SrasV1, PubMed, Checkpoint, bibRecord, 002399

Vesicular stomatitis virus pseudotyped with severe acute respiratory syndrome coronavirus spike protein.

Identifieur interne : 002399 ( PubMed/Checkpoint ); précédent : 002398; suivant : 002400

Vesicular stomatitis virus pseudotyped with severe acute respiratory syndrome coronavirus spike protein.

Auteurs : Shuetsu Fukushi [Japon] ; Tetsuya Mizutani [Japon] ; Masayuki Saijo [Japon] ; Shutoku Matsuyama [Japon] ; Naoko Miyajima [Japon] ; Fumihiro Taguchi [Japon] ; Shigeyuki Itamura [Japon] ; Ichiro Kurane [Japon] ; Shigeru Morikawa [Japon]

Source :

The Journal of general virology [ 0022-1317 ] ; 2005.

RBID : pubmed:16033974

Descripteurs français

English descriptors

KwdEn :
- Angiotensin-Converting Enzyme Inhibitors (pharmacology), Animals, Carboxypeptidases (antagonists & inhibitors), Carboxypeptidases (metabolism), Chlorocebus aethiops, Dose-Response Relationship, Drug, Hemagglutinins, Viral (metabolism), Hemagglutinins, Viral (physiology), Humans, Membrane Glycoproteins (metabolism), Membrane Glycoproteins (physiology), Peptidyl-Dipeptidase A, Reassortant Viruses (metabolism), Reassortant Viruses (physiology), Rhabdoviridae Infections (virology), SARS Virus (chemistry), SARS Virus (physiology), Spike Glycoprotein, Coronavirus, Vero Cells, Vesicular stomatitis Indiana virus (metabolism), Vesicular stomatitis Indiana virus (physiology), Viral Envelope Proteins (metabolism), Viral Envelope Proteins (physiology), Virus Replication.
MESH :
- chemical , antagonists & inhibitors : Carboxypeptidases.
- chemical , metabolism : Carboxypeptidases, Hemagglutinins, Viral, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , pharmacology : Angiotensin-Converting Enzyme Inhibitors.
- chemical , physiology : Hemagglutinins, Viral, Membrane Glycoproteins, Viral Envelope Proteins.
- chemistry : SARS Virus.
- metabolism : Reassortant Viruses, Vesicular stomatitis Indiana virus.
- physiology : Reassortant Viruses, SARS Virus, Vesicular stomatitis Indiana virus.
- virology : Rhabdoviridae Infections.
- Animals, Chlorocebus aethiops, Dose-Response Relationship, Drug, Humans, Peptidyl-Dipeptidase A, Spike Glycoprotein, Coronavirus, Vero Cells, Virus Replication.

Abstract

Severe acute respiratory syndrome coronavirus (SARS-CoV) contains a single spike (S) protein, which binds to its receptor, angiotensin-converting enzyme 2 (ACE2), induces membrane fusion and serves as a neutralizing antigen. A SARS-CoV-S protein-bearing vesicular stomatitis virus (VSV) pseudotype using the VSVDeltaG* system was generated. Partial deletion of the SARS-CoV-S protein cytoplasmic domain allowed efficient incorporation into VSV particles and led to the generation of a pseudotype (VSV-SARS-St19) at high titre. Green fluorescent protein expression was demonstrated as early as 7 h after infection of Vero E6 cells with VSV-SARS-St19. VSV-SARS-St19 was neutralized by anti-SARS-CoV antibody and soluble ACE2, and its infection was blocked by treatment of Vero E6 cells with anti-ACE2 antibody. These results indicated that VSV-SARS-St19 infection is mediated by SARS-CoV-S protein in an ACE2-dependent manner. VSV-SARS-St19 will be useful for analysing the function of SARS-CoV-S protein and for developing rapid methods of detecting neutralizing antibodies specific for SARS-CoV infection.

DOI: 10.1099/vir.0.80955-0
PubMed: 16033974

Affiliations:

