Dissecting Toxicity: The Venom Gland Transcriptome and the Venom Proteome of the Highly Venomous Scorpion (Karsch, 1879)

Overview

Journal Toxins (Basel)

Publisher MDPI

Specialty Toxicology

Date 2019 May 5

PMID 31052267

Citations 11

Authors

Jimena I Cid-Uribe

Erika P Meneses

Cesar V F Batista

Ernesto Ortiz

Lourival D Possani

Affiliations

Soon will be listed here.

Abstract

Venom glands and soluble venom from the Mexican scorpion (Karsch, 1879) were used for transcriptomic and proteomic analyses, respectively. An RNA-seq was performed by high-throughput sequencing with the Illumina platform. Approximately 80 million reads were obtained and assembled into 198,662 putative transcripts, of which 11,058 were annotated by similarity to sequences from available databases. A total of 192 venom-related sequences were identified, including Na and K channel-acting toxins, enzymes, host defense peptides, and other venom components. The most diverse transcripts were those potentially coding for ion channel-acting toxins, mainly those active on Na channels (NaScTx). Sequences corresponding to β- scorpion toxins active of K channels (KScTx) and λ-KScTx are here reported for the first time for a scorpion of the genus . Mass fingerprint corroborated that NaScTx are the most abundant components in this venom. Liquid chromatography coupled to mass spectometry (LC-MS/MS) allowed the identification of 46 peptides matching sequences encoded in the transcriptome, confirming their expression in the venom. This study corroborates that, in the venom of toxic buthid scorpions, the more abundant and diverse components are ion channel-acting toxins, mainly NaScTx, while they lack the HDP diversity previously demonstrated for the non-buthid scorpions. The highly abundant and diverse antareases explain the pancreatitis observed after envenomation by this species.

Citing Articles

First evidence of Tityus confluens Borelli, 1899 (Buthidae) venom altering purine metabolism in rat blood cells.

da Silva Portilho R, Brito I, Santos A, Moreschi B, de Lucena M, Otsubo Jaques J Purinergic Signal. 2025; .

PMID: 39992594 DOI: 10.1007/s11302-025-10076-9.

Optimizing Scorpion Toxin Processing through Artificial Intelligence.

Psenicnik A, Ojanguren-Affilastro A, Graham M, Hassan M, Abdel-Rahman M, Sharma P Toxins (Basel). 2024; 16(10).

PMID: 39453213 PMC: 11511117. DOI: 10.3390/toxins16100437.

Unveiling the Protein Components of the Secretory-Venom Gland and Venom of the Scorpion (Buthidae) through Omic Technologies.

Garcia-Villalvazo P, Jimenez-Vargas J, Lino-Lopez G, Meneses E, Bermudez-Guzman M, Barajas-Saucedo C Toxins (Basel). 2023; 15(8).

PMID: 37624255 PMC: 10467079. DOI: 10.3390/toxins15080498.

Bioactive peptides from venoms against glioma progression.

Majc B, Novak M, Lah T, Krizaj I Front Oncol. 2022; 12:965882.

PMID: 36119523 PMC: 9476555. DOI: 10.3389/fonc.2022.965882.

The Enzymatic Core of Scorpion Venoms.

Delgado-Prudencio G, Cid-Uribe J, Morales J, Possani L, Ortiz E, Romero-Gutierrez T Toxins (Basel). 2022; 14(4).

PMID: 35448857 PMC: 9030722. DOI: 10.3390/toxins14040248.

References

Chippaux J, Goyffon M . Epidemiology of scorpionism: a global appraisal. Acta Trop. 2008; 107(2):71-9. DOI: 10.1016/j.actatropica.2008.05.021. View

Conde R, Zamudio F, Becerril B, Possani L . Phospholipin, a novel heterodimeric phospholipase A2 from Pandinus imperator scp6pion venom. FEBS Lett. 1999; 460(3):447-50. DOI: 10.1016/s0014-5793(99)01392-7. View

Santibanez-Lopez C, Francke O, Ureta C, Possani L . Scorpions from Mexico: From Species Diversity to Venom Complexity. Toxins (Basel). 2015; 8(1). PMC: 4728524. DOI: 10.3390/toxins8010002. View

Hill A, Sunde M, Campbell T, Vandenberg J . Mechanism of block of the hERG K+ channel by the scorpion toxin CnErg1. Biophys J. 2007; 92(11):3915-29. PMC: 1868980. DOI: 10.1529/biophysj.106.101956. View

