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ORIGINAL RESEARCH article

Front. Pharmacol.
Sec. Integrative and Regenerative Pharmacology
Volume 15 - 2024 | doi: 10.3389/fphar.2024.1464648

First transcriptome analysis of the venom glands of the scorpion Hottentotta zagrosensis (Scorpions: Buthidae) with focus on venom lipolysis activating peptides

Provisionally accepted
Fatemeh Salabi Fatemeh Salabi 1Hedieh Jafari Hedieh Jafari 1Masoud Mahdavinia Masoud Mahdavinia 2Reza Azadnasab Reza Azadnasab 2Saeedeh Shariati Saeedeh Shariati 2Mahsa L. Baghal Mahsa L. Baghal 1Majid Tebianian Majid Tebianian 3Masoumeh Baradaran Masoumeh Baradaran 2*
  • 1 Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization (AREEO), Ahvaz, Iran
  • 2 Toxicology Research Center, Medical Basic Sciences Research Institute, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Khuzestan, Iran
  • 3 Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization (AREEO), Karaj, Alborz, Iran

The final, formatted version of the article will be published soon.

    Introduction: Scorpion venom is a rich source of biological active peptides and proteins.Transcriptome analysis of the venom gland provides detailed insights about peptide and protein venom components. Following the transcriptome analysis of different species in our previous studies, our research team has focused on the Hottentotta zagrosensis as one of the endemic scorpions of Iran to obtain information about its venom proteins, in order to develop biological research focusing on medicinal applications of scorpion venom components and antivenom production. To gain insights into the protein composition of this scorpion venom, we performed transcriptomic analysis.Methods:Transcriptomic analysis of the venom gland of H. zagrosensis, prepared from the Khuzestan province, was performed through Illumina paired-end sequencing(RNA-Seq), Trinity de novo assembly, CD-Hit-EST clustering, and annotation of identified primary structures using bioinformatics approaches.Results:Transcriptome analysis showed the presence of 96.4% of complete arthropod BUSCOs, indicating a high-quality assembly. From total of 45,795,108 paired-end 150 bp trimmed reads, the clustering step resulted in the generation of 101,180 de novo assembled transcripts with N50 size of 1,149 bp. 96,071 Unigenes and 131,235 transcripts had a significant similarity(E-value 1e-3) with known proteins from UniProt, Swissprot, Animal toxin annotation project, and the Pfam database. The results were validated using InterProScan.These mainly correspond to ion channel inhibitors, metalloproteinases, neurotoxins, protease inhibitors, protease activators, Cysteine-rich secretory proteins, phospholipase A enzymes, antimicrobial peptides, growth factors, lipolysis-activating peptides, hyaluronidase, and, phospholipase D. Our venom gland transcriptomic approach identified several biologically active peptides including five LVP1-alpha and LVP1-beta isoforms, which we named HzLVP1_alpha1, HzLVP1_alpha2, HzLVP1_alpha3, HzLVP1_beta1, and HzLVP1_beta and have extremely characterized here.Discussion: Except for HzLVP1_beta1, all other identified LVP1s are predicted to be stable proteins(instability index <40). Moreover, all isoform of LVP1s alpha and beta subunits are thermostable, with the most stability for HzLVP1_alpha2(aliphatic index=71.38). HzLVP1_alpha2 has also the highest half-life.Three-dimensional structure of all identified proteins compacts with three disulfide bridges. The extra cysteine residue may allow the proteins to form a hetero-or homodimer.LVP1 subunits of H. zagrosensis potentially interact with adipose triglyceride lipase(ATGL) and hormone-sensitive lipase (HSL), two key enzymes in regulation of lipolysis in adipocytes, suggesting pharmacological properties of these identified proteins.

    Keywords: lipolysis activating peptide, Hottentotta Zagrosensis, transcriptome analysis, venom gland components, Pharmacological properties

    Received: 14 Jul 2024; Accepted: 29 Oct 2024.

    Copyright: © 2024 Salabi, Jafari, Mahdavinia, Azadnasab, Shariati, Baghal, Tebianian and Baradaran. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence: Masoumeh Baradaran, Toxicology Research Center, Medical Basic Sciences Research Institute, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Khuzestan, Iran

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