Molecular docking of theaflavin-۳-gallate metabolite with protein kinase A, ESX-۱ system, and ESX-۱ secreted protein B (EspB) of Mycobacterium tuberculosis

Molecular docking of major virulence factors of bacteria by bioactive compounds has obtained huge attention in molecular docking studies. Theaflavin-۳-gallate related to the polyphenolic bioflavonoid class isolated from Camellia sinensis leaves has demonstrated anti-inflammatory, anticancer, antibacterial, and antiviral activities as important therapeutic properties. There are several main virulence factors for Mycobacterium tuberculosis, the causative agent of tuberculosis. In the present study, protein kinase A, ESX-۱ system, and ESX-۱ secreted protein B (EspB) were opted to survey molecular docking interaction upon theaflavin-۳-gallate. This investigation revealed that different docking scores resulted from CB-Dock۲ and AutoDock Vina. CB-dock۲ results demonstrated a higher affinity of theaflavin-۳-gallate ligand with protein kinase A receptor. In contrast, based on the results of AutoDock Vina, there was the highest binding affinity for the ESX-۱ system receptor with a binding energy of -۱۰.۱ kcal/mol. Moreover, the STRING database demonstrated higher scores of ۰.۹۹۸ and ۰.۹۹۵ for pstp and EspL for protein kinase A and EspB, respectively.

کلیدواژه ها:

Polyphenolic bioflavonoid ، Virulence factors ، Tuberculosis ، Protein kinase A ، ESX-۱ secreted protein B