Generic placeholder image

Journal of Current Toxicology and Venomics

Editor-in-Chief

ISSN (Print): 2950-5704
ISSN (Online): 2950-5712

Research Article

Identification of Linear B-cell Epitopes of Odontobuthus doriae Scorpion Venom Using Peptide Library

Author(s): Abbas Rami, Mahdi Behdani and Fatemeh Kazemi-Lomedasht*

Volume 4, 2024

Published on: 09 January, 2024

Article ID: e26661217280650 Pages: 5

DOI: 10.2174/0126661217280650231204071837

Price: $65

Abstract

Background: Envenomation with Odontobuthus doriae scorpion results in pain at the bite site, inflammation, necrosis, and neurotoxicity. Administration of anti-scorpion antiserum prepared from immunized horses is the main therapy for envenomation. However, in some cases, anaphylactic shock related to antiserum administration limits its use. Therefore, the identification of the venom component and the development of a specific neutralizing agent is very important. Identification of linear epitopes of O. doriae using a peptide-displayed phage library (Ph.D.TM -7) was the main aim of the current study.

Methods: Three rounds of biopanning were performed on immobilized immunoglobulins (IgGs) isolated from the sera of an immunized horse. The biopanning process was checked by polyclonal phage enzymelinked immunosorbent assay (ELISA). Forty blue phage colonies were randomly selected from the third round of biopanning, amplified, DNA extracted and submitted for sequencing.

Results: Polyclonal phage ELISA results confirmed the progress of the biopanning process. The antigens involved in stimulating the horse's immune system were identified, namely sodium channel toxin, potassium channel toxin, chloride channel toxin, cell protein, venom protein, and antimicrobial peptide.

Conclusion: Identified epitopes promise further research to develop novel diagnostic or therapies against O. doriae envenomation.

[1]
Kassiri H, Kasiri N, Dianat A. Species composition, sex ratio, geographical distribution, seasonal and monthly activity of scorpions and epidemiological features of scorpionism in Zarrin-dasht County, Fars Province, Southern Iran. Asian Pac J Trop Dis 2015; 5: S99-S103.
[http://dx.doi.org/10.1016/S2222-1808(15)60867-2]
[2]
Vatanpour H, Jalali A. G Rowan E, Rahim F. Effects of Odontobuthus doriae scorpion venom on mouse sciatic nerve. Iran J Pharm Res 2013; 12: 145-51.
[PMID: 24250682]
[3]
Maertens C, Cuypers E, Amininasab M, Jalali A, Vatanpour H, Tytgat J. Potent modulation of the voltage-gated sodium channel Nav1.7 by OD1, a toxin from the scorpion Odonthobuthus doriae. Mol Pharmacol 2006; 70(1): 405-14.
[http://dx.doi.org/10.1124/mol.106.022970] [PMID: 16641312]
[4]
Jalali A, Bosmans F, Amininasab M, et al. OD1, the first toxin isolated from the venom of the scorpion Odonthobuthus doriae active on voltage‐gated Na + channels. FEBS Lett 2005; 579(19): 4181-6.
[http://dx.doi.org/10.1016/j.febslet.2005.06.052] [PMID: 16038905]
[5]
Boyer L, Degan J, Ruha AM, Mallie J, Mangin E. Alagón A. Safety of intravenous equine F(ab’)2: Insights following clinical trials involving 1534 recipients of scorpion antivenom. Toxicon 2013; 76: 386-93.
[http://dx.doi.org/10.1016/j.toxicon.2013.07.017] [PMID: 23916602]
[6]
Jahdasani R, Jamnani FR, Behdani M, et al. Identification of the immunogenic epitopes of the whole venom component of the Hemiscorpius lepturus scorpion using the phage display peptide library. Toxicon 2016; 124: 83-93.
[http://dx.doi.org/10.1016/j.toxicon.2016.11.247] [PMID: 27845058]
[7]
Kazemi-Lomedasht F, Jamnani FR, Behdani M, Shahbazzadeh D. Linear mimotope analysis of Iranian cobra (Naja oxiana) snake venom using peptide displayed phage library. Toxin Rev 2018.
[8]
Almaaytah A, Albalas Q. Scorpion venom peptides with no disulfide bridges: A review. Peptides 2014; 51: 35-45.
[http://dx.doi.org/10.1016/j.peptides.2013.10.021] [PMID: 24184590]
[9]
Wagstaff SC, Laing GD, Theakston RDG, Papaspyridis C, Harrison RA. Bioinformatics and multiepitope DNA immunization to design rational snake antivenom. PLoS Med 2006; 3(6): e184.
[http://dx.doi.org/10.1371/journal.pmed.0030184] [PMID: 16737347]
[10]
Chen J, Liu H, Yang J, Chou KC. Prediction of linear B-cell epitopes using amino acid pair antigenicity scale. Amino Acids 2007; 33(3): 423-8.
[http://dx.doi.org/10.1007/s00726-006-0485-9] [PMID: 17252308]
[11]
Van Regenmortel MHV. Immunoinformatics may lead to a reappraisal of the nature of B cell epitopes and of the feasibility of synthetic peptide vaccines. J Mol Recognit 2006; 19(3): 183-7.
[http://dx.doi.org/10.1002/jmr.768] [PMID: 16680720]
[12]
Ponomarenko JV, Bourne PE. Antibody-protein interactions: Benchmark datasets and prediction tools evaluation. BMC Struct Biol 2007; 7(1): 64.
[http://dx.doi.org/10.1186/1472-6807-7-64] [PMID: 17910770]
[13]
Hans D, Young P, Fairlie D. Current status of short synthetic peptides as vaccines. Med Chem 2006; 2(6): 627-46.
[http://dx.doi.org/10.2174/1573406410602060627] [PMID: 17105445]
[14]
Arnon R, Ben-Yedidia T. Old and new vaccine approaches. Int Immunopharmacol 2003; 3(8): 1195-204.
[http://dx.doi.org/10.1016/S1567-5769(03)00016-X] [PMID: 12860175]

Rights & Permissions Print Cite
© 2025 Bentham Science Publishers | Privacy Policy