About: The recently emerged SARS-COV2 caused a major pandemic of coronavirus disease (COVID-19). The main goal of this study is to elucidate the structural conformations of non structural protein 1(nsp1), prediction of epitope sites and identification of important residues for targeted therapy against COVID-19. In this study, molecular modelling coupled with molecular dynamics simulations were performed to analyse the conformational change of SARS-COV1, SARS-COV2 and MERS-COV at molecular level. Free energy landscape was constructed by using the first (PC1) and second (PC2) principle components. From the sequence alignment it was observed when compared to SERS-COV1 28 mutations are present in SERS-COV2 nsp1 protein. Several B-cell and T-cell epitopes were identified by immunoinformatics study. The ΔG values for SARS-COV1, SARS-COV2 and MERS-COV nsp1 proteins were 4.44, 5.82 and 6.15 kJ/mol respectively. SARS-COV2 nsp1 protein binds with the interface region of the palm and finger domain of POLA1 by using hydrogen bonds and salt bridges interactions. The present study provided a comprehensive structural model of nsp1 by threading process. The MD simulation parameters indicated that all three nsp1 proteins were stable during the simulation run. These findings can be used to develop therapeutics specific against COVID-19. Highlights Structural elucidation at molecular level of nsp1 of SARS-COV1, SARS-COV2, and MERS-COV Identifications of epitopes by immunoinformatics approach SARS-COV2 nsp1 cover a large conformational space due to greater flexibility Molecular docking between SARS-COV2 nsp1 and POLA1 to identify important residues Structural insights of nsp1 could be used in drug design process against COVID-19 Graphical abstract   Goto Sponge  NotDistinct  Permalink

An Entity of Type : fabio:Abstract, within Data Space : wasabi.inria.fr associated with source document(s)

AttributesValues
type
value
  • The recently emerged SARS-COV2 caused a major pandemic of coronavirus disease (COVID-19). The main goal of this study is to elucidate the structural conformations of non structural protein 1(nsp1), prediction of epitope sites and identification of important residues for targeted therapy against COVID-19. In this study, molecular modelling coupled with molecular dynamics simulations were performed to analyse the conformational change of SARS-COV1, SARS-COV2 and MERS-COV at molecular level. Free energy landscape was constructed by using the first (PC1) and second (PC2) principle components. From the sequence alignment it was observed when compared to SERS-COV1 28 mutations are present in SERS-COV2 nsp1 protein. Several B-cell and T-cell epitopes were identified by immunoinformatics study. The ΔG values for SARS-COV1, SARS-COV2 and MERS-COV nsp1 proteins were 4.44, 5.82 and 6.15 kJ/mol respectively. SARS-COV2 nsp1 protein binds with the interface region of the palm and finger domain of POLA1 by using hydrogen bonds and salt bridges interactions. The present study provided a comprehensive structural model of nsp1 by threading process. The MD simulation parameters indicated that all three nsp1 proteins were stable during the simulation run. These findings can be used to develop therapeutics specific against COVID-19. Highlights Structural elucidation at molecular level of nsp1 of SARS-COV1, SARS-COV2, and MERS-COV Identifications of epitopes by immunoinformatics approach SARS-COV2 nsp1 cover a large conformational space due to greater flexibility Molecular docking between SARS-COV2 nsp1 and POLA1 to identify important residues Structural insights of nsp1 could be used in drug design process against COVID-19 Graphical abstract
subject
  • Viral respiratory tract infections
  • COVID-19
  • Hydrogen physics
  • 2019 disasters in China
part of
is abstract of
is hasSource of
Faceted Search & Find service v1.13.91 as of Mar 24 2020


Alternative Linked Data Documents: Sponger | ODE     Content Formats:       RDF       ODATA       Microdata      About   
This material is Open Knowledge   W3C Semantic Web Technology [RDF Data]
OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software