MersV1, Ncbi, Merge, bibRecord, 001035

ATP1A1-mediated Src signaling inhibits coronavirus entry into host cells.

Identifieur interne : 001035 ( Ncbi/Merge ); précédent : 001034; suivant : 001036

ATP1A1-mediated Src signaling inhibits coronavirus entry into host cells.

Auteurs : Christine Burkard [Pays-Bas] ; Monique H. Verheije [Pays-Bas] ; Bart L. Haagmans [Pays-Bas] ; Frank J. Van Kuppeveld [Pays-Bas] ; Peter J M. Rottier [Pays-Bas] ; Berend-Jan Bosch [Pays-Bas] ; Cornelis A M. De Haan [Pays-Bas]

Source :

Journal of virology [ 1098-5514 ] ; 2015.

RBID : pubmed:25653449

Descripteurs français

KwdFr :
- Animaux, Attachement viral (), Bufanolide (pharmacologie), Cellules Vero, Concentration en ions d'hydrogène, Coronavirus félin (physiologie), Extinction de l'expression des gènes, Glucosides cardiotoniques (pharmacologie), Humains, Infections à Coronaviridae (physiopathologie), Lignée cellulaire, Ouabaïne (pharmacologie), Petit ARN interférent (génétique), Pénétration virale (), Réaction de polymérisation en chaine en temps réel, Sodium-Potassium-Exchanging ATPase (métabolisme), Souris, Transduction du signal (physiologie), Virus de l'hépatite murine (physiologie).
MESH :
- génétique : Petit ARN interférent.
- métabolisme : Sodium-Potassium-Exchanging ATPase.
- pharmacologie : Bufanolide, Glucosides cardiotoniques, Ouabaïne.
- physiologie : Coronavirus félin, Transduction du signal, Virus de l'hépatite murine.
- physiopathologie : Infections à Coronaviridae.
- Animaux, Attachement viral, Cellules Vero, Concentration en ions d'hydrogène, Extinction de l'expression des gènes, Humains, Lignée cellulaire, Pénétration virale, Réaction de polymérisation en chaine en temps réel, Souris.

English descriptors

KwdEn :
- Animals, Bufanolides (pharmacology), Cardiac Glycosides (pharmacology), Cell Line, Chlorocebus aethiops, Coronaviridae Infections (physiopathology), Coronavirus, Feline (physiology), Gene Silencing, Humans, Hydrogen-Ion Concentration, Mice, Murine hepatitis virus (physiology), Ouabain (pharmacology), RNA, Small Interfering (genetics), Real-Time Polymerase Chain Reaction, Signal Transduction (physiology), Sodium-Potassium-Exchanging ATPase (metabolism), Vero Cells, Virus Attachment (drug effects), Virus Internalization (drug effects).
MESH :
- chemical , genetics : RNA, Small Interfering.
- chemical , metabolism : Sodium-Potassium-Exchanging ATPase.
- chemical , pharmacology : Bufanolides, Cardiac Glycosides, Ouabain.
- drug effects : Virus Attachment, Virus Internalization.
- physiology : Coronavirus, Feline, Murine hepatitis virus, Signal Transduction.
- physiopathology : Coronaviridae Infections.
- Animals, Cell Line, Chlorocebus aethiops, Gene Silencing, Humans, Hydrogen-Ion Concentration, Mice, Real-Time Polymerase Chain Reaction, Vero Cells.

Abstract

In addition to transporting ions, the multisubunit Na(+),K(+)-ATPase also functions by relaying cardiotonic steroid (CTS)-binding-induced signals into cells. In this study, we analyzed the role of Na(+),K(+)-ATPase and, in particular, of its ATP1A1 α subunit during coronavirus (CoV) infection. As controls, the vesicular stomatitis virus (VSV) and influenza A virus (IAV) were included. Using gene silencing, the ATP1A1 protein was shown to be critical for infection of cells with murine hepatitis virus (MHV), feline infectious peritonitis virus (FIPV), and VSV but not with IAV. Lack of ATP1A1 did not affect virus binding to host cells but resulted in inhibited entry of MHV and VSV. Consistently, nanomolar concentrations of the cardiotonic steroids ouabain and bufalin, which are known not to affect the transport function of Na(+),K(+)-ATPase, inhibited infection of cells with MHV, FIPV, Middle East respiratory syndrome (MERS)-CoV, and VSV, but not IAV, when the compounds were present during virus inoculation. Cardiotonic steroids were shown to inhibit entry of MHV at an early stage, resulting in accumulation of virions close to the cell surface and, as a consequence, in reduced fusion. In agreement with an early block in infection, the inhibition of VSV by CTSs could be bypassed by low-pH shock. Viral RNA replication was not affected when these compounds were added after virus entry. The antiviral effect of ouabain could be relieved by the addition of different Src kinase inhibitors, indicating that Src signaling mediated via ATP1A1 plays a crucial role in the inhibition of CoV and VSV infections.