Ramirez A, Martin B, Gurrola G, Possani L . Isolation and characterization of a novel toxin from the venom of the scorpion Centruroides limpidus limpidus Karsch. Toxicon. 1994; 32(4):479-90. DOI: 10.1016/0041-0101(94)90300-x. View

Jablonsky M, WATT D, Krishna N . Solution structure of an Old World-like neurotoxin from the venom of the New World scorpion Centruroides sculpturatus Ewing. J Mol Biol. 1995; 248(2):449-58. DOI: 10.1016/s0022-2836(95)80062-x. View

Ruiming Z, Yibao M, Yawen H, Zhiyong D, Yingliang W, Zhijian C . Comparative venom gland transcriptome analysis of the scorpion Lychas mucronatus reveals intraspecific toxic gene diversity and new venomous components. BMC Genomics. 2010; 11:452. PMC: 3091649. DOI: 10.1186/1471-2164-11-452. View

Gonzalez-Santillan E, Possani L . North American scorpion species of public health importance with a reappraisal of historical epidemiology. Acta Trop. 2018; 187:264-274. DOI: 10.1016/j.actatropica.2018.08.002. View

Touchard A, Aili S, Goncalves Paterson Fox E, Escoubas P, Orivel J, Nicholson G . The Biochemical Toxin Arsenal from Ant Venoms. Toxins (Basel). 2016; 8(1). PMC: 4728552. DOI: 10.3390/toxins8010030. View

10.

Rodriguez de la Vega R, Possani L . Current views on scorpion toxins specific for K+-channels. Toxicon. 2004; 43(8):865-75. DOI: 10.1016/j.toxicon.2004.03.022. View

11.

Tytgat J, Chandy K, Garcia M, Gutman G, Martin-Eauclaire M, Van der Walt J . A unified nomenclature for short-chain peptides isolated from scorpion venoms: alpha-KTx molecular subfamilies. Trends Pharmacol Sci. 1999; 20(11):444-7. DOI: 10.1016/s0165-6147(99)01398-x. View

12.

Romero-Gutierrez T, Peguero-Sanchez E, Cevallos M, Batista C, Ortiz E, Possani L . A Deeper Examination of Thorellius atrox Scorpion Venom Components with Omic Techonologies. Toxins (Basel). 2017; 9(12). PMC: 5744119. DOI: 10.3390/toxins9120399. View

13.

Possani L, Martin B, Fletcher M, Fletcher Jr P . Discharge effect on pancreatic exocrine secretion produced by toxins purified from Tityus serrulatus scorpion venom. J Biol Chem. 1991; 266(5):3178-85. View

14.

Fletcher P, Fletcher M, Fainter L, Terrian D . Action of New World scorpion venom and its neurotoxins in secretion. Toxicon. 1996; 34(11-12):1399-411. DOI: 10.1016/s0041-0101(96)00093-1. View

15.

Wang X, Wang G . Insights into Antimicrobial Peptides from Spiders and Scorpions. Protein Pept Lett. 2016; 23(8):707-21. PMC: 4967028. DOI: 10.2174/0929866523666160511151320. View

16.

Restano-Cassulini R, Olamendi-Portugal T, Zamudio F, Becerril B, Possani L . Two novel ergtoxins, blockers of K+-channels, purified from the Mexican scorpion Centruroides elegans elegans. Neurochem Res. 2008; 33(8):1525-33. DOI: 10.1007/s11064-008-9634-8. View

17.

Zhang L, Shi W, Zeng X, Ge F, Yang M, Nie Y . Unique diversity of the venom peptides from the scorpion Androctonus bicolor revealed by transcriptomic and proteomic analysis. J Proteomics. 2015; 128:231-50. DOI: 10.1016/j.jprot.2015.07.030. View

18.

Zeng X, Zhou L, Shi W, Luo X, Zhang L, Nie Y . Three new antimicrobial peptides from the scorpion Pandinus imperator. Peptides. 2013; 45:28-34. DOI: 10.1016/j.peptides.2013.03.026. View

19.

Alagon A, Guzman H, Martin B, Ramirez A, Carbone E, Possani L . Isolation and characterization of two toxins from the Mexican scorpion Centruroides limpidus limpidus Karsch. Comp Biochem Physiol B. 1988; 89(1):153-61. DOI: 10.1016/0305-0491(88)90277-5. View

20.

Chen Z, Wang B, Hu J, Yang W, Cao Z, Zhuo R . SjAPI, the first functionally characterized Ascaris-type protease inhibitor from animal venoms. PLoS One. 2013; 8(3):e57529. PMC: 3606364. DOI: 10.1371/journal.pone.0057529. View