tetano
Editor, Senior Moderator
Curr Issues Mol Biol
. 2023 Dec 18;45(12):10225-10247.
doi: 10.3390/cimb45120638. In Silico Analysis of SARS-CoV-2 Non-Structural Proteins Reveals an Interaction with the Host's Heat Shock Proteins That May Contribute to Viral Replications and Development
Mthembu Yamkela[SUP] 1 [/SUP], Zingisa Sitobo[SUP] 1 [/SUP], Xolani H Makhoba[SUP] 2 [/SUP]
Affiliations
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.
Keywords: AdoMetDC; COVID-19; NSP2; SARS-CoV-2; docking; heat shock proteins; molecular dynamics; pharmacophore; polyamines.
. 2023 Dec 18;45(12):10225-10247.
doi: 10.3390/cimb45120638. In Silico Analysis of SARS-CoV-2 Non-Structural Proteins Reveals an Interaction with the Host's Heat Shock Proteins That May Contribute to Viral Replications and Development
Mthembu Yamkela[SUP] 1 [/SUP], Zingisa Sitobo[SUP] 1 [/SUP], Xolani H Makhoba[SUP] 2 [/SUP]
Affiliations
- PMID: 38132484
- PMCID: PMC10742040
- DOI: 10.3390/cimb45120638
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.
Keywords: AdoMetDC; COVID-19; NSP2; SARS-CoV-2; docking; heat shock proteins; molecular dynamics; pharmacophore; polyamines.