Open Access Open Badges Research article

Profiling the resting venom gland of the scorpion Tityus stigmurus through a transcriptomic survey

Diego D Almeida1, Katia C Scortecci2, Leonardo S Kobashi3, Lucymara F Agnez-Lima2, Silvia R B Medeiros2, Arnóbio A Silva-Junior1, Inácio de L M Junqueira-de-Azevedo3 and Matheus de F Fernandes-Pedrosa1*

Author affiliations

1 Laboratório de Tecnologia e Biotecnologia Farmacêutica, Universidade Federal do Rio Grande do Norte, Av. Gal. Cordeiro de Farias, s/n, CEP 59010-180 Natal, RN, Brazil

2 Laboratório de Biologia Molecular e Genômica, Universidade Federal do Rio Grande do Norte, Natal, RN, Brazil

3 Centro de Biotecnologia, Instituto Butantan, Av. Prof. Vital Brazil, 1500, CEP 05503-900, São Paulo, SP, Brazil

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Citation and License

BMC Genomics 2012, 13:362  doi:10.1186/1471-2164-13-362

Published: 1 August 2012



The scorpion Tityus stigmurus is widely distributed in Northeastern Brazil and known to cause severe human envenoming, inducing pain, hyposthesia, edema, erythema, paresthesia, headaches and vomiting. The present study uses a transcriptomic approach to characterize the gene expression profile from the non-stimulated venom gland of Tityus stigmurus scorpion.


A cDNA library was constructed and 540 clones were sequenced and grouped into 153 clusters, with one or more ESTs (expressed sequence tags). Forty-one percent of ESTs belong to recognized toxin-coding sequences, with transcripts encoding antimicrobial toxins (AMP-like) being the most abundant, followed by alfa KTx- like, beta KTx-like, beta NaTx-like and alfa NaTx-like. Our analysis indicated that 34% of the transcripts encode “other possible venom molecules”, which correspond to anionic peptides, hypothetical secreted peptides, metalloproteinases, cystein-rich peptides and lectins. Fifteen percent of ESTs are similar to cellular transcripts. Sequences without good matches corresponded to 11%.


This investigation provides the first global view of gene expression of the venom gland from Tityus stigmurus under resting conditions. This approach enables characterization of a large number of venom gland component molecules, which belong either to known or non yet described types of venom peptides and proteins from the Buthidae family.