Three antibody molecules can bind simultaneously to each monomer of the tetramer of influenza virus neuraminidase and the trimer of influenza virus hemagglutinin
Identifieur interne : 001216 ( Istex/Corpus ); précédent : 001215; suivant : 001217Three antibody molecules can bind simultaneously to each monomer of the tetramer of influenza virus neuraminidase and the trimer of influenza virus hemagglutinin
Auteurs : D. C. Jackson ; B. S. Crabb ; P. Poumbourios ; W. R. Tulip ; W. G. LaverSource :
- Archives of Virology [ 0304-8608 ] ; 1991-03-01.
English descriptors
- Teeft :
- Amino acid sequences, Antibody, Antibody binding, Antibody fragments, Antibody molecules, Antigenic, Antigenic determinants, Antigenic sites, Antigenic structure, Available surface area, Avian virus, Carbohydrate side chains, Clear evidence, Conformational changes, Constant amount, Dimensional structure, Elution profiles, Elution time, Epitope, Final concentration, Flow rate, Fplc system, Gradient length, Hemagglutinin, Immune, Immune complexes, Immunol, Individual fractions, Influenza, Influenza virus, Influenza virus hemagglutinin, Influenza virus neuraminidase, Influenza viruses, Large number, Laver, Linear sucrose gradients, Molecular mass, Molecular weight, Monoclonal, Monoclonal antibodies, Monovalent, Monovalent antibody, Monovalent antibody fragments, Neuraminidase, Normal rabbit, Pbsa, Permeation chromatography, Physical properties, Polyclonal antibody preparation, Present study, Protein surface, Relative mobilities, Room temperature, Saturating conditions, Sedimentation, Sedimentation coefficient, Sedimentation coefficients, Species stokes, Standard proteins, Steric constraints, Steric hindrance, Stokes, Sucrose, Surface area, Varghese, Velocity sedimentation experiments, Virology.
Abstract
Summary: Trimeric hemagglutinin and tetrameric neuraminidase molecules isolated from influenza virus bind an average of 9 and 13 molecules respectively of monovalent antibody fragments prepared from IgG isolated from polyclonal sera. In each case this represents an average of approximately three molecules of antibody binding to each protomer. Although there is compelling evidence for the presence of multiple adjacent and overlapping epitopes covering the surface of these two viral antigens, steric hindrance ensures that even under saturating conditions only three molecules of monovalent antibody fragments can be simultaneously accommodated on each monomer.
Url:
DOI: 10.1007/BF01319230
Links to Exploration step
ISTEX:8B146BE02DC1F5C0058E805DA6C6ED6AF77ED527Le document en format XML
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C." last="Jackson">D. C. Jackson</name><affiliation><mods:affiliation>Department of Microbiology, University of Melbourne, Parkville</mods:affiliation></affiliation></author><author><name sortKey="Crabb, B S" sort="Crabb, B S" uniqKey="Crabb B" first="B. S." last="Crabb">B. S. Crabb</name><affiliation><mods:affiliation>Department of Microbiology, University of Melbourne, Parkville</mods:affiliation></affiliation></author><author><name sortKey="Poumbourios, P" sort="Poumbourios, P" uniqKey="Poumbourios P" first="P." last="Poumbourios">P. Poumbourios</name><affiliation><mods:affiliation>Department of Microbiology, University of Melbourne, Parkville</mods:affiliation></affiliation></author><author><name sortKey="Tulip, W R" sort="Tulip, W R" uniqKey="Tulip W" first="W. R." last="Tulip">W. R. 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Although there is compelling evidence for the presence of multiple adjacent and overlapping epitopes covering the surface of these two viral antigens, steric hindrance ensures that even under saturating conditions only three molecules of monovalent antibody fragments can be simultaneously accommodated on each monomer.</abstract><qualityIndicators><score>7.58</score><pdfWordCount>4476</pdfWordCount><pdfCharCount>25651</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>12</pdfPageCount><pdfPageSize>562 x 774 pts</pdfPageSize><refBibsNative>false</refBibsNative><abstractWordCount>92</abstractWordCount><abstractCharCount>664</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Three antibody molecules can bind simultaneously to each monomer of the tetramer of influenza virus neuraminidase and the trimer of influenza virus hemagglutinin</title><pmid><json:string>2001177</json:string></pmid><genre><json:string>research-article</json:string></genre><host><title>Archives of Virology</title><language><json:string>unknown</json:string></language><publicationDate>1991</publicationDate><copyrightDate>1991</copyrightDate><issn><json:string>0304-8608</json:string></issn><eissn><json:string>1432-8798</json:string></eissn><journalId><json:string>705</json:string></journalId><volume>116</volume><issue>1-4</issue><pages><first>45</first><last>56</last></pages><genre><json:string>journal</json:string></genre><subject><json:item><value>Medical