Abstract
The snake’s venom conformation consists of several enzymes and other proteins which all contribute to the envenomation phenomena. Our objective consists in finding an enzymatic core along a snake-population study in order to achieve a better understanding of the role played by these enzymes. Such identification will build up our hypothesis that all venomous organisms share an enzymatic core. For enzymes identification, transcriptomic data available from selected snake species was processed, followed by an intersection analysis. An enzymatic core composed by 50 enzyme classes was found with an overall high presence of hydrolases. Unexpectedly, among the core components, an elevated amount of serine endopeptidases was identified and associated to the enhancement of the venom’s action in its host, which has been described in the properties of Furin in Loxosceles’ venom. Evidence was found of a correlation between previously described scorpion’s enzymatic core and snake’s enzymatic core described herein, supporting the idea of a shared enzymatic core among all venomous animals.
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References
Post, Y., et al.: Snake venom gland organoids. Cell 180(2), 233–247.e21 (2020). https://doi.org/10.1016/j.cell.2019.11.038
Bottrall, J.L., Madaras, F., Biven, C.D., Venning, M.G., Mirtschin, P.J.: Proteolytic activity of Elapid and Viperid Snake venoms and its implication to digestion (2010)
Thornton, S.L.: Snakes. In: Encyclopedia of Toxicology, pp. 310–312. Elsevier (2014). https://doi.org/10.1016/B978-0-12-386454-3.00786-7
Charvat, R.A., Strobel, R.M., Pasternak, M.A., Klass, S.M., Rheubert, J.L.: Analysis of snake venom composition and antimicrobial activity. Toxicon 150, 151–167 (2018). https://doi.org/10.1016/j.toxicon.2018.05.016
Delgado-Prudencio, G., Cid-Uribe, J.I., Morales, J.A., Possani, L.D., Ortiz, E., Romero-Gutiérrez, T.: The enzymatic core of scorpion venoms. Toxins (Basel) 14(4), 248 (2022). https://doi.org/10.3390/TOXINS14040248
Ramstedt, B., Slotte, J.P.: Membrane properties of sphingomyelins. FEBS Lett. 531(1), 33–37 (2002). https://doi.org/10.1016/S0014-5793(02)03406-3
Dunbar, J.P., Sulpice, R., Dugon, M.M.: The kiss of (cell) death: can venom-induced immune response contribute to dermal necrosis following arthropod envenomations? Clin. Toxicol. 57(8), 677–685 (2019). https://doi.org/10.1080/15563650.2019.1578367
Cid-Uribe, J.I., Veytia-Bucheli, J.I., Romero-Gutierrez, T., Ortiz, E., Possani, L.D.: Scorpion venomics: a 2019 overview. Exp. Rev. Proteomics 17(1), 67–83 (2019). https://doi.org/10.1080/14789450.2020.1705158
Lazarovici, P.: Snake- and spider-venom-derived toxins as lead compounds for drug development. Methods Mol. Biol. 2068, 3–26 (2020). https://doi.org/10.1007/978-1-4939-9845-6_1
Minutti-Zanella, C., Gil-Leyva, E.J., Vergara, I.: Immunomodulatory properties of molecules from animal venoms. Toxicon 191, 54–68 (2021). https://doi.org/10.1016/j.toxicon.2020.12.018. Elsevier Ltd
Costa, T.R., Burin, S.M., Menaldo, D.L., de Castro, F.A., Sampaio, S.V.: Snake venom L-amino acid oxidases: an overview on their antitumor effects. J. Venomous Animals Toxins Includ. Trop. Dis. 20(1), 23 (2014). https://doi.org/10.1186/1678-9199-20-23
Tasoulis, T., Isbister, G.K.: A review and database of snake venom proteomes. Toxins 9(9) (2017). https://doi.org/10.3390/toxins9090290. (MDPI AG)
Adamude, F.A., et al.: Proteomic analysis of three medically important Nigerian Naja (Naja haje, Naja katiensis and Naja nigricollis) snake venoms. Toxicon 197, 24–32 (2021). https://doi.org/10.1016/J.TOXICON.2021.03.014
Bénard-Valle, M., et al.: Functional, proteomic and transcriptomic characterization of the venom from Micrurus browni browni: identification of the first lethal multimeric neurotoxin in coral snake venom. J. Proteomics 225, 103863 (2020). https://doi.org/10.1016/J.JPROT.2020.103863
Santos, W.S., et al.: Proteomic analysis reveals rattlesnake venom modulation of proteins associated with cardiac tissue damage in mouse hearts. J. Proteomics 258, 104530 (2022). https://doi.org/10.1016/J.JPROT.2022.104530
