SrasV1, PubMed, Checkpoint, bibRecord, 003416

Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein.

Identifieur interne : 003416 ( PubMed/Checkpoint ); précédent : 003415; suivant : 003417

Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein.

Auteurs : M. Godet [France] ; J. Grosclaude ; B. Delmas ; H. Laude

Source :

Journal of virology [ 0022-538X ] ; 1994.

RBID : pubmed:7525985

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Monoclonal, Base Sequence, Binding Sites, Cell Line, DNA Primers, Epitopes (analysis), Fluorescent Antibody Technique, Genetic Vectors, Membrane Glycoproteins (biosynthesis), Membrane Glycoproteins (metabolism), Molecular Sequence Data, Mutagenesis, Site-Directed, Neutralization Tests, Nucleopolyhedroviruses, Polymerase Chain Reaction, Receptors, Virus (metabolism), Recombinant Proteins (biosynthesis), Recombinant Proteins (metabolism), Restriction Mapping, Spike Glycoprotein, Coronavirus, Spodoptera, Swine, Transfection, Transmissible gastroenteritis virus (genetics), Transmissible gastroenteritis virus (metabolism), Viral Envelope Proteins (biosynthesis), Viral Envelope Proteins (metabolism).
MESH :
- chemical , analysis : Epitopes.
- chemical , biosynthesis : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Receptors, Virus, Recombinant Proteins, Viral Envelope Proteins.
- chemical : Antibodies, Monoclonal, DNA Primers, Spike Glycoprotein, Coronavirus.
- genetics : Transmissible gastroenteritis virus.
- metabolism : Transmissible gastroenteritis virus.
- Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Cell Line, Fluorescent Antibody Technique, Genetic Vectors, Molecular Sequence Data, Mutagenesis, Site-Directed, Neutralization Tests, Nucleopolyhedroviruses, Polymerase Chain Reaction, Restriction Mapping, Spodoptera, Swine, Transfection.

Abstract

The spike glycoprotein (S) of coronavirus, the major target for virus-neutralizing antibodies, is assumed to mediate the attachment of virions to the host cell. A 26-kilodalton fragment proteolytically cleaved from transmissible gastroenteritis virus (TGEV) S protein was previously shown to bear two adjacent antigenic sites, A and B, both defined by high-titer neutralizing antibodies. Recombinant baculoviruses expressing C-terminal truncations of the 26-kilodalton region were used to localize functionally important determinants in the S protein primary structure. Two overlapping 223- and 150-amino-acid-long products with serine 506 as a common N terminus expressed all of the site A and B epitopes and induced virus-binding antibodies. Coexpression of one of these truncated protein S derivatives with aminopeptidase N (APN), a cell surface molecule acting as a receptor for TGEV, led to the formation of a complex which could be immunoprecipitated by anti-S antibodies. These data provide evidence that major neutralization-mediating and receptor-binding determinants reside together within a domain of the S protein which behaves like an independent module. In spite of their ability to prevent S-APN interaction, the neutralizing antibodies appeared to recognize a preformed complex, thus indicating that antibody- and receptor-binding determinants should be essentially distinct. Together these findings bring new insight into the molecular mechanism of TGEV neutralization.

PubMed: 7525985

Affiliations:

France

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 003524
to stream PubMed, to step Curation: 003524