Microbiology</value></json:item><json:item><value>Virology</value></json:item><json:item><value>Infectious Diseases</value></json:item></subject></host><namedEntities><unitex><date></date><geogName></geogName><orgName></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName></persName><placeName></placeName><ref_url></ref_url><ref_bibl></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/1BB-5LNVCHFK-H</json:string></ark><categories><wos><json:string>1 - 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In each case this represents an average of approximately three molecules of antibody binding to each protomer. Although there is compelling evidence for the presence of multiple adjacent and overlapping epitopes covering the surface of these two viral antigens, steric hindrance ensures that even under saturating conditions only three molecules of monovalent antibody fragments can be simultaneously accommodated on each monomer.</p></abstract><textClass><keywords scheme="Journal Subject"><list><head>Biomedicine</head><item><term>Medical Microbiology</term></item><item><term>Virology</term></item><item><term>Infectious Diseases</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1990-04-26">Created</change><change when="1991-03-01">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/1BB-5LNVCHFK-H/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="corpus springer-journals not found" 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Diseases</JournalSubject></JournalSubjectGroup></JournalInfo><Volume><VolumeInfo VolumeType="Regular" TocLevels="0"><VolumeIDStart>116</VolumeIDStart><VolumeIDEnd>116</VolumeIDEnd><VolumeIssueCount>4</VolumeIssueCount></VolumeInfo><Issue IssueType="Combined"><IssueInfo TocLevels="0"><IssueIDStart>1</IssueIDStart><IssueIDEnd>4</IssueIDEnd><IssueArticleCount>27</IssueArticleCount><IssueHistory><CoverDate><DateString>1991</DateString><Year>1991</Year><Month>3</Month></CoverDate></IssueHistory><IssueCopyright><CopyrightHolderName>Springer-Verlag</CopyrightHolderName><CopyrightYear>1991</CopyrightYear></IssueCopyright></IssueInfo><Article ID="Art5"><ArticleInfo Language="En" ArticleType="OriginalPaper" NumberingStyle="Unnumbered" TocLevels="0" ContainsESM="No"><ArticleID>BF01319230</ArticleID><ArticleDOI>10.1007/BF01319230</ArticleDOI><ArticleSequenceNumber>5</ArticleSequenceNumber><ArticleTitle Language="En">Three antibody molecules can bind simultaneously to each monomer of the tetramer of influenza virus neuraminidase and the trimer of influenza virus hemagglutinin</ArticleTitle><ArticleCategory>Original Papers</ArticleCategory><ArticleFirstPage>45</ArticleFirstPage><ArticleLastPage>56</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2005</Year><Month>3</Month><Day>3</Day></RegistrationDate><Received><Year>1990</Year><Month>4</Month><Day>26</Day></Received><Accepted><Year>1990</Year><Month>8</Month><Day>14</Day></Accepted></ArticleHistory><ArticleCopyright><CopyrightHolderName>Springer-Verlag</CopyrightHolderName><CopyrightYear>1991</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants><ArticleContext><JournalID>705</JournalID><VolumeIDStart>116</VolumeIDStart><VolumeIDEnd>116</VolumeIDEnd><IssueIDStart>1</IssueIDStart><IssueIDEnd>4</IssueIDEnd></ArticleContext></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>D.</GivenName><GivenName>C.</GivenName><FamilyName>Jackson</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>B.</GivenName><GivenName>S.</GivenName><FamilyName>Crabb</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>P.</GivenName><FamilyName>Poumbourios</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>W.</GivenName><GivenName>R.</GivenName><FamilyName>Tulip</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff3"><AuthorName DisplayOrder="Western"><GivenName>W.</GivenName><GivenName>G.</GivenName><FamilyName>Laver</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgDivision>Department of Microbiology</OrgDivision><OrgName>University of Melbourne</OrgName><OrgAddress><City>Parkville</City></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgName>CSIRO Division of Biomolecular Engineering</OrgName><OrgAddress><City>Parkville</City><State>Victoria</State></OrgAddress></Affiliation><Affiliation ID="Aff3"><OrgDivision>John Curtin School of Medical Research</OrgDivision><OrgName>Australian National University</OrgName><OrgAddress><City>Canberra</City><State>ACT</State><Country>Australia</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Summary</Heading><Para>Trimeric hemagglutinin and tetrameric neuraminidase molecules isolated from influenza virus bind an average of 9 and 13 molecules respectively of monovalent antibody fragments prepared from IgG isolated from polyclonal sera. In each case this represents an average of approximately three molecules of antibody binding to each protomer. Although there is compelling evidence for the presence of multiple adjacent and overlapping epitopes covering the surface of these two viral antigens, steric hindrance ensures that even under saturating conditions only three molecules of monovalent antibody fragments can be simultaneously accommodated on each monomer.