Molecular Characterization of a cDNA Encoding of an Anionic Cysteine-Free Antimicrobial Peptide From the Iranian Scorpion Odontobuthus Doriae Venom Glands
- سال انتشار: 1401
- محل انتشار: مجله تحقیقات دارویی و بیومدیک، دوره: 8، شماره: 3
- کد COI اختصاصی: JR_PBRE-8-3_005
- زبان مقاله: انگلیسی
- تعداد مشاهده: 174
نویسندگان
Department of Operating Room, Langroud School of Allied Medical Sciences, Guilan University of Medical Sciences, Rasht, Iran.
Department of Toxicology, School of Pharmacy, Toxicology Research Center, Medical Basic Sciences Research Institute, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran.
Department of Biology, Faculty of Science, Shahid Chamran University of Ahvaz, Ahvaz, Iran.
Department of Toxicology, School of Pharmacy, Toxicology Research center, Medical Basic Sciences Research Institute, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran
Department of Toxicology, School of Pharmacy, Toxicology Research center, Medical Basic Sciences Research Institute, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran
Department of Biology, Faculty of Science, Shahid Chamran University of Ahvaz, Ahvaz, Iran.
چکیده
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 ODAMP۵. 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 ۶ scorpion venom glands. The cDNA related to ODAMP۵ was isolated from one positive clone of the library. Results: The analysis of ODAMP۵ reveals a ۵۱-residue mature peptide with an anionic property that was stable in physiological states. ODAMP۵ was similar to anionic peptide Aba-۲ 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 ODAMP۵ has a small size which makes it convenient for synthesis. Conclusion: Furthermore, we created a framework to express the ODAMP۵ peptide for future biomedical and pharmacological studies. ODAMP۵ may be a new suitable therapeutic strategy for bacterial infection among a few recognized scorpion venom peptides without disulfide bridges.کلیدواژه ها
Anionic cysteine-free, Molecular characterization, cDNA library, Odontobuthus doriae, Venom glandsاطلاعات بیشتر در مورد COI
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