DOI: 10.1128/JVI.03274-14
PubMed: 25653449

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Le document en format XML

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<front><div type="abstract" xml:lang="en">In addition to transporting ions, the multisubunit Na(+),K(+)-ATPase also functions by relaying cardiotonic steroid (CTS)-binding-induced signals into cells. In this study, we analyzed the role of Na(+),K(+)-ATPase and, in particular, of its ATP1A1 α subunit during coronavirus (CoV) infection. As controls, the vesicular stomatitis virus (VSV) and influenza A virus (IAV) were included. Using gene silencing, the ATP1A1 protein was shown to be critical for infection of cells with murine hepatitis virus (MHV), feline infectious peritonitis virus (FIPV), and VSV but not with IAV. Lack of ATP1A1 did not affect virus binding to host cells but resulted in inhibited entry of MHV and VSV. Consistently, nanomolar concentrations of the cardiotonic steroids ouabain and bufalin, which are known not to affect the transport function of Na(+),K(+)-ATPase, inhibited infection of cells with MHV, FIPV, Middle East respiratory syndrome (MERS)-CoV, and VSV, but not IAV, when the compounds were present during virus inoculation. Cardiotonic steroids were shown to inhibit entry of MHV at an early stage, resulting in accumulation of virions close to the cell surface and, as a consequence, in reduced fusion. In agreement with an early block in infection, the inhibition of VSV by CTSs could be bypassed by low-pH shock. Viral RNA replication was not affected when these compounds were added after virus entry. The antiviral effect of ouabain could be relieved by the addition of different Src kinase inhibitors, indicating that Src signaling mediated via ATP1A1 plays a crucial role in the inhibition of CoV and VSV infections.</div>
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<ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.03274-14</ELocationID>
<Abstract><AbstractText Label="UNLABELLED">In addition to transporting ions, the multisubunit Na(+),K(+)-ATPase also functions by relaying cardiotonic steroid (CTS)-binding-induced signals into cells. In this study, we analyzed the role of Na(+),K(+)-ATPase and, in particular, of its ATP1A1 α subunit during coronavirus (CoV) infection. As controls, the vesicular stomatitis virus (VSV) and influenza A virus (IAV) were included. Using gene silencing, the ATP1A1 protein was shown to be critical for infection of cells with murine hepatitis virus (MHV), feline infectious peritonitis virus (FIPV), and VSV but not with IAV. Lack of ATP1A1 did not affect virus binding to host cells but resulted in inhibited entry of MHV and VSV. Consistently, nanomolar concentrations of the cardiotonic steroids ouabain and bufalin, which are known not to affect the transport function of Na(+),K(+)-ATPase, inhibited infection of cells with MHV, FIPV, Middle East respiratory syndrome (MERS)-CoV, and VSV, but not IAV, when the compounds were present during virus inoculation. Cardiotonic steroids were shown to inhibit entry of MHV at an early stage, resulting in accumulation of virions close to the cell surface and, as a consequence, in reduced fusion. In agreement with an early block in infection, the inhibition of VSV by CTSs could be bypassed by low-pH shock. Viral RNA replication was not affected when these compounds were added after virus entry. The antiviral effect of ouabain could be relieved by the addition of different Src kinase inhibitors, indicating that Src signaling mediated via ATP1A1 plays a crucial role in the inhibition of CoV and VSV infections.</AbstractText>
<AbstractText Label="IMPORTANCE" NlmCategory="OBJECTIVE">Coronaviruses (CoVs) are important pathogens of animals and humans, as demonstrated by the recent emergence of new human CoVs of zoonotic origin. Antiviral drugs targeting CoV infections are lacking. In the present study, we show that the ATP1A1 subunit of Na(+),K(+)-ATPase, an ion transporter and signaling transducer, supports CoV infection. Targeting ATP1A1 either by gene silencing or by low concentrations of the ATP1A1-binding cardiotonic steroids ouabain and bufalin resulted in inhibition of infection with murine, feline, and MERS-CoVs at an early entry stage. Infection with the control virus VSV was also inhibited. Src signaling mediated by ATP1A1 was shown to play a crucial role in the inhibition of virus entry by ouabain and bufalin. These results suggest that targeting the Na(+),K(+)-ATPase using cardiotonic steroids, several of which are FDA-approved compounds, may be an attractive therapeutic approach against CoV and VSV infections.</AbstractText>
<CopyrightInformation>Copyright © 2015, American Society for Microbiology. All Rights Reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Burkard</LastName>
<ForeName>Christine</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Verheije</LastName>
<ForeName>Monique H</ForeName>
<Initials>MH</Initials>
<AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Haagmans</LastName>
<ForeName>Bart L</ForeName>
<Initials>BL</Initials>
