Open AccessPHYTOCHEMICAL TO INTERACT WITH NLS BINDING SITE ON IMA3 TO INHIBIT IMPORTIN Α/Β1 MEDIATED NUCLEAR IMPORT OF SARS-COV-2 CARGO
Author(s) -
Basavapattana Rudresh Bharath,
Hrishikesh Damle,
Shiban Ganju,
Latha Damle
Publication year - 2020
Publication title -
international journal of pharmacy and pharmaceutical sciences/international journal of pharmacy and pharmaceutical sciences
Language(s) - English
Resource type - Journals
eISSN - 2656-0097
pISSN - 0975-1491
DOI - 10.22159/ijpps.2020v12i8.38184
Subject(s) - importin , nls , nuclear transport , integrase , docking (animal) , phytochemical , ran , chemistry , virology , nuclear localization sequence , biology , stereochemistry , biochemistry , human immunodeficiency virus (hiv) , medicine , cell nucleus , gene , veterinary medicine
Objective: Ivermectin is an FDA-approved, broad-spectrum anti-parasitic agent. It was originally identified as an inhibitor of interaction between the human 29 immunodeficiency virus-1 (HIV-1) integrase protein (IN) and the Importin (IMP) α/β1 30 heterodimers, which are responsible for IN nuclear import. Recent studies demonstrate that ivermectin is worthy of further consideration as a possible SARS-CoV-2 antiviral.
Methods: We built the pathogen-host interactome and analyzed it using PHISTO. We compared Ivermectin and plant molecules for their interaction with Importin α3 (IMA3) using molecular docking studies.
Results: A phytochemical ATRI001 with the lowest binding energy-7.290 Kcal/mol was found to be superior to Ivermectin with binding energy-4.946 Kcal/mol.
Conclusion: ATRI001 may be a potential anti-SARS-CoV-2 agent; however, it requires clinical evaluation.