Links to Exploration step

pubmed:7525985

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein.</title>
<author><name sortKey="Godet, M" sort="Godet, M" uniqKey="Godet M" first="M" last="Godet">M. Godet</name>
<affiliation wicri:level="1"><nlm:affiliation>Unité de Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, Jouy-en-Josas, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Unité de Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, Jouy-en-Josas</wicri:regionArea>
<wicri:noRegion>Jouy-en-Josas</wicri:noRegion>
<wicri:noRegion>Jouy-en-Josas</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Grosclaude, J" sort="Grosclaude, J" uniqKey="Grosclaude J" first="J" last="Grosclaude">J. Grosclaude</name>
</author>
<author><name sortKey="Delmas, B" sort="Delmas, B" uniqKey="Delmas B" first="B" last="Delmas">B. Delmas</name>
</author>
<author><name sortKey="Laude, H" sort="Laude, H" uniqKey="Laude H" first="H" last="Laude">H. Laude</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="1994">1994</date>
<idno type="RBID">pubmed:7525985</idno>
<idno type="pmid">7525985</idno>
<idno type="wicri:Area/PubMed/Corpus">003524</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">003524</idno>
<idno type="wicri:Area/PubMed/Curation">003524</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">003524</idno>
<idno type="wicri:Area/PubMed/Checkpoint">003416</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">003416</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein.</title>
<author><name sortKey="Godet, M" sort="Godet, M" uniqKey="Godet M" first="M" last="Godet">M. Godet</name>
<affiliation wicri:level="1"><nlm:affiliation>Unité de Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, Jouy-en-Josas, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Unité de Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, Jouy-en-Josas</wicri:regionArea>
<wicri:noRegion>Jouy-en-Josas</wicri:noRegion>
<wicri:noRegion>Jouy-en-Josas</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Grosclaude, J" sort="Grosclaude, J" uniqKey="Grosclaude J" first="J" last="Grosclaude">J. Grosclaude</name>
</author>
<author><name sortKey="Delmas, B" sort="Delmas, B" uniqKey="Delmas B" first="B" last="Delmas">B. Delmas</name>
</author>
<author><name sortKey="Laude, H" sort="Laude, H" uniqKey="Laude H" first="H" last="Laude">H. Laude</name>
</author>
</analytic>
<series><title level="j">Journal of virology</title>
<idno type="ISSN">0022-538X</idno>
<imprint><date when="1994" type="published">1994</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Antibodies, Monoclonal</term>
<term>Base Sequence</term>
<term>Binding Sites</term>
<term>Cell Line</term>
<term>DNA Primers</term>
<term>Epitopes (analysis)</term>
<term>Fluorescent Antibody Technique</term>
<term>Genetic Vectors</term>
<term>Membrane Glycoproteins (biosynthesis)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Molecular Sequence Data</term>
<term>Mutagenesis, Site-Directed</term>
<term>Neutralization Tests</term>
<term>Nucleopolyhedroviruses</term>
<term>Polymerase Chain Reaction</term>
<term>Receptors, Virus (metabolism)</term>
<term>Recombinant Proteins (biosynthesis)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Restriction Mapping</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Spodoptera</term>
<term>Swine</term>
<term>Transfection</term>
<term>Transmissible gastroenteritis virus (genetics)</term>
<term>Transmissible gastroenteritis virus (metabolism)</term>
<term>Viral Envelope Proteins (biosynthesis)</term>
<term>Viral Envelope Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Amorces ADN</term>
<term>Animaux</term>
<term>Anticorps monoclonaux</term>
<term>Cartographie de restriction</term>
<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires (biosynthèse)</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
<term>Lignée cellulaire</term>
<term>Mutagenèse dirigée</term>
<term>Protéines de l'enveloppe virale (biosynthèse)</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
<term>Protéines recombinantes (biosynthèse)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Réaction de polymérisation en chaîne</term>
<term>Récepteurs viraux (métabolisme)</term>
<term>Sites de fixation</term>
<term>Spodoptera</term>
<term>Suidae</term>
<term>Séquence d'acides aminés</term>
<term>Séquence nucléotidique</term>
<term>Technique d'immunofluorescence</term>
<term>Tests de neutralisation</term>
<term>Transfection</term>
<term>Vecteurs génétiques</term>
<term>Virus de la gastroentérite transmissible (génétique)</term>
<term>Virus de la gastroentérite transmissible (métabolisme)</term>
<term>Épitopes (analyse)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Epitopes</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Membrane Glycoproteins</term>
<term>Recombinant Proteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term>
<term>Receptors, Virus</term>
<term>Recombinant Proteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Antibodies, Monoclonal</term>
<term>DNA Primers</term>
<term>Spike Glycoprotein, Coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Épitopes</term>
</keywords>
<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Transmissible gastroenteritis virus</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Virus de la gastroentérite transmissible</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Transmissible gastroenteritis virus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines recombinantes</term>
<term>Récepteurs viraux</term>
<term>Virus de la gastroentérite transmissible</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Base Sequence</term>
<term>Binding Sites</term>
<term>Cell Line</term>
<term>Fluorescent Antibody Technique</term>
<term>Genetic Vectors</term>
<term>Molecular Sequence Data</term>
<term>Mutagenesis, Site-Directed</term>
<term>Neutralization Tests</term>
<term>Nucleopolyhedroviruses</term>
<term>Polymerase Chain Reaction</term>
<term>Restriction Mapping</term>
<term>Spodoptera</term>
<term>Swine</term>
<term>Transfection</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Amorces ADN</term>
<term>Animaux</term>
<term>Anticorps monoclonaux</term>
<term>Cartographie de restriction</term>
<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Lignée cellulaire</term>
<term>Mutagenèse dirigée</term>
<term>Réaction de polymérisation en chaîne</term>
<term>Sites de fixation</term>
<term>Spodoptera</term>
<term>Suidae</term>
<term>Séquence d'acides aminés</term>
<term>Séquence nucléotidique</term>
<term>Technique d'immunofluorescence</term>
<term>Tests de neutralisation</term>
<term>Transfection</term>
