Interaction Studies Between Myricetin and papain-like Protease of Infectious Bronchitis Virus
Interaction Studies Between Myricetin and papain-like Protease of Infectious Bronchitis Virus
Samira Ameri Golestan,1,*
1. Department of Genetics, Faculty of Biological Sciences and Technology, Shahid Ashrafi Esfahani University, Isfahan, Iran.
Introduction: The infectious bronchitis virus (IBV) is the cause of avian infectious bronchitis, an acute contact respiratory infectious disease that affects poultry. Controlling avian infectious bronchitis due to the continuous emergence of new serotypes and variants by vaccination is difficult. IBV causes severe economic losses in the poultry industry worldwide. IBV encodes a nonstructural protein called papain-like protease (PLpro). It plays a key role in viral replication and blocking host immune response. Myricetin is a flavonoid found in tea, berries, fruits, wine, and herbs and has been reported to exhibit antiviral, antimicrobial, anticancer, and antiplatelet effects. In this article, we investigate the interaction between myricetin and papain-like protease of infectious bronchitis virus.
Methods: First, the Discovery Studio software version 3.5 was installed on the laptop CPU Intel corei7 9750H – RAM 16GBytes DDR4 – Graphics GTX 1650. 2. In the second stage, various articles were used to obtain the desired protein code. The most frequently used code in the articles was selected as the protein code, and then the enzyme code was entered into the search section of the PDB site to download the desired protein. The code for the desired compound was entered on the PubChem website to obtain the suitable ligand, and its 3D structure was downloaded in SDF format. Since the Discovery Studio software did not support this format, the SDF file was converted to PDB format. The ligand and protein were docked to form a ligand-protein complex using the Auto Dock Vina, version 1.0.5. Using the Discovery Studio program, the different kinds of hydrogen bonds that were created in the ligand-protein complex were analyzed.
Results: The protein (code 4X2Z) and the ligand (code 5281672 myricetin) were selected for interaction analysis and examination. After completing the docking process, the study was carried out using Discovery Studio 3.5 software, and four hydrogen bonds were identified, involving the following amino acids: ALA106, ASN155, THR291 and SER105.
Conclusion: The compound under investigation formed a ligand-protein complex with the Papain-like protease enzyme by creating four hydrogen bonds. It should be noted that the above studies were bioinformatics-based. To confirm the results and for further investigation, it is necessary to examine the inhibitory effects of the compound myricetin on the Papain-like protease enzyme under in vitro conditions.