</Para></Abstract></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Three antibody molecules can bind simultaneously to each monomer of the tetramer of influenza virus neuraminidase and the trimer of influenza virus hemagglutinin</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Three antibody molecules can bind simultaneously to each monomer of the tetramer of influenza virus neuraminidase and the trimer of influenza virus hemagglutinin</title></titleInfo><name type="personal"><namePart type="given">D.</namePart><namePart type="given">C.</namePart><namePart type="family">Jackson</namePart><affiliation>Department of Microbiology, University of Melbourne, Parkville</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">B.</namePart><namePart type="given">S.</namePart><namePart type="family">Crabb</namePart><affiliation>Department of Microbiology, University of Melbourne, Parkville</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">P.</namePart><namePart type="family">Poumbourios</namePart><affiliation>Department of Microbiology, University of Melbourne, Parkville</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">W.</namePart><namePart type="given">R.</namePart><namePart type="family">Tulip</namePart><affiliation>CSIRO Division of Biomolecular Engineering, Parkville, Victoria</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">W.</namePart><namePart type="given">G.</namePart><namePart type="family">Laver</namePart><affiliation>John Curtin School of Medical Research, Australian National University, Canberra, ACT, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>Springer-Verlag</publisher><place><placeTerm type="text">Vienna</placeTerm></place><dateCreated encoding="w3cdtf">1990-04-26</dateCreated><dateIssued encoding="w3cdtf">1991-03-01</dateIssued><copyrightDate encoding="w3cdtf">1991</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Summary: Trimeric hemagglutinin and tetrameric neuraminidase molecules isolated from influenza virus bind an average of 9 and 13 molecules respectively of monovalent antibody fragments prepared from IgG isolated from polyclonal sera. In each case this represents an average of approximately three molecules of antibody binding to each protomer. Although there is compelling evidence for the presence of multiple adjacent and overlapping epitopes covering the surface of these two viral antigens, steric hindrance ensures that even under saturating conditions only three molecules of monovalent antibody fragments can be simultaneously accommodated on each monomer.</abstract><note>Original Papers</note><relatedItem type="host"><titleInfo><title>Archives of Virology</title></titleInfo><titleInfo type="abbreviated"><title>Archives of Virology</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>Springer</publisher><dateIssued encoding="w3cdtf">1991-03-01</dateIssued><copyrightDate encoding="w3cdtf">1991</copyrightDate></originInfo><subject><genre>Biomedicine</genre><topic>Medical Microbiology</topic><topic>Virology</topic><topic>Infectious Diseases</topic></subject><identifier type="ISSN">0304-8608</identifier><identifier type="eISSN">1432-8798</identifier><identifier type="JournalID">705</identifier><identifier type="IssueArticleCount">27</identifier><identifier type="VolumeIssueCount">4</identifier><part><date>1991</date><detail type="volume"><number>116</number><caption>vol.</caption></detail><detail type="issue"><number>1-4</number><caption>no.</caption></detail><extent unit="pages"><start>45</start><end>56</end></extent></part><recordInfo><recordOrigin>Springer-Verlag, 1991</recordOrigin></recordInfo></relatedItem><identifier type="istex">8B146BE02DC1F5C0058E805DA6C6ED6AF77ED527</identifier><identifier type="ark">ark:/67375/1BB-5LNVCHFK-H</identifier><identifier type="DOI">10.1007/BF01319230</identifier><identifier type="ArticleID">BF01319230</identifier><identifier type="ArticleID">Art5</identifier><accessCondition type="use and reproduction" contentType="copyright">Springer-Verlag, 1991</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Springer-Verlag, 1991</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/1BB-5LNVCHFK-H/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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