Molecular Characterization of a cDNA Encoding of an Anionic Cysteine-Free Antimicrobial Peptide From the Iranian Scorpion Odontobuthus Doriae Venom Glands

Amir Jalali; Masoud Mahdavinia; Hamid Galehdari; Masoumeh Baradaran; Davood Valdi-Biranvand; Maryam Naderi Soork

doi:10.18502/pbr.v8i3.11034

Amir Jalali Department of Operating Room, Langroud School of Allied Medical Sciences, Guilan University of Medical Sciences, Rasht, Iran
Masoud Mahdavinia Department of Toxicology, School of Pharmacy, Toxicology Research center, Medical Basic Sciences Research Institute, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran
Hamid Galehdari Department of Biology, Faculty of Science, Shahid Chamran University of Ahvaz, Ahvaz, Iran
Masoumeh Baradaran Department of Toxicology, School of Pharmacy, Toxicology Research center, Medical Basic Sciences Research Institute, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran
Davood Valdi-Biranvand Department of Toxicology, School of Pharmacy, Toxicology Research center, Medical Basic Sciences Research Institute, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran
Maryam Naderi Soork Department of Biology, Faculty of Science, Shahid Chamran University of Ahvaz, Ahvaz, Iran.

DOI: https://doi.org/10.18502/pbr.v8i3.11034

Keywords: Anionic cysteinefree, Molecular characterization, cDNA library, Odontobuthus doriae, Venom glands

Abstract

Background: The venom peptides from the scorpion fauna of Iran have been poorly characterized so far.

Objectives: In this study, we identified a cDNA encoding of an anionic cysteine-free antimicrobial peptide from the Iranian yellow scorpion odontobuthus doriae (O.doriae).

Methods: The cDNA sequence of an anionic antimicrobial-peptide (AMP) was determined from the venom gland cDNA library of Iranian yellow scorpion O.doriae and was named ODAMP5. This sequence was characterized by a software. Then, the structure and function of its putative peptide were predicted in a bioinformatics manner. The library was constructed from 6 scorpion venom glands. The cDNA related to ODAMP5 was isolated from one positive clone of the library.

Results: The analysis of ODAMP5 reveals a 51-residue mature peptide with an anionic property that was stable in physiological states. ODAMP5 was similar to anionic peptide Aba-2 from Androctonus bicolor and according to its structure, it can be a member of helical structure AMPs with a new type of putative conserved domain. Putative ODAMP5 has a small size which makes it convenient for synthesis.

Conclusion: Furthermore, we created a framework to express the ODAMP5 peptide for future biomedical and pharmacological studies. ODAMP5 may be a new suitable therapeutic strategy for bacterial infection among a few recognized scorpion venom peptides without disulfide bridges.