About: Structural and functional conservation of the programmed −1 ribosomal frameshift signal of SARS coronavirus 2 (SARS-CoV-2)

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About: Structural and functional conservation of the programmed −1 ribosomal frameshift signal of SARS coronavirus 2 (SARS-CoV-2) Goto Sponge NotDistinct Permalink

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

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Structural and functional conservation of the programmed −1 ribosomal frameshift signal of SARS coronavirus 2 (SARS-CoV-2)
Creator	Neupane, Krishna Dinman, Jonathan Kelly, Jamie Woodside, Michael Emeterio, Josue Munshi, Sneha Olson, Alexandra Pollack, Lois
source	Medline; PMC
abstract	Approximately 17 years after the severe acute respiratory syndrome coronavirus (SARS-CoV) epidemic, the world is currently facing the COVID-19 pandemic caused by SARS corona virus 2 (SARS-CoV-2). According to the most optimistic projections, it will take more than a year to develop a vaccine, so the best short-term strategy may lie in identifying virus-specific targets for small molecule–based interventions. All coronaviruses utilize a molecular mechanism called programmed −1 ribosomal frameshift (−1 PRF) to control the relative expression of their proteins. Previous analyses of SARS-CoV have revealed that it employs a structurally unique three-stemmed mRNA pseudoknot that stimulates high −1 PRF rates and that it also harbors a −1 PRF attenuation element. Altering −1 PRF activity impairs virus replication, suggesting that this activity may be therapeutically targeted. Here, we comparatively analyzed the SARS-CoV and SARS-CoV-2 frameshift signals. Structural and functional analyses revealed that both elements promote similar −1 PRF rates and that silent coding mutations in the slippery sites and in all three stems of the pseudoknot strongly ablate −1 PRF activity. We noted that the upstream attenuator hairpin activity is also functionally retained in both viruses, despite differences in the primary sequence in this region. Small-angle X-ray scattering analyses indicated that the pseudoknots in SARS-CoV and SARS-CoV-2 have the same conformation. Finally, a small molecule previously shown to bind the SARS-CoV pseudoknot and inhibit −1 PRF was similarly effective against −1 PRF in SARS-CoV-2, suggesting that such frameshift inhibitors may be promising lead compounds to combat the current COVID-19 pandemic.
has issue date	2020-07-31(xsd:dateTime)
bibo:doi	10.1074/jbc.ac120.013449
bibo:pmid	32571880
has license	no-cc
sha1sum (hex)	da3b885d4db408a7009c39679e1b432b39f84799
schema:url	https://doi.org/10.1074/jbc.ac120.013449
resource representing a document's title	Structural and functional conservation of the programmed −1 ribosomal frameshift signal of SARS coronavirus 2 (SARS-CoV-2)
has PubMed Central identifier	PMC7397099
has PubMed identifier	32571880
schema:publication	J Biol Chem
resource representing a document's body	covid:da3b885d4db408a7009c39679e1b432b39f84799#body_text
is schema:about of	named entity 'IDENTIFYING' named entity 'pseudoknot' named entity 'corona virus' named entity 'ribosomal frameshift' named entity 'severe acute respiratory syndrome coronavirus' named entity 'frameshift' named entity 'SARS-CoV' named entity 'SARS-CoV-2' named entity 'COVID-19 pandemic' named entity 'SARS-CoV-2' named entity 'conformation' named entity 'SARS-CoV-2' named entity 'SARS-CoV' named entity 'viruses' named entity 'amino acid' named entity 'virus' named entity 'minus-strand' named entity 'SARS-CoV' named entity 'DNA sequencing' named entity 'Promega' named entity 'RNA' named entity 'SARS-CoV' named entity 'Renilla' named entity 'ligand' named entity 'Frameshifting' named entity 'SARS-CoV-2' named entity 'luciferase' named entity 'nucleotides' named entity 'ester' named entity 'primary sequence' named entity 'ligating' named entity 'SAXS' named entity 'SARS-CoV-2' named entity 'frameshift' named entity 'X-ray' named entity 'slippery sequence' named entity 'HEPES' named entity 'coronaviruses' named entity 'cell-based' named entity 'SAXS' named entity 'SARS-CoV-2' named entity 'Luciferase' named entity 'SARS-CoV' named entity 'Plasmids' named entity 'Student's t test' named entity 'reading frame' named entity 'frameshift' named entity 'SARS-CoV-2' named entity 'SARS-CoV-2' named entity 'penicillin' named entity 'T7 polymerase' named entity 'SAXS' named entity 'pseudoknot' named entity 'chromatography' named entity 'frameshift' named entity 'SARS-CoV-2' named entity 'frameshift' named entity 'pseudoknot' named entity 'positive control' named entity 'penicillin' named entity 'ORF2' named entity 'Escherichia coli' named entity 'SARS-CoV-2' named entity 'SEC' named entity 'plasmid' named entity 'SARS-CoV-2' named entity 'antisense' named entity 'avian infectious bronchitis virus' named entity 'coronavirus' named entity 'small-molecule' named entity 'ligand' named entity 'SAXS' named entity 'SARS-CoV' named entity 'single point mutation'

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