Choksawangkarn, W., et al.: Combined proteomic strategies for in-depth venomic analysis of the beaked sea snake (Hydrophis schistosus) from Songkhla Lake, Thailand. J. Proteomics 259 (2022). https://doi.org/10.1016/j.jprot.2022.104559
Zhang, S.X., et al.: Transcriptome analysis of venom gland and identification of functional genes for snake venom protein in Agkistrodon acutus. Zhongguo Zhong Yao Za Zhi 44(22), 4820–4829 (2019). https://doi.org/10.19540/J.CNKI.CJCMM.20190829.105
Modahl, C.M., Brahma, R.K., Koh, C.Y., Shioi, N., Kini, R.M.: Omics technologies for profiling toxin diversity and evolution in snake venom: impacts on the discovery of therapeutic and diagnostic agents. Annu. Rev. Anim. Biosci. 8, 91–116 (2020). https://doi.org/10.1146/ANNUREV-ANIMAL-021419-083626
Leinonen, R., Sugawara, H., Shumway, M.: The sequence read archive. Nucleic Acids Res. 39(SUPPL), 1 (2011). https://doi.org/10.1093/nar/gkq1019
Bushmanova, E., Antipov, D., Lapidus, A., Prjibelski, A.D.: RnaSPAdes: A de novo transcriptome assembler and its application to RNA-Seq data. Gigascience 8(9) (2019). https://doi.org/10.1093/gigascience/giz100
Prjibelski, A., Antipov, D., Meleshko, D., Lapidus, A., Korobeynikov, A.: Using SPAdes De Novo Assembler. Curr. Protocols Bioinf. 70(1) (2020). https://doi.org/10.1002/cpbi.102
Buchfink, B., Reuter, K., Drost, H.-G.: Brief Communication Sensitive protein alignments at tree-of-life scale using DIAMOND. Nat. Methods https://doi.org/10.1038/s41592-021-01101-x
Chang, A., et al.: BRENDA, the ELIXIR core data resource in 2021: new developments and updates. Nucleic Acids Res. 49(D1), D498–D508 (2021). https://doi.org/10.1093/nar/gkaa1025
Casewell, N.R., Jackson, T.N.W., Laustsen, A.H., Sunagar, K.: Causes and consequences of snake venom variation. Trends Pharmacol. Sci. 41(8), 570–581 (2020). https://doi.org/10.1016/j.tips.2020.05.006
Tan, C.H.: Snake venomics: fundamentals, recent updates, and a look to the next decade. Toxins 14(4) (2022). https://doi.org/10.3390/toxins14040247. (MDPI)
Corrêa-Netto, C., et al.: Snake venomics and venom gland transcriptomic analysis of Brazilian coral snakes, Micrurus altirostris and M. corallinus. J. Proteomics 74(9), 1795–1809 (2011). https://doi.org/10.1016/J.JPROT.2011.04.003
Rodrigues, R.S., et al.: Combined snake venomics and venom gland transcriptomic analysis of Bothropoides pauloensis. J. Proteomics 75(9), 2707–2720 (2012). https://doi.org/10.1016/J.JPROT.2012.03.028
Izidoro, L.F.M., et al.: Snake Venom L-Amino acid oxidases: trends in pharmacology and biochemistry. Biomed. Res. Int. 2014, 1–19 (2014). https://doi.org/10.1155/2014/196754
Hiu, J.J., Yap, M.K.K.: Cytotoxicity of snake venom enzymatic toxins: phospholipase A2 and <scp>l</scp> -amino acid oxidase. Biochem. Soc. Trans. 48(2), 719–731 (2020). https://doi.org/10.1042/BST20200110
Montecucco, C., Gutiérrez, J.M., Lomonte, B.: Cellular pathology induced by snake venom phospholipase A2 myotoxins and neurotoxins: common aspects of their mechanisms of action. Cell. Mol. Life Sci. 65(18), 2897–2912 (2008). https://doi.org/10.1007/s00018-008-8113-3
Laing, G.D., Moura-da-Silva, A.M.: Jararhagin and its multiple effects on hemostasis. Toxicon 45(8), 987–996 (2005). https://doi.org/10.1016/j.toxicon.2005.02.013
Mutter, N.L., Soskine, M., Huang, G., Albuquerque, I.S., Bernardes, G.J.L., Maglia, G.: Modular pore-forming immunotoxins with caged cytotoxicity tailored by directed evolution. ACS Chem. Biol. 13(11), 3153–3160 (2018). https://doi.org/10.1021/acschembio.8b00720
Lopes, P.H., van den Berg, C.W., Tambourgi, D.V.: Sphingomyelinases D from Loxosceles Spider Venoms and Cell Membranes: Action on Lipid Rafts and Activation of Endogenous Metalloproteinases. Front. Pharmacol. 11 (2020). https://doi.org/10.3389/fphar.2020.00636
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Juárez-Zucco, L., Alvarado-Aparicio, V., Romero-Gutiérrez, T., Borrayo, E. (2023). The Enzymatic Core of Snakes. In: Trujillo-Romero, C.J., et al. XLV Mexican Conference on Biomedical Engineering. CNIB 2022. IFMBE Proceedings, vol 86. Springer, Cham. https://doi.org/10.1007/978-3-031-18256-3_26
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