Determination of mosquito Larvicidal potential of Bacillus thuringiensis Cry11Ba fusion protein through molecular docking
Autor: | Nadeem Ahmed, Rabbia Pervaiz, Hafsa Naeem, Ahmad Usman Zafar, Mohsin Khan |
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Rok vydání: | 2018 |
Předmět: |
0301 basic medicine
biology In silico Anopheles gambiae fungi 030231 tropical medicine Cell Biology Plant Science Aedes aegypti biology.organism_classification Biochemistry Fusion protein Culex quinquefasciatus 03 medical and health sciences Mosquito control 030104 developmental biology 0302 clinical medicine Bacillus thuringiensis parasitic diseases Genetics Animal Science and Zoology Receptor Molecular Biology Ecology Evolution Behavior and Systematics |
Zdroj: | Biologia. 73:1015-1023 |
ISSN: | 1336-9563 0006-3088 |
DOI: | 10.2478/s11756-018-0103-9 |
Popis: | Mosquitoes spread deadly infections around the world. Since decades Bacillus thuringiensis (Bt) δ-endotoxins have been used successfully as a biopesticide for controlling mosquito larvae. However, over a few years, mosquito larvae have evolved tolerance against Bt δ-endotoxins, rendering them ineffective for mosquito control. Such a problem entails the development of improved toxins with enhanced toxicity, affinity towards a wide range of mosquito receptors and ability to overcome or delay the resistance buildup. In this study, using in silico tools, we aimed to design a fusion protein by fusing active region of Bt subsp. jegathesan Cry11Ba protein with Aedes aegypti TMOF (trypsin modulating oostatic factor). Using computational study, the fusion protein was validated and its mosquitocidal potential was determined through molecular docking against cadherin and aminopeptidase N midgut receptors of Aedes aegypti, Anopheles gambiae and Culex quinquefasciatus. Molecular docking revealed that from Cry11Ba-TMOF fusion protein, domain II amino acids of Cry11Ba protein showed hydrogen bond interactions with cadherin and aminopeptidase N receptors of the targeted mosquitoes. These results conclude that Cry11Ba-TMOF fusion protein has a strong affinity for the receptors of Ae.aegypti, An.gambiae and Cx.quinquefasciatus. Thus the designed fusion protein can be used as a potent mosquitocidal agent for the control of targeted mosquitoes. |
Databáze: | OpenAIRE |
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