Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1 subunit-specific monoclonal antibody.
Identifieur interne : 003411 ( PubMed/Checkpoint ); précédent : 003410; suivant : 003412Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1 subunit-specific monoclonal antibody.
Auteurs : B. Grosse [Allemagne] ; S G SiddellSource :
- Virology [ 0042-6822 ] ; 1994.
Descripteurs français
- KwdFr :
- Amorces ADN (), Anticorps antiviraux (immunologie), Anticorps monoclonaux (immunologie), Antigènes viraux (), Conformation des protéines, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (immunologie), Mutagenèse dirigée, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (immunologie), Relation structure-activité, Séquence d'acides aminés, Séquence nucléotidique, Tests de neutralisation, Virus de l'hépatite murine (immunologie).
- MESH :
- immunologie : Anticorps antiviraux, Anticorps monoclonaux, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Virus de l'hépatite murine.
- Amorces ADN, Antigènes viraux, Conformation des protéines, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Mutagenèse dirigée, Protéines de l'enveloppe virale, Relation structure-activité, Séquence d'acides aminés, Séquence nucléotidique, Tests de neutralisation.
English descriptors
- KwdEn :
- Amino Acid Sequence, Antibodies, Monoclonal (immunology), Antibodies, Viral (immunology), Antigens, Viral (chemistry), Base Sequence, DNA Primers (chemistry), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (immunology), Molecular Sequence Data, Murine hepatitis virus (immunology), Mutagenesis, Site-Directed, Neutralization Tests, Protein Conformation, Spike Glycoprotein, Coronavirus, Structure-Activity Relationship, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (immunology).
- MESH :
- chemical , chemistry : Antigens, Viral, DNA Primers, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , immunology : Antibodies, Monoclonal, Antibodies, Viral, Membrane Glycoproteins, Viral Envelope Proteins.
- immunology : Murine hepatitis virus.
- Amino Acid Sequence, Base Sequence, Molecular Sequence Data, Mutagenesis, Site-Directed, Neutralization Tests, Protein Conformation, Spike Glycoprotein, Coronavirus, Structure-Activity Relationship.
Abstract
We have isolated 10 monoclonal-antibody-resistant variants (MAR variants) of the murine hepatitis virus (MHV) by selection with a neutralizing monoclonal antibody that binds to the S1 subunit of the surface glycoprotein (MAb 11F, E. Routledge et al., J. Virol. 65, 254-262, 1991). The variant viruses escape neutralization and are able to mediate membrane fusion in the presence of high concentrations of antibody. Sequence analysis of the variant S protein genes showed that they are not mutated in the codons for the amino acids that bind MAb 11F (positions 33 to 40). Instead, they have mutations that encode single amino acid changes in the S2 subunit of the protein (positions 1109, 1110, and 1116). These amino acid substitutions are conservative. Using a T7/vaccinia virus system, we have confirmed that each of the S2 subunit substitutions is able to confer the MAR phenotype on transiently expressed S proteins. The indirect immunoprecipitation of metabolically labeled S protein from cell lysates of MHV- or MAR variant-infected cells shows that the MAR-variant S proteins no longer bind MAb 11F, although they are still bound by a large panel of monoclonal antibodies that recognize many different discontinuous and linear determinants on both the S1 and S2 subunits of the protein. These data provide new insights into the interaction between defined regions of the S1 and S2 subunits of the MHV S protein.
DOI: 10.1006/viro.1994.1403
PubMed: 8030244
Affiliations:
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Grosse</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Virology, University of Würzburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute of Virology, University of Würzburg</wicri:regionArea><wicri:noRegion>University of Würzburg</wicri:noRegion><wicri:noRegion>University of Würzburg</wicri:noRegion><wicri:noRegion>University of Würzburg</wicri:noRegion></affiliation></author><author><name sortKey="Siddell, S G" sort="Siddell, S G" uniqKey="Siddell S" first="S G" last="Siddell">S G Siddell</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1994">1994</date><idno type="RBID">pubmed:8030244</idno><idno type="pmid">8030244</idno><idno type="doi">10.1006/viro.1994.1403</idno><idno type="wicri:Area/PubMed/Corpus">003527</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">003527</idno><idno type="wicri:Area/PubMed/Curation">003527</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">003527</idno><idno type="wicri:Area/PubMed/Checkpoint">003411</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">003411</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1 subunit-specific monoclonal antibody.</title><author><name sortKey="Grosse, B" sort="Grosse, B" uniqKey="Grosse B" first="B" last="Grosse">B. Grosse</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Virology, University of Würzburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute of Virology, University of Würzburg</wicri:regionArea><wicri:noRegion>University of Würzburg</wicri:noRegion><wicri:noRegion>University of Würzburg</wicri:noRegion><wicri:noRegion>University of Würzburg</wicri:noRegion></affiliation></author><author><name sortKey="Siddell, S G" sort="Siddell, S G" uniqKey="Siddell S" first="S G" last="Siddell">S G Siddell</name></author></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</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>Antibodies, Monoclonal (immunology)</term><term>Antibodies, Viral (immunology)</term><term>Antigens, Viral (chemistry)</term><term>Base Sequence</term><term>DNA Primers (chemistry)</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (immunology)</term><term>Molecular Sequence Data</term><term>Murine hepatitis