Interference of ribosomal frameshifting by antisense peptide nucleic acids suppresses SARS coronavirus replication.
Identifieur interne : 001473 ( PubMed/Checkpoint ); précédent : 001472; suivant : 001474Interference of ribosomal frameshifting by antisense peptide nucleic acids suppresses SARS coronavirus replication.
Auteurs : Dae-Gyun Ahn [Corée du Sud] ; Wooseong Lee ; Jin-Kyu Choi ; Seong-Jun Kim ; Ewan P. Plant ; Fernando Almazán ; Deborah R. Taylor ; Luis Enjuanes ; Jong-Won OhSource :
- Antiviral research [ 1872-9096 ] ; 2011.
Descripteurs français
- KwdFr :
- ARN viral (), ARN viral (génétique), ARN viral (métabolisme), Animaux, Antiviraux (pharmacologie), Cadres ouverts de lecture, Cricetinae, Décalage ribosomique du cadre de lecture, Gènes chevauchants (génétique), Gènes rapporteurs, Génome viral (génétique), Humains, Interféron de type I (biosynthèse), Lignée cellulaire, Luciférases des lucioles, Oligoribonucléotides antisens (génétique), Oligoribonucléotides antisens (métabolisme), Peptides de pénétration cellulaire (génétique), RNA replicase (génétique), RNA replicase (métabolisme), RT-PCR, Réplication virale, Test de retard de migration électrophorétique, Virus du SRAS (génétique), Virus du SRAS (physiologie).
- MESH :
- biosynthèse : Interféron de type I.
- génétique : ARN viral, Gènes chevauchants, Génome viral, Oligoribonucléotides antisens, Peptides de pénétration cellulaire, RNA replicase, Virus du SRAS.
- métabolisme : ARN viral, Oligoribonucléotides antisens, RNA replicase.
- pharmacologie : Antiviraux.
- physiologie : Virus du SRAS.
- ARN viral, Animaux, Cadres ouverts de lecture, Cricetinae, Décalage ribosomique du cadre de lecture, Gènes rapporteurs, Humains, Lignée cellulaire, Luciférases des lucioles, RT-PCR, Réplication virale, Test de retard de migration électrophorétique.
English descriptors
- KwdEn :
- Animals, Antiviral Agents (pharmacology), Cell Line, Cell-Penetrating Peptides (genetics), Cricetinae, Electrophoretic Mobility Shift Assay, Frameshifting, Ribosomal, Genes, Overlapping (genetics), Genes, Reporter, Genome, Viral (genetics), Humans, Interferon Type I (biosynthesis), Luciferases, Firefly, Oligoribonucleotides, Antisense (genetics), Oligoribonucleotides, Antisense (metabolism), Open Reading Frames, RNA Replicase (genetics), RNA Replicase (metabolism), RNA, Viral (chemistry), RNA, Viral (genetics), RNA, Viral (metabolism), Reverse Transcriptase Polymerase Chain Reaction, SARS Virus (genetics), SARS Virus (physiology), Virus Replication.
- MESH :
- chemical , biosynthesis : Interferon Type I.
- chemical , chemistry : RNA, Viral.
- chemical , genetics : Cell-Penetrating Peptides, Oligoribonucleotides, Antisense, RNA Replicase, RNA, Viral.
- chemical , metabolism : Oligoribonucleotides, Antisense, RNA Replicase, RNA, Viral.
- chemical , pharmacology : Antiviral Agents.
- genetics : Genes, Overlapping, Genome, Viral, SARS Virus.
- physiology : SARS Virus.
- Animals, Cell Line, Cricetinae, Electrophoretic Mobility Shift Assay, Frameshifting, Ribosomal, Genes, Reporter, Humans, Luciferases, Firefly, Open Reading Frames, Reverse Transcriptase Polymerase Chain Reaction, Virus Replication.
Abstract
The programmed -1 ribosomal frameshifting (-1 PRF) utilized by eukaryotic RNA viruses plays a crucial role for the controlled, limited synthesis of viral RNA replicase polyproteins required for genome replication. The viral RNA replicase polyproteins of severe acute respiratory syndrome coronavirus (SARS-CoV) are encoded by the two overlapping open reading frames 1a and 1b, which are connected by a -1 PRF signal. We evaluated the antiviral effects of antisense peptide nucleic acids (PNAs) targeting a highly conserved RNA sequence on the - PRF signal. The ribosomal frameshifting was inhibited by the PNA, which bound sequence-specifically a pseudoknot structure in the -1 PRF signal, in cell lines as assessed using a dual luciferase-based reporter plasmid containing the -1 PRF signal. Treatment of cells, which were transfected with a SARS-CoV-replicon expressing firefly luciferase, with the PNA fused to a cell-penetrating peptide (CPP) resulted in suppression of the replication of the SARS-CoV replicon, with a 50% inhibitory concentration of 4.4μM. There was no induction of type I interferon responses by PNA treatment, suggesting that the effect of PNA is not due to innate immune responses. Our results demonstrate that -1 PRF, critical for SARS-CoV viral replication, can be inhibited by CPP-PNA, providing an effective antisense strategy for blocking -1 PRF signals.
