous Animal Envenomation and StudiesAmphibian and Reptile BiologyGenomics and Phylogenetic Studies

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From genome to “venome”: Molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins

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Fry, Bryan G.·2005·Genome Research

DOI 10.1101/gr.3228405PMC PMC551567

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Abstract

This study analyzed the origin and evolution of snake venom proteome by means of phylogenetic analysis of the amino acid sequences of the toxins and related nonvenom proteins. The snake toxins were shown to have arisen from recruitment events of genes from within the following protein families: acetylcholinesterase, ADAM (disintegrin/metalloproteinase), AVIT, complement C3, crotasin/β defensin, cystatin, endothelin, factor V, factor X, kallikrein, kunitz-type proteinase inhibitor, LYNX/SLUR, L-amino oxidase, lectin, natriuretic peptide, βnerve growth factor, phospholipase A 2, SPla/Ryanodine, vascular endothelial growth factor, and whey acidic protein/secretory leukoproteinase inhibitor. Toxin recruitment events were found to have occurred at least 24 times in the evolution of snake venom. Two of these toxin derivations (CRISP and kallikrein toxins) appear to have been actually the result of modifications of existing salivary proteins rather than gene recruitment events. One snake toxin type, the waglerin peptides from Tropidolaemus wagleri (Wagler's Viper), did not have a match with known proteins and may be derived from a uniquely reptilian peptide. All of the snake toxin types still possess the bioactivity of the ancestral proteins in at least some of the toxin isoforms. However, this study revealed that the toxin types, where the ancestral protein was extensively cysteine cross-linked, were the ones that flourished into functionally diverse, novel toxin multigene families.

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Authors: Fry, B. G.
Affiliations: European Bioinformatics Institute (GB)
Corresponding author: Fry, Bryan G.
ORCID: Fry, Bryan G.
Venue: Genome Research
Publisher: Cold Spring Harbor Laboratory
Published: 2005-03
Volume: 15
Issue: 3
Pages: 403-420
ISSN: 1088-9051 (ISSN-L)
DOI: 10.1101/gr.3228405
PMC: PMC551567
OpenAlex: W2073555092
Cited by: 486
References: 45
Citations by year: 2026: 9 · 2025: 19 · 2024: 14 · 2023: 9 · 2022: 20 · 2021: 20 · 2020: 27 · 2019: 23 · 2018: 14 · 2017: 30 · 2016: 29 · 2015: 23 · 2014: 40 · 2013: 30 · 2012: 21
Type: posted content
Language: en
Open access: bronze
doi.org
Locations: Genome Research (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: European Bioinformatics Institute
Australian Academy of Science
University of Melbourne
Australian Research Council (DP0451663)
Topics: Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Venomous Animal Envenomation and Studies
Life Sciences › Agricultural and Biological Sciences › Ecology, Evolution, Behavior and Systematics › Amphibian and Reptile Biology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
Keywords: snake venom proteome, gene recruitment, acetylcholinesterase, Adam, kallikrein, phospholipase A2, cysteine cross-linking, salivary proteins
MeSH terms: Animals, Phylogeny, Snake Venoms, Snakes, Tissue Distribution, Evolution, Molecular, Proteome

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From genome to “venome”: Molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins

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