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Le document en format XML

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<term>Carboxypeptidases (metabolism)</term>
<term>Chlorocebus aethiops</term>
<term>Dose-Response Relationship, Drug</term>
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<term>Reassortant Viruses (physiology)</term>
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<term>SARS Virus (physiology)</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Vero Cells</term>
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<term>Vesicular stomatitis Indiana virus (physiology)</term>
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<term>Carboxypeptidases (métabolisme)</term>
<term>Cellules Vero</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
<term>Glycoprotéines membranaires (physiologie)</term>
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<term>Hémagglutinines virales (métabolisme)</term>
<term>Hémagglutinines virales (physiologie)</term>
<term>Infections à Rhabdoviridae (virologie)</term>
<term>Inhibiteurs de l'enzyme de conversion de l'angiotensine (pharmacologie)</term>
<term>Peptidyl-Dipeptidase A</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
<term>Protéines de l'enveloppe virale (physiologie)</term>
<term>Relation dose-effet des médicaments</term>
<term>Réplication virale</term>
<term>Virus de la stomatite vésiculeuse de type Indiana (métabolisme)</term>
<term>Virus de la stomatite vésiculeuse de type Indiana (physiologie)</term>
<term>Virus du SRAS ()</term>
<term>Virus du SRAS (physiologie)</term>
<term>Virus recombinants (métabolisme)</term>
<term>Virus recombinants (physiologie)</term>
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<term>Hemagglutinins, Viral</term>
<term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Angiotensin-Converting Enzyme Inhibitors</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Hemagglutinins, Viral</term>
<term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
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<keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Carboxypeptidases</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term>
</keywords>
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<term>Glycoprotéines membranaires</term>
<term>Hémagglutinines virales</term>
<term>Protéines de l'enveloppe virale</term>
<term>Virus de la stomatite vésiculeuse de type Indiana</term>
<term>Virus recombinants</term>
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<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Inhibiteurs de l'enzyme de conversion de l'angiotensine</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Glycoprotéines membranaires</term>
<term>Hémagglutinines virales</term>
<term>Protéines de l'enveloppe virale</term>
<term>Virus de la stomatite vésiculeuse de type Indiana</term>
<term>Virus du SRAS</term>
<term>Virus recombinants</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Reassortant Viruses</term>
<term>SARS Virus</term>
<term>Vesicular stomatitis Indiana virus</term>
</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Infections à Rhabdoviridae</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Rhabdoviridae Infections</term>
</keywords>
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<term>Peptidyl-Dipeptidase A</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<term>Virus Replication</term>
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<term>Cellules Vero</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Humains</term>
<term>Peptidyl-Dipeptidase A</term>
<term>Relation dose-effet des médicaments</term>
<term>Réplication virale</term>
<term>Virus du SRAS</term>
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus (SARS-CoV) contains a single spike (S) protein, which binds to its receptor, angiotensin-converting enzyme 2 (ACE2), induces membrane fusion and serves as a neutralizing antigen. A SARS-CoV-S protein-bearing vesicular stomatitis virus (VSV) pseudotype using the VSVDeltaG* system was generated. Partial deletion of the SARS-CoV-S protein cytoplasmic domain allowed efficient incorporation into VSV particles and led to the generation of a pseudotype (VSV-SARS-St19) at high titre. Green fluorescent protein expression was demonstrated as early as 7 h after infection of Vero E6 cells with VSV-SARS-St19. VSV-SARS-St19 was neutralized by anti-SARS-CoV antibody and soluble ACE2, and its infection was blocked by treatment of Vero E6 cells with anti-ACE2 antibody. These results indicated that VSV-SARS-St19 infection is mediated by SARS-CoV-S protein in an ACE2-dependent manner. VSV-SARS-St19 will be useful for analysing the function of SARS-CoV-S protein and for developing rapid methods of detecting neutralizing antibodies specific for SARS-CoV infection.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16033974</PMID>
<DateCompleted><Year>2005</Year>
<Month>09</Month>
<Day>07</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>04</Month>
<Day>15</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-1317</ISSN>
<JournalIssue CitedMedium="Print"><Volume>86</Volume>
<Issue>Pt 8</Issue>
<PubDate><Year>2005</Year>
<Month>Aug</Month>
</PubDate>
</JournalIssue>
<Title>The Journal of general virology</Title>
<ISOAbbreviation>J. Gen. Virol.</ISOAbbreviation>
</Journal>
<ArticleTitle>Vesicular stomatitis virus pseudotyped with severe acute respiratory syndrome coronavirus spike protein.</ArticleTitle>
<Pagination><MedlinePgn>2269-2274</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1099/vir.0.80955-0</ELocationID>
<Abstract><AbstractText>Severe acute respiratory syndrome coronavirus (SARS-CoV) contains a single spike (S) protein, which binds to its receptor, angiotensin-converting enzyme 2 (ACE2), induces membrane fusion and serves as a neutralizing antigen. A SARS-CoV-S protein-bearing vesicular stomatitis virus (VSV) pseudotype using the VSVDeltaG* system was generated. Partial deletion of the SARS-CoV-S protein cytoplasmic domain allowed efficient incorporation into VSV particles and led to the generation of a pseudotype (VSV-SARS-St19) at high titre. Green fluorescent protein expression was demonstrated as early as 7 h after infection of Vero E6 cells with VSV-SARS-St19. VSV-SARS-St19 was neutralized by anti-SARS-CoV antibody and soluble ACE2, and its infection was blocked by treatment of Vero E6 cells with anti-ACE2 antibody. These results indicated that VSV-SARS-St19 infection is mediated by SARS-CoV-S protein in an ACE2-dependent manner. VSV-SARS-St19 will be useful for analysing the function of SARS-CoV-S protein and for developing rapid methods of detecting neutralizing antibodies specific for SARS-CoV infection.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fukushi</LastName>
