Related Experiment Video
Updated: Jul 7, 2025
Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods
Published on: December 21, 2019
In Silico Analysis of SARS-CoV-2 Non-Structural Proteins Reveals an Interaction with the Host's Heat Shock Proteins
Mthembu Yamkela1, Zingisa Sitobo1, Xolani H Makhoba2
1Department of Microbiology and Biochemistry, University of Fort Hare, Alice Campus, Alice 5700, South Africa.
Abstract:
The non-structural protein 2 (NSP2) is an RNA-binding protein involved in coronavirus genome replication, and it often decreases human immune response to promote viral invasion and development. It is believed that the NSP2 associates itself with polyamines and heat shock proteins inside the host cell to proceed with viral development. This study aimed to investigate how the SARS-CoV-2 virus' key non-structural proteins (NSP2) utilize polyamines and heat shock proteins using a molecular docking approach and molecular dynamics (MD). ClusPro and HADDOCK servers were used for the docking and Discovery Studio, chimera, and PyMOL were used for analysis. Docking of the heat shock proteins 40 (HSP40), 70 (HSP70), and 90 (HSP90) with SARS-CoV-2 NSP2 resulted in 32, 28, and 19 interactions, respectively. Molecular dynamics revealed Arg458, Asn508, Met297, Arg301, and Trp417 as active residues, and pharmacophore modeling indicated ZINC395648, ZINC01150525, and ZINC85324008 from the zinc database as possible inhibitors for this NSP2.
