From genome to "venome": molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins
- PMID: 15741511
- PMCID: PMC551567
- DOI: 10.1101/gr.3228405
From genome to "venome": molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins
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/beta defensin, cystatin, endothelin, factor V, factor X, kallikrein, kunitz-type proteinase inhibitor, LYNX/SLUR, L-amino oxidase, lectin, natriuretic peptide, betanerve 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.
Figures
![Figure 1.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf1a_1o_rev2.gif)
![Figure 1.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf1a_1o_rev2.gif)
![Figure 2.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf2a_1o_rev2.gif)
![Figure 2.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf2a_1o_rev2.gif)
![Figure 3.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf3a_1o_rev1.gif)
![Figure 3.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf3a_1o_rev1.gif)
![Figure 4.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf4a_1o_rev2.gif)
![Figure 4.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf4a_1o_rev2.gif)
![Figure 5.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf5a_1o_rev4.gif)
![Figure 5.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf5a_1o_rev4.gif)
![Figure 6.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf6a_1o_rev1.gif)
![Figure 6.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf6a_1o_rev1.gif)
![Figure 7.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf7a_1o_rev2.gif)
![Figure 7.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf7a_1o_rev2.gif)
![Figure 8.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf8a_1o_rev2.gif)
![Figure 8.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf8a_1o_rev2.gif)
![Figure 9.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf9a_1o_rev2.gif)
![Figure 9.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf9a_1o_rev2.gif)
![Figure 10.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf10a_1o_rev2.gif)
![Figure 10.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf10a_1o_rev2.gif)
![Figure 11.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf11a_1o_rev2.gif)
![Figure 11.](https://cdn.statically.io/img/www.ncbi.nlm.nih.gov/pmc/articles/instance/551567/bin/GR32284rf11a_1o_rev2.gif)
Similar articles
-
Assembling an arsenal: origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences.Mol Biol Evol. 2004 May;21(5):870-83. doi: 10.1093/molbev/msh091. Epub 2004 Mar 10. Mol Biol Evol. 2004. PMID: 15014162
-
Evolution of an arsenal: structural and functional diversification of the venom system in the advanced snakes (Caenophidia).Mol Cell Proteomics. 2008 Feb;7(2):215-46. doi: 10.1074/mcp.M700094-MCP200. Epub 2007 Sep 12. Mol Cell Proteomics. 2008. PMID: 17855442
-
Tracking the recruitment and evolution of snake toxins using the evolutionary context provided by the Bothrops jararaca genome.Proc Natl Acad Sci U S A. 2021 May 18;118(20):e2015159118. doi: 10.1073/pnas.2015159118. Proc Natl Acad Sci U S A. 2021. PMID: 33972420 Free PMC article.
-
Biochemistry and toxicology of proteins and peptides purified from the venom of Vipera berus berus.Toxicon X. 2022 Jun 12;15:100131. doi: 10.1016/j.toxcx.2022.100131. eCollection 2022 Sep. Toxicon X. 2022. PMID: 35769869 Free PMC article. Review.
-
Colubrid Venom Composition: An -Omics Perspective.Toxins (Basel). 2016 Jul 23;8(8):230. doi: 10.3390/toxins8080230. Toxins (Basel). 2016. PMID: 27455326 Free PMC article. Review.
Cited by
-
The evolutionary novelty of insect defensins: from bacterial killing to toxin neutralization.Cell Mol Life Sci. 2024 May 23;81(1):230. doi: 10.1007/s00018-024-05273-5. Cell Mol Life Sci. 2024. PMID: 38780625 Free PMC article.
-
A Review of Rattlesnake Venoms.Toxins (Basel). 2023 Dec 19;16(1):2. doi: 10.3390/toxins16010002. Toxins (Basel). 2023. PMID: 38276526 Free PMC article. Review.
-
Venomous Noodles: The Evolution of Toxins in Nemertea through Positive Selection and Gene Duplication.Toxins (Basel). 2023 Nov 12;15(11):650. doi: 10.3390/toxins15110650. Toxins (Basel). 2023. PMID: 37999513 Free PMC article.
-
Pulmonary involvement from animal toxins: the cellular mechanisms.J Venom Anim Toxins Incl Trop Dis. 2023 Sep 18;29:e20230026. doi: 10.1590/1678-9199-JVATITD-2023-0026. eCollection 2023. J Venom Anim Toxins Incl Trop Dis. 2023. PMID: 37727535 Free PMC article.
-
Genomic, transcriptomic, and epigenomic analysis of a medicinal snake, Bungarus multicinctus, to provides insights into the origin of Elapidae neurotoxins.Acta Pharm Sin B. 2023 May;13(5):2234-2249. doi: 10.1016/j.apsb.2022.11.015. Epub 2022 Nov 17. Acta Pharm Sin B. 2023. PMID: 37250171 Free PMC article.
References
-
- Aiken, S.P., Sellin, L.C., Schmidt, J.J., Weinstein, S.A., and McArdle, J.J. 1992. A novel peptide toxin from Trimeresurus wagleri acts pre- and post-synaptically to block transmission at the rat neuromuscular junction. Pharmacol. Toxicol. 70: 459-462. - PubMed
-
- Bovy, P.R. 1990. Structure activity in the atrial natriuretic peptide (ANP) family. Med. Res. Rev. 10: 115-142. - PubMed
-
- Chimienti, F., Hogg, R.C., Plantard, L., Lehmann, C., Brakch, N., Fischer, J., Huber, M., Bertrand, D., and Hohl, D. 2003. Identification of SLURP-1 as an epidermal neuromodulator explains the clinical phenotype of Mal de Meleda. Hum. Mol. Genet. 12: 3017-3024. - PubMed
-
- de Plater, G.M., Martin, R.L., and Milburn, P.J. 1998a. The natriuretic peptide (ovCNP-39) from platypus (Ornithorhynchus anatinus) venom relaxes the isolated rat uterus and promotes oedema and mast cell histamine release. Toxicon 36: 847-857. - PubMed
-
- ____. 1998b. A C-type natriuretic peptide from the venom of the platypus (Ornithorhynchus anatinus):structure and pharmacology. Comp. Biochem. Physiol. C Pharmacol. Toxicol. Endocrinol. 120: 99-110. - PubMed
WEB SITE REFERENCES
-
- http://www.expasy.org/cgi-bin/sprot-search-ful; SWISS-PROT accessional nos.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Miscellaneous