- Title
- Homology modeling and docking of AahII-Nanobody complexes reveal the epitope binding site on AahII scorpion toxin
- Creator
- Ksouri, Ayoub, Ghedira, Kais, Abderrazek, Rahma Ben, Shankar, B A Gowri, Benkahla, Alia, Tastan Bishop, Özlem, Bouhaouala-Zahar, Balkis
- Date
- 2018
- Type
- text
- Type
- article
- Identifier
- http://hdl.handle.net/10962/124604
- Identifier
- vital:35637
- Identifier
- https://doi.10.1016/j.bbrc.2018.01.036
- Description
- Scorpion envenoming and its treatment is a public health problem in many parts of the world due to highly toxic venom polypeptides diffusing rapidly within the body of severely envenomed victims. Recently, 38 AahII-specific Nanobody sequences (Nbs) were retrieved from which the performance of NbAahII10 nanobody candidate, to neutralize the most poisonous venom compound namely AahII acting on sodium channels, was established. Herein, structural computational approach is conducted to elucidate the Nb-AahII interactions that support the biological characteristics, using Nb multiple sequence alignment (MSA) followed by modeling and molecular docking investigations (RosettaAntibody, ZDOCK software tools). Sequence and structural analysis showed two dissimilar residues of NbAahII10 CDR1 (Tyr27 and Tyr29) and an inserted polar residue Ser30 that appear to play an important role. Indeed, CDR3 region of NbAahII10 is characterized by a specific Met104 and two negatively chargedresidues Asp115 and Asp117. Complex dockings reveal that NbAahII17 and NbAahII38 share one common binding site on the surface of the AahII toxin divergent from the NbAahII10 one's. At least, a couple of NbAahII10 e AahII residue interactions (Gln38 e Asn44 and Arg62, His64, respectively) are mainly involved in the toxic AahII binding site. Altogether, this study gives valuable insights in the design and development of next generation of antivenom.
- Format
- 8 pages, pdf
- Language
- English
- Relation
- Biochemical and Biophysical Research Communications, Ksouri, A., Ghedira, K., Abderrazek, R.B., Shankar, B.G., Benkahla, A., Bishop, O.T. and Bouhaouala-Zahar, B., 2018. Homology modeling and docking of AahII-Nanobody complexes reveal the epitope binding site on AahII scorpion toxin. Biochemical and biophysical research communications, 496(4), pp.1025-1032, Biochemical and Biophysical Research Communications volume 496 number 4 1025 1032 2018 0006-291X
- Rights
- Biochemical and Biophysical Research Communications
- Rights
- Use of this resource is governed by the terms and conditions of the Elsevier Terms & Conditions statement (https://www.elsevier.com/legal/elsevier-website-terms-and-conditions)
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Tastan Bishop, Ozlem (Prof)
RU Department of Biochemistry, Microbiology and Bioinformatics
SDG 03. Good Health and Well-Being
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