<term>Vecteurs génétiques</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">The spike glycoprotein (S) of coronavirus, the major target for virus-neutralizing antibodies, is assumed to mediate the attachment of virions to the host cell. A 26-kilodalton fragment proteolytically cleaved from transmissible gastroenteritis virus (TGEV) S protein was previously shown to bear two adjacent antigenic sites, A and B, both defined by high-titer neutralizing antibodies. Recombinant baculoviruses expressing C-terminal truncations of the 26-kilodalton region were used to localize functionally important determinants in the S protein primary structure. Two overlapping 223- and 150-amino-acid-long products with serine 506 as a common N terminus expressed all of the site A and B epitopes and induced virus-binding antibodies. Coexpression of one of these truncated protein S derivatives with aminopeptidase N (APN), a cell surface molecule acting as a receptor for TGEV, led to the formation of a complex which could be immunoprecipitated by anti-S antibodies. These data provide evidence that major neutralization-mediating and receptor-binding determinants reside together within a domain of the S protein which behaves like an independent module. In spite of their ability to prevent S-APN interaction, the neutralizing antibodies appeared to recognize a preformed complex, thus indicating that antibody- and receptor-binding determinants should be essentially distinct. Together these findings bring new insight into the molecular mechanism of TGEV neutralization.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">7525985</PMID>
<DateCompleted><Year>1994</Year>
<Month>12</Month>
<Day>12</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>04</Month>
<Day>15</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-538X</ISSN>
<JournalIssue CitedMedium="Print"><Volume>68</Volume>
<Issue>12</Issue>
<PubDate><Year>1994</Year>
<Month>Dec</Month>
</PubDate>
</JournalIssue>
<Title>Journal of virology</Title>
<ISOAbbreviation>J. Virol.</ISOAbbreviation>
</Journal>
<ArticleTitle>Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein.</ArticleTitle>
<Pagination><MedlinePgn>8008-16</MedlinePgn>
</Pagination>
<Abstract><AbstractText>The spike glycoprotein (S) of coronavirus, the major target for virus-neutralizing antibodies, is assumed to mediate the attachment of virions to the host cell. A 26-kilodalton fragment proteolytically cleaved from transmissible gastroenteritis virus (TGEV) S protein was previously shown to bear two adjacent antigenic sites, A and B, both defined by high-titer neutralizing antibodies. Recombinant baculoviruses expressing C-terminal truncations of the 26-kilodalton region were used to localize functionally important determinants in the S protein primary structure. Two overlapping 223- and 150-amino-acid-long products with serine 506 as a common N terminus expressed all of the site A and B epitopes and induced virus-binding antibodies. Coexpression of one of these truncated protein S derivatives with aminopeptidase N (APN), a cell surface molecule acting as a receptor for TGEV, led to the formation of a complex which could be immunoprecipitated by anti-S antibodies. These data provide evidence that major neutralization-mediating and receptor-binding determinants reside together within a domain of the S protein which behaves like an independent module. In spite of their ability to prevent S-APN interaction, the neutralizing antibodies appeared to recognize a preformed complex, thus indicating that antibody- and receptor-binding determinants should be essentially distinct. Together these findings bring new insight into the molecular mechanism of TGEV neutralization.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Godet</LastName>
<ForeName>M</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Unité de Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, Jouy-en-Josas, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Grosclaude</LastName>
<ForeName>J</ForeName>
<Initials>J</Initials>
</Author>
<Author ValidYN="Y"><LastName>Delmas</LastName>
<ForeName>B</ForeName>
<Initials>B</Initials>
</Author>
<Author ValidYN="Y"><LastName>Laude</LastName>
<ForeName>H</ForeName>
<Initials>H</Initials>
</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>United States</Country>
<MedlineTA>J Virol</MedlineTA>
<NlmUniqueID>0113724</NlmUniqueID>
<ISSNLinking>0022-538X</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000911">Antibodies, Monoclonal</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D017931">DNA Primers</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000939">Epitopes</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="D011991">Receptors, Virus</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011994">Recombinant Proteins</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>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000911" MajorTopicYN="N">Antibodies, Monoclonal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017931" MajorTopicYN="N">DNA Primers</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000939" MajorTopicYN="N">Epitopes</DescriptorName>
<QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005455" MajorTopicYN="N">Fluorescent Antibody Technique</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005822" MajorTopicYN="N">Genetic Vectors</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName>
<QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009500" MajorTopicYN="N">Neutralization Tests</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017924" MajorTopicYN="N">Nucleopolyhedroviruses</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016133" MajorTopicYN="N">Polymerase Chain Reaction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011991" MajorTopicYN="N">Receptors, Virus</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName>
<QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015183" MajorTopicYN="N">Restriction Mapping</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018411" MajorTopicYN="N">Spodoptera</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013552" MajorTopicYN="N">Swine</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014162" MajorTopicYN="N">Transfection</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005760" MajorTopicYN="N">Transmissible gastroenteritis virus</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName>
<QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1994</Year>
<Month>12</Month>
<Day>1</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>1994</Year>
<Month>12</Month>
<Day>1</Day>
<Hour>0</Hour>
<Minute>1</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>1994</Year>
<Month>12</Month>
<Day>1</Day>
<Hour>0</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">7525985</ArticleId>