virus (immunology)</term><term>Mutagenesis, Site-Directed</term><term>Neutralization Tests</term><term>Protein Conformation</term><term>Spike Glycoprotein, Coronavirus</term><term>Structure-Activity Relationship</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (immunology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Amorces ADN ()</term><term>Anticorps antiviraux (immunologie)</term><term>Anticorps monoclonaux (immunologie)</term><term>Antigènes viraux ()</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Glycoprotéines membranaires (immunologie)</term><term>Mutagenèse dirigée</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (immunologie)</term><term>Relation structure-activité</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Tests de neutralisation</term><term>Virus de l'hépatite murine (immunologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antigens, Viral</term><term>DNA Primers</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Antibodies, Viral</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps antiviraux</term><term>Anticorps monoclonaux</term><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Virus de l'hépatite murine</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Neutralization Tests</term><term>Protein Conformation</term><term>Spike Glycoprotein, Coronavirus</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Amorces ADN</term><term>Antigènes viraux</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Mutagenèse dirigée</term><term>Protéines de l'enveloppe virale</term><term>Relation structure-activité</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Tests de neutralisation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have isolated 10 monoclonal-antibody-resistant variants (MAR variants) of the murine hepatitis virus (MHV) by selection with a neutralizing monoclonal antibody that binds to the S1 subunit of the surface glycoprotein (MAb 11F, E. Routledge et al., J. Virol. 65, 254-262, 1991). The variant viruses escape neutralization and are able to mediate membrane fusion in the presence of high concentrations of antibody. Sequence analysis of the variant S protein genes showed that they are not mutated in the codons for the amino acids that bind MAb 11F (positions 33 to 40). Instead, they have mutations that encode single amino acid changes in the S2 subunit of the protein (positions 1109, 1110, and 1116). These amino acid substitutions are conservative. Using a T7/vaccinia virus system, we have confirmed that each of the S2 subunit substitutions is able to confer the MAR phenotype on transiently expressed S proteins. The indirect immunoprecipitation of metabolically labeled S protein from cell lysates of MHV- or MAR variant-infected cells shows that the MAR-variant S proteins no longer bind MAb 11F, although they are still bound by a large panel of monoclonal antibodies that recognize many different discontinuous and linear determinants on both the S1 and S2 subunits of the protein. These data provide new insights into the interaction between defined regions of the S1 and S2 subunits of the MHV S protein.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8030244</PMID><DateCompleted><Year>1994</Year><Month>08</Month><Day>11</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0042-6822</ISSN><JournalIssue CitedMedium="Print"><Volume>202</Volume><Issue>2</Issue><PubDate><Year>1994</Year><Month>Aug</Month><Day>01</Day></PubDate></JournalIssue><Title>Virology</Title><ISOAbbreviation>Virology</ISOAbbreviation></Journal><ArticleTitle>Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1 subunit-specific monoclonal antibody.</ArticleTitle><Pagination><MedlinePgn>814-24</MedlinePgn></Pagination><Abstract><AbstractText>We have isolated 10 monoclonal-antibody-resistant variants (MAR variants) of the murine hepatitis virus (MHV) by selection with a neutralizing monoclonal antibody that binds to the S1 subunit of the surface glycoprotein (MAb 11F, E. Routledge et al., J. Virol. 65, 254-262, 1991). The variant viruses escape neutralization and are able to mediate membrane fusion in the presence of high concentrations of antibody. Sequence analysis of the variant S protein genes showed that they are not mutated in the codons for the amino acids that bind MAb 11F (positions 33 to 40). Instead, they have mutations that encode single amino acid changes in the S2 subunit of the protein (positions 1109, 1110, and 1116). These amino acid substitutions are conservative. Using a T7/vaccinia virus system, we have confirmed that each of the S2 subunit substitutions is able to confer the MAR phenotype on transiently expressed S proteins. The indirect immunoprecipitation of metabolically labeled S protein from cell lysates of MHV- or MAR variant-infected cells shows that the MAR-variant S proteins no longer bind MAb 11F, although they are still bound by a large panel of monoclonal antibodies that recognize many different discontinuous and linear determinants on both the S1 and S2 subunits of the protein. These data provide new insights into the interaction between defined regions of the S1 and S2 subunits of the MHV S protein.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Grosse</LastName><ForeName>B</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Institute of Virology, University of Würzburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Siddell</LastName><ForeName>S G</ForeName><Initials>SG</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>Virology</MedlineTA><NlmUniqueID>0110674</NlmUniqueID><ISSNLinking>0042-6822</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1994</Year><Month>8</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1994</Year><Month>8</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1994</Year><Month>8</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8030244</ArticleId><ArticleId 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