<ForeName>Shuetsu</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Special Pathogens Laboratory, Department of Virology I, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashimurayama, Tokyo 208-0011, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Mizutani</LastName>
<ForeName>Tetsuya</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Special Pathogens Laboratory, Department of Virology I, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashimurayama, Tokyo 208-0011, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Saijo</LastName>
<ForeName>Masayuki</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Special Pathogens Laboratory, Department of Virology I, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashimurayama, Tokyo 208-0011, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Matsuyama</LastName>
<ForeName>Shutoku</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Laboratory of Respiratory Viral Diseases and SARS, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashimurayama, Tokyo 208-0011, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Miyajima</LastName>
<ForeName>Naoko</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Laboratory of Respiratory Viral Diseases and SARS, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashimurayama, Tokyo 208-0011, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Taguchi</LastName>
<ForeName>Fumihiro</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>Laboratory of Respiratory Viral Diseases and SARS, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashimurayama, Tokyo 208-0011, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Itamura</LastName>
<ForeName>Shigeyuki</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Laboratory of Influenza Virus, Department of Virology III, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashimurayama, Tokyo 208-0011, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kurane</LastName>
<ForeName>Ichiro</ForeName>
<Initials>I</Initials>
<AffiliationInfo><Affiliation>Special Pathogens Laboratory, Department of Virology I, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashimurayama, Tokyo 208-0011, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Morikawa</LastName>
<ForeName>Shigeru</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Special Pathogens Laboratory, Department of Virology I, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashimurayama, Tokyo 208-0011, Japan.</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>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>J Gen Virol</MedlineTA>
<NlmUniqueID>0077340</NlmUniqueID>
<ISSNLinking>0022-1317</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000806">Angiotensin-Converting Enzyme Inhibitors</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D006389">Hemagglutinins, Viral</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C578553">MHV surface projection glycoprotein</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C578557">spike glycoprotein, SARS-CoV</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.-</RegistryNumber>
<NameOfSubstance UI="D002268">Carboxypeptidases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.15.1</RegistryNumber>
<NameOfSubstance UI="D007703">Peptidyl-Dipeptidase A</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.17.-</RegistryNumber>
<NameOfSubstance UI="C413524">angiotensin converting enzyme 2</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000806" MajorTopicYN="N">Angiotensin-Converting Enzyme Inhibitors</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002268" MajorTopicYN="N">Carboxypeptidases</DescriptorName>
<QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004305" MajorTopicYN="N">Dose-Response Relationship, Drug</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006389" MajorTopicYN="N">Hemagglutinins, Viral</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007703" MajorTopicYN="N">Peptidyl-Dipeptidase A</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016865" MajorTopicYN="N">Reassortant Viruses</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018353" MajorTopicYN="N">Rhabdoviridae Infections</DescriptorName>
<QualifierName UI="Q000821" MajorTopicYN="Y">virology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014709" MajorTopicYN="N">Vero Cells</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014721" MajorTopicYN="N">Vesicular stomatitis Indiana virus</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014779" MajorTopicYN="N">Virus Replication</DescriptorName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year>
<Month>7</Month>
<Day>22</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2005</Year>
<Month>9</Month>
<Day>8</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2005</Year>
<Month>7</Month>
<Day>22</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">16033974</ArticleId>
<ArticleId IdType="doi">10.1099/vir.0.80955-0</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>Japon</li>
</country>
<region><li>Région de Kantō</li>
</region>
<settlement><li>Tokyo</li>
</settlement>
</list>
<tree><country name="Japon"><region name="Région de Kantō"><name sortKey="Fukushi, Shuetsu" sort="Fukushi, Shuetsu" uniqKey="Fukushi S" first="Shuetsu" last="Fukushi">Shuetsu Fukushi</name>
</region>
<name sortKey="Itamura, Shigeyuki" sort="Itamura, Shigeyuki" uniqKey="Itamura S" first="Shigeyuki" last="Itamura">Shigeyuki Itamura</name>
<name sortKey="Kurane, Ichiro" sort="Kurane, Ichiro" uniqKey="Kurane I" first="Ichiro" last="Kurane">Ichiro Kurane</name>
<name sortKey="Matsuyama, Shutoku" sort="Matsuyama, Shutoku" uniqKey="Matsuyama S" first="Shutoku" last="Matsuyama">Shutoku Matsuyama</name>
<name sortKey="Miyajima, Naoko" sort="Miyajima, Naoko" uniqKey="Miyajima N" first="Naoko" last="Miyajima">Naoko Miyajima</name>
<name sortKey="Mizutani, Tetsuya" sort="Mizutani, Tetsuya" uniqKey="Mizutani T" first="Tetsuya" last="Mizutani">Tetsuya Mizutani</name>
<name sortKey="Morikawa, Shigeru" sort="Morikawa, Shigeru" uniqKey="Morikawa S" first="Shigeru" last="Morikawa">Shigeru Morikawa</name>
<name sortKey="Saijo, Masayuki" sort="Saijo, Masayuki" uniqKey="Saijo M" first="Masayuki" last="Saijo">Masayuki Saijo</name>
<name sortKey="Taguchi, Fumihiro" sort="Taguchi, Fumihiro" uniqKey="Taguchi F" first="Fumihiro" last="Taguchi">Fumihiro Taguchi</name>
</country>
</tree>
</affiliations>
</record>

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Vesicular stomatitis virus pseudotyped with severe acute respiratory syndrome coronavirus spike protein.

Vesicular stomatitis virus pseudotyped with severe acute respiratory syndrome coronavirus spike protein.

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