<AffiliationInfo><Affiliation>Department of Viroscience, Erasmus MC, Rotterdam, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>van Kuppeveld</LastName>
<ForeName>Frank J</ForeName>
<Initials>FJ</Initials>
<AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Rottier</LastName>
<ForeName>Peter J M</ForeName>
<Initials>PJ</Initials>
<AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bosch</LastName>
<ForeName>Berend-Jan</ForeName>
<Initials>BJ</Initials>
<AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>de Haan</LastName>
<ForeName>Cornelis A M</ForeName>
<Initials>CA</Initials>
<AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands c.a.m.dehaan@uu.nl.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2015</Year>
<Month>02</Month>
<Day>04</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>J Virol</MedlineTA>
<NlmUniqueID>0113724</NlmUniqueID>
<ISSNLinking>0022-538X</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D002018">Bufanolides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D002301">Cardiac Glycosides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D034741">RNA, Small Interfering</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>5ACL011P69</RegistryNumber>
<NameOfSubstance UI="D010042">Ouabain</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber>
<NameOfSubstance UI="C499076">ATP1A1 protein, human</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 7.2.2.13</RegistryNumber>
<NameOfSubstance UI="D000254">Sodium-Potassium-Exchanging ATPase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>U549S98QLW</RegistryNumber>
<NameOfSubstance UI="C022777">bufalin</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002018" MajorTopicYN="N">Bufanolides</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002301" MajorTopicYN="N">Cardiac Glycosides</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003333" MajorTopicYN="N">Coronaviridae Infections</DescriptorName>
<QualifierName UI="Q000503" MajorTopicYN="Y">physiopathology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016765" MajorTopicYN="N">Coronavirus, Feline</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020868" MajorTopicYN="N">Gene Silencing</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006517" MajorTopicYN="N">Murine hepatitis virus</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010042" MajorTopicYN="N">Ouabain</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D034741" MajorTopicYN="N">RNA, Small Interfering</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D060888" MajorTopicYN="N">Real-Time Polymerase Chain Reaction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000254" MajorTopicYN="N">Sodium-Potassium-Exchanging ATPase</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014709" MajorTopicYN="N">Vero Cells</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053585" MajorTopicYN="N">Virus Attachment</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053586" MajorTopicYN="N">Virus Internalization</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName>
</MeshHeading>
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<Day>6</Day>
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</PubmedData>
</pubmed>
<affiliations><list><country><li>Pays-Bas</li>
</country>
<region><li>Hollande-Méridionale</li>
<li>Utrecht (province)</li>
</region>
<settlement><li>Rotterdam</li>
<li>Utrecht</li>
</settlement>
<orgName><li>Université d'Utrecht</li>
</orgName>
</list>
<tree><country name="Pays-Bas"><region name="Utrecht (province)"><name sortKey="Burkard, Christine" sort="Burkard, Christine" uniqKey="Burkard C" first="Christine" last="Burkard">Christine Burkard</name>
</region>
<name sortKey="Bosch, Berend Jan" sort="Bosch, Berend Jan" uniqKey="Bosch B" first="Berend-Jan" last="Bosch">Berend-Jan Bosch</name>
<name sortKey="De Haan, Cornelis A M" sort="De Haan, Cornelis A M" uniqKey="De Haan C" first="Cornelis A M" last="De Haan">Cornelis A M. De Haan</name>
<name sortKey="Haagmans, Bart L" sort="Haagmans, Bart L" uniqKey="Haagmans B" first="Bart L" last="Haagmans">Bart L. Haagmans</name>
<name sortKey="Rottier, Peter J M" sort="Rottier, Peter J M" uniqKey="Rottier P" first="Peter J M" last="Rottier">Peter J M. Rottier</name>
<name sortKey="Van Kuppeveld, Frank J" sort="Van Kuppeveld, Frank J" uniqKey="Van Kuppeveld F" first="Frank J" last="Van Kuppeveld">Frank J. Van Kuppeveld</name>
<name sortKey="Verheije, Monique H" sort="Verheije, Monique H" uniqKey="Verheije M" first="Monique H" last="Verheije">Monique H. Verheije</name>
</country>
</tree>
</affiliations>
</record>

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{{Explor lien
   |wiki=    Sante
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   |clé=     pubmed:25653449
   |texte=   ATP1A1-mediated Src signaling inhibits coronavirus entry into host cells.
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	Serveur d'exploration MERS
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Serveur d'exploration MERS

ATP1A1-mediated Src signaling inhibits coronavirus entry into host cells.

ATP1A1-mediated Src signaling inhibits coronavirus entry into host cells.

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