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System for Efficacy and Cytotoxicity Screening of Inhibitors Targeting Intracellular Mycobacterium tuberculosis
Published on: April 5, 2017
In silico evaluation of snake venom proteins against multidrug-resistant Mycobacterium tuberculosis: A molecular
Maged Fouda1, Mohammad J S Mantargi2, Mousa O Germoush1
1Biology Department, College of Science, Jouf University, Sakaka, Saudi Arabia.
Background:
Mycobacterium tuberculosis (Mtb), a pathogen that belongs to the M. tuberculosis complex, causes tuberculosis (TB), an infectious bacterial disease. Although it usually affects the lungs and results in pulmonary TB, it can also lead to extra-pulmonary TB by affecting other regions of the body. TB, which ranks first on the list of infectious diseases that kill the most people, affects one-third of the world's population and has a high mortality and morbidity rate. The clinical treatment of active TB infection mainly relies on the use of Isoniazid (INH) in combination with three other drugs-rifampin, pyrazinamide, and ethambutol. However, the situation is getting worse due to the rise of extensively drug-resistant tuberculosis (XDR-TB) and multidrug-resistant tuberculosis (MDR-TB). Finding more effective drugs is always a top priority. In this regard, animal venoms, such as snake toxins, contain antibacterial chemicals that have significant therapeutic properties and prevent bacterial infections and disease progression. This suggests that snake venom is a good natural source of promising novel anti-TB drugs.
Aim:
This study examines the snake venom protein's capacity in silico to interrupt the intracellular enzymes of Mtb, which is responsible for the development of MDR-TB in humans.
Methods:
From Research Collaboratory for Structural Bioinformatics (RCSB)-Protein Data Bank, the active protein structure of catalase-peroxidase, RNA polymerase, and snake venom proteins was derived. Using molecular docking software such as PyRx, PyMOL, and Ligplot analyzers the interactions between those proteins and the targeted intracellular proteins were evaluated.
Results:
Our findings reveal fascinating affinities and interaction patterns between snake venom proteins and MDR-TB intracellular enzymes. Analysis of the effects of these interactions and their capacity to impair catalase-peroxidase and RNA polymerase showed that Russell's viper venom proteins were active against the catalase-peroxidase system, whereas Bothrops jararaca venom proteins were active against the RNA polymerase system.
Conclusion:
This study highlights a prospective approach for advancing anti-TB agents by using snake venom proteins to inhibit the growth, replication, and transmission of MDR-TB. This will provide a basis for exploring pharmacophore-based drugs to combat MDR-TB infections.