DOI: 10.1016/j.antiviral.2011.04.009
PubMed: 21549154
Affiliations:
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The viral RNA replicase polyproteins of severe acute respiratory syndrome coronavirus (SARS-CoV) are encoded by the two overlapping open reading frames 1a and 1b, which are connected by a -1 PRF signal. We evaluated the antiviral effects of antisense peptide nucleic acids (PNAs) targeting a highly conserved RNA sequence on the - PRF signal. The ribosomal frameshifting was inhibited by the PNA, which bound sequence-specifically a pseudoknot structure in the -1 PRF signal, in cell lines as assessed using a dual luciferase-based reporter plasmid containing the -1 PRF signal. Treatment of cells, which were transfected with a SARS-CoV-replicon expressing firefly luciferase, with the PNA fused to a cell-penetrating peptide (CPP) resulted in suppression of the replication of the SARS-CoV replicon, with a 50% inhibitory concentration of 4.4μM. There was no induction of type I interferon responses by PNA treatment, suggesting that the effect of PNA is not due to innate immune responses. Our results demonstrate that -1 PRF, critical for SARS-CoV viral replication, can be inhibited by CPP-PNA, providing an effective antisense strategy for blocking -1 PRF signals.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21549154</PMID><DateCompleted><Year>2011</Year><Month>12</Month><Day>02</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1872-9096</ISSN><JournalIssue CitedMedium="Internet"><Volume>91</Volume><Issue>1</Issue><PubDate><Year>2011</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Antiviral research</Title><ISOAbbreviation>Antiviral Res.</ISOAbbreviation></Journal><ArticleTitle>Interference of ribosomal frameshifting by antisense peptide nucleic acids suppresses SARS coronavirus replication.</ArticleTitle><Pagination><MedlinePgn>1-10</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.antiviral.2011.04.009</ELocationID><Abstract><AbstractText>The programmed -1 ribosomal frameshifting (-1 PRF) utilized by eukaryotic RNA viruses plays a crucial role for the controlled, limited synthesis of viral RNA replicase polyproteins required for genome replication. The viral RNA replicase polyproteins of severe acute respiratory syndrome coronavirus (SARS-CoV) are encoded by the two overlapping open reading frames 1a and 1b, which are connected by a -1 PRF signal. We evaluated the antiviral effects of antisense peptide nucleic acids (PNAs) targeting a highly conserved RNA sequence on the - PRF signal. The ribosomal frameshifting was inhibited by the PNA, which bound sequence-specifically a pseudoknot structure in the -1 PRF signal, in cell lines as assessed using a dual luciferase-based reporter plasmid containing the -1 PRF signal. Treatment of cells, which were transfected with a SARS-CoV-replicon expressing firefly luciferase, with the PNA fused to a cell-penetrating peptide (CPP) resulted in suppression of the replication of the SARS-CoV replicon, with a 50% inhibitory concentration of 4.4μM. There was no induction of type I interferon responses by PNA treatment, suggesting that the effect of PNA is not due to innate immune responses. Our results demonstrate that -1 PRF, critical for SARS-CoV viral replication, can be inhibited by CPP-PNA, providing an effective antisense strategy for blocking -1 PRF signals.</AbstractText><CopyrightInformation>Copyright © 2011 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ahn</LastName><ForeName>Dae-Gyun</ForeName><Initials>DG</Initials><AffiliationInfo><Affiliation>Department of Biotechnology and Translational Research Center for Protein Function Control, Yonsei University, Seoul, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Wooseong</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Choi</LastName><ForeName>Jin-Kyu</ForeName><Initials>JK</Initials></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Seong-Jun</ForeName><Initials>SJ</Initials></Author><Author ValidYN="Y"><LastName>Plant</LastName><ForeName>Ewan P</ForeName><Initials>EP</Initials></Author><Author ValidYN="Y"><LastName>Almazán</LastName><ForeName>Fernando</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Taylor</LastName><ForeName>Deborah R</ForeName><Initials>DR</Initials></Author><Author ValidYN="Y"><LastName>Enjuanes</LastName><ForeName>Luis</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Oh</LastName><ForeName>Jong-Won</ForeName><Initials>JW</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>P01 AI060699</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>04</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Antiviral Res</MedlineTA><NlmUniqueID>8109699</NlmUniqueID><ISSNLinking>0166-3542</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000998">Antiviral Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D057846">Cell-Penetrating Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007370">Interferon Type I</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020320">Oligoribonucleotides, Antisense</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012367">RNA, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.13.12.7</RegistryNumber><NameOfSubstance UI="D049409">Luciferases, Firefly</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.7.48</RegistryNumber><NameOfSubstance UI="D012324">RNA Replicase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000998" MajorTopicYN="N">Antiviral Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057846" MajorTopicYN="N">Cell-Penetrating Peptides</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006224" MajorTopicYN="N">Cricetinae</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D024202" MajorTopicYN="N">Electrophoretic Mobility Shift Assay</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018965" MajorTopicYN="Y">Frameshifting, Ribosomal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005807" MajorTopicYN="N">Genes, Overlapping</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017930" MajorTopicYN="N">Genes, Reporter</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016679" MajorTopicYN="N">Genome, Viral</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007370" MajorTopicYN="N">Interferon Type I</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D049409" MajorTopicYN="N">Luciferases, Firefly</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020320" MajorTopicYN="N">Oligoribonucleotides, Antisense</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016366" MajorTopicYN="N">Open Reading Frames</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012324" MajorTopicYN="N">RNA Replicase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012367" MajorTopicYN="N">RNA, Viral</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020133" MajorTopicYN="N">Reverse Transcriptase Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000235" 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