<ArticleId IdType="pmc">PMC237264</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>Virology. 1992 Feb;186(2):742-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1310195</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1991 Dec;185(2):732-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1660201</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1992 Jun;188(2):666-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1316677</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1992 Jun 4;357(6377):417-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1350661</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1992 Jun 4;357(6377):420-2</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1350662</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1986 Jan;67 ( Pt 1):119-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2418148</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1986 Jul;67 ( Pt 7):1405-18</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2425049</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1986 Oct;60(1):131-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2427744</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1987 Jul;68 ( Pt 7):1883-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3037011</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1987 Aug 20;196(4):963-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3681988</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1988 Dec;69 ( Pt 12):2939-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3058868</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1989 May;170(1):31-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2497580</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1989 Aug;171(2):493-502</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2548329</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1990 Jan;64(1):339-46</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2403441</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1989 Dec;173(2):664-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2556846</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1990 Jan;174(1):87-94</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2152996</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1990 Feb;71 ( Pt 2):271-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2155284</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biotechniques. 1989 May;7(5):466-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2699236</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1992 Oct;66(10):6194-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1326665</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1992 Sep;190(1):92-105</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1326823</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):1716-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8383324</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Vet Res. 1993;24(2):125-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8393722</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1994 May;75 ( Pt 5):1195-200</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8176382</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Arch Virol. 1994;135(1-2):227-37</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8198447</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Adv Exp Med Biol. 1993;342:293-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7911642</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Adv Exp Med Biol. 1993;342:55-60</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8209771</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1994 Aug;68(8):5216-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7913510</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1990 Jun;64(6):3051-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1692350</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1990 Jun;71 ( Pt 6):1313-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1693663</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1990 Aug;177(2):559-69</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2164725</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1990 Nov;64(11):5367-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2170676</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 1990 Oct 11;18(19):5667-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2216760</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Microbiol. 1990;44:303-33</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2252386</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1990 Nov;71 ( Pt 11):2599-607</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2174956</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1991 Jun;182(2):765-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1850927</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1991 Jul 1;88(13):5533-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1648219</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virus Res. 1991 Jul;20(2):107-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1950169</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1992 Mar;187(1):178-88</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1310555</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>France</li>
</country>
</list>
<tree><noCountry><name sortKey="Delmas, B" sort="Delmas, B" uniqKey="Delmas B" first="B" last="Delmas">B. Delmas</name>
<name sortKey="Grosclaude, J" sort="Grosclaude, J" uniqKey="Grosclaude J" first="J" last="Grosclaude">J. Grosclaude</name>
<name sortKey="Laude, H" sort="Laude, H" uniqKey="Laude H" first="H" last="Laude">H. Laude</name>
</noCountry>
<country name="France"><noRegion><name sortKey="Godet, M" sort="Godet, M" uniqKey="Godet M" first="M" last="Godet">M. Godet</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/PubMed/Checkpoint

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 003416 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd -nk 003416 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    SrasV1
   |flux=    PubMed
   |étape=   Checkpoint
   |type=    RBID
   |clé=     pubmed:7525985
   |texte=   Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/RBID.i   -Sk "pubmed:7525985" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd   \
       | NlmPubMed2Wicri -a SrasV1

This area was generated with Dilib version V0.6.33.
Data generation: Tue Apr 28 14:49:16 2020. Site generation: Sat Mar 27 22:06:49 2021

	Serveur d'exploration SRAS
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration SRAS

Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein.

Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki