Three-Dimensional Structures of Influenza Virus Neuraminidase-Antibody Complexes
X-ray diffraction analysis of crystals of a monoclonal Fab fragment NC41 bound to a viral antigen, influenza virus neuraminidase, shows an epitope involving five surface loops of the antigen. In addition it reveals an unusual pairing pattern between the domains of light and heavy chains in the varia...
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| Veröffentlicht in: | Philosophical transactions of the Royal Society of London. Series B, Biological sciences Biological sciences, 1989-06, Vol.323 (1217), p.511-518 |
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| container_title | Philosophical transactions of the Royal Society of London. Series B, Biological sciences |
| container_volume | 323 |
| creator | Colman, P. M. Tulip, W. R. Varghese, J. N. Tulloch, P. A. Baker, A. T. Laver, W. G. Air, G. M. Webster, R. G. |
| description | X-ray diffraction analysis of crystals of a monoclonal Fab fragment NC41 bound to a viral antigen, influenza virus neuraminidase,
shows an epitope involving five surface loops of the antigen. In addition it reveals an unusual pairing pattern between the
domains of light and heavy chains in the variable module of the antibody. We interpret this result to imply that association
with antigen can induce changes in the quaternary structure of the Fab, through a sliding of domains at the variable light/
variable heavy chains (V$_L$-V$_H$) interface. In addition, Fab binding has altered the conformation
of some of the surface loops of the antigen. The structure of the NC10 Fab-neuraminidase complex has now also been solved.
It binds an epitope that overlaps the NC41 epitope. In this structure, there is no electron density for the C-module of the
Fab fragment, implying it is disordered in the crystal lattice. The implications of these, and other antibody-antigen structures,
for immune recognition are discussed. |
| doi_str_mv | 10.1098/rstb.1989.0028 |
| format | Article |
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shows an epitope involving five surface loops of the antigen. In addition it reveals an unusual pairing pattern between the
domains of light and heavy chains in the variable module of the antibody. We interpret this result to imply that association
with antigen can induce changes in the quaternary structure of the Fab, through a sliding of domains at the variable light/
variable heavy chains (V$_L$-V$_H$) interface. In addition, Fab binding has altered the conformation
of some of the surface loops of the antigen. The structure of the NC10 Fab-neuraminidase complex has now also been solved.
It binds an epitope that overlaps the NC41 epitope. In this structure, there is no electron density for the C-module of the
Fab fragment, implying it is disordered in the crystal lattice. The implications of these, and other antibody-antigen structures,
for immune recognition are discussed.</description><identifier>ISSN: 0962-8436</identifier><identifier>ISSN: 0080-4622</identifier><identifier>EISSN: 1471-2970</identifier><identifier>EISSN: 2054-0280</identifier><identifier>DOI: 10.1098/rstb.1989.0028</identifier><identifier>PMID: 2569208</identifier><identifier>CODEN: PTRBAE</identifier><language>eng</language><publisher>London: The Royal Society</publisher><subject>Amino acids ; Antibodies ; Antigen-Antibody Complex ; Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation ; Antigens ; Biological and medical sciences ; Crystals ; Electron density ; Epitopes ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Immunoglobulin Fab Fragments ; Immunoglobulins ; Macromolecular Substances ; Models, Molecular ; Molecular immunology ; Neuraminidase - immunology ; Orthomyxoviridae ; Orthomyxoviridae - enzymology ; Protein Conformation ; Viral morphology ; Viruses ; X-Ray Diffraction</subject><ispartof>Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 1989-06, Vol.323 (1217), p.511-518</ispartof><rights>Copyright 1989 The Royal Society</rights><rights>Scanned images copyright © 2017, Royal Society</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c571t-46b9c59913e212dbf196be9bd07cede396d1c8d4cf402720ae428b4bf04c28fe3</citedby><cites>FETCH-LOGICAL-c571t-46b9c59913e212dbf196be9bd07cede396d1c8d4cf402720ae428b4bf04c28fe3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2396874$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2396874$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,27903,27904,57995,58228</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19292259$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2569208$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Colman, P. M.</creatorcontrib><creatorcontrib>Tulip, W. R.</creatorcontrib><creatorcontrib>Varghese, J. N.</creatorcontrib><creatorcontrib>Tulloch, P. A.</creatorcontrib><creatorcontrib>Baker, A. T.</creatorcontrib><creatorcontrib>Laver, W. G.</creatorcontrib><creatorcontrib>Air, G. M.</creatorcontrib><creatorcontrib>Webster, R. G.</creatorcontrib><title>Three-Dimensional Structures of Influenza Virus Neuraminidase-Antibody Complexes</title><title>Philosophical transactions of the Royal Society of London. Series B, Biological sciences</title><addtitle>Phil. Trans. R. Soc. Lond. B</addtitle><addtitle>Philos Trans R Soc Lond B Biol Sci</addtitle><description>X-ray diffraction analysis of crystals of a monoclonal Fab fragment NC41 bound to a viral antigen, influenza virus neuraminidase,
shows an epitope involving five surface loops of the antigen. In addition it reveals an unusual pairing pattern between the
domains of light and heavy chains in the variable module of the antibody. We interpret this result to imply that association
with antigen can induce changes in the quaternary structure of the Fab, through a sliding of domains at the variable light/
variable heavy chains (V$_L$-V$_H$) interface. In addition, Fab binding has altered the conformation
of some of the surface loops of the antigen. The structure of the NC10 Fab-neuraminidase complex has now also been solved.
It binds an epitope that overlaps the NC41 epitope. In this structure, there is no electron density for the C-module of the
Fab fragment, implying it is disordered in the crystal lattice. The implications of these, and other antibody-antigen structures,
for immune recognition are discussed.</description><subject>Amino acids</subject><subject>Antibodies</subject><subject>Antigen-Antibody Complex</subject><subject>Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation</subject><subject>Antigens</subject><subject>Biological and medical sciences</subject><subject>Crystals</subject><subject>Electron density</subject><subject>Epitopes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Immunoglobulin Fab Fragments</subject><subject>Immunoglobulins</subject><subject>Macromolecular Substances</subject><subject>Models, Molecular</subject><subject>Molecular immunology</subject><subject>Neuraminidase - immunology</subject><subject>Orthomyxoviridae</subject><subject>Orthomyxoviridae - enzymology</subject><subject>Protein Conformation</subject><subject>Viral morphology</subject><subject>Viruses</subject><subject>X-Ray Diffraction</subject><issn>0962-8436</issn><issn>0080-4622</issn><issn>1471-2970</issn><issn>2054-0280</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc1v1DAQxSMEKqVw5QRSLnDLYjtxEp9QWb4qVYDowtVynDHrVRKnnhjY_vU4uyuqFaIny5rfe37znCRPKVlQIupXHqdmQUUtFoSw-l5ySouKZkxU5H5ySkTJsrrIy4fJI8QNIUTwqjhJThgvBSP1afJltfYA2Vvbw4DWDapLryYf9BQ8YOpMejGYLsBwo9Lv1gdMP0HwqreDbRVCdj5MtnHtNl26fuzgN-Dj5IFRHcKTw3mWfHv_brX8mF1-_nCxPL_MNK_olBVlIzQXgubAKGsbQ0XZgGhaUmloIRdlS3XdFtoUhFWMKChY3RSNIYVmtYH8LHm59x29uw6Ak-wtaug6NYALKCtBKS85j-BiD2rvED0YOXrbK7-VlMi5QjlXKOcK5VxhFDw_OIemh_Yvfugszl8c5gq16oxXg7Z46yqYYIyLyOGe824bm3DawrSVGxd8bBnl16vVm7i0-Jmz3FJGKxm9KeGccCpv7LiLNQMyAtIiBpA77Djuv-nzu179787P9qoNTs7frhz_oa6KOCb78dr-WP-yHuSRe7yM0W7OuUvIKY2S13dK5ve1GyYYpiOhNKHr5Nia_A8Tj-L6</recordid><startdate>19890612</startdate><enddate>19890612</enddate><creator>Colman, P. M.</creator><creator>Tulip, W. R.</creator><creator>Varghese, J. N.</creator><creator>Tulloch, P. A.</creator><creator>Baker, A. T.</creator><creator>Laver, W. G.</creator><creator>Air, G. M.</creator><creator>Webster, R. G.</creator><general>The Royal Society</general><general>Royal Society of London</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19890612</creationdate><title>Three-Dimensional Structures of Influenza Virus Neuraminidase-Antibody Complexes</title><author>Colman, P. M. ; Tulip, W. R. ; Varghese, J. N. ; Tulloch, P. A. ; Baker, A. T. ; Laver, W. G. ; Air, G. M. ; Webster, R. G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c571t-46b9c59913e212dbf196be9bd07cede396d1c8d4cf402720ae428b4bf04c28fe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Amino acids</topic><topic>Antibodies</topic><topic>Antigen-Antibody Complex</topic><topic>Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation</topic><topic>Antigens</topic><topic>Biological and medical sciences</topic><topic>Crystals</topic><topic>Electron density</topic><topic>Epitopes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Immunoglobulin Fab Fragments</topic><topic>Immunoglobulins</topic><topic>Macromolecular Substances</topic><topic>Models, Molecular</topic><topic>Molecular immunology</topic><topic>Neuraminidase - immunology</topic><topic>Orthomyxoviridae</topic><topic>Orthomyxoviridae - enzymology</topic><topic>Protein Conformation</topic><topic>Viral morphology</topic><topic>Viruses</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Colman, P. M.</creatorcontrib><creatorcontrib>Tulip, W. R.</creatorcontrib><creatorcontrib>Varghese, J. N.</creatorcontrib><creatorcontrib>Tulloch, P. A.</creatorcontrib><creatorcontrib>Baker, A. T.</creatorcontrib><creatorcontrib>Laver, W. G.</creatorcontrib><creatorcontrib>Air, G. M.</creatorcontrib><creatorcontrib>Webster, R. G.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Philosophical transactions of the Royal Society of London. Series B, Biological sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Colman, P. M.</au><au>Tulip, W. R.</au><au>Varghese, J. N.</au><au>Tulloch, P. A.</au><au>Baker, A. T.</au><au>Laver, W. G.</au><au>Air, G. M.</au><au>Webster, R. G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Three-Dimensional Structures of Influenza Virus Neuraminidase-Antibody Complexes</atitle><jtitle>Philosophical transactions of the Royal Society of London. Series B, Biological sciences</jtitle><stitle>Phil. Trans. R. Soc. Lond. B</stitle><addtitle>Philos Trans R Soc Lond B Biol Sci</addtitle><date>1989-06-12</date><risdate>1989</risdate><volume>323</volume><issue>1217</issue><spage>511</spage><epage>518</epage><pages>511-518</pages><issn>0962-8436</issn><issn>0080-4622</issn><eissn>1471-2970</eissn><eissn>2054-0280</eissn><coden>PTRBAE</coden><abstract>X-ray diffraction analysis of crystals of a monoclonal Fab fragment NC41 bound to a viral antigen, influenza virus neuraminidase,
shows an epitope involving five surface loops of the antigen. In addition it reveals an unusual pairing pattern between the
domains of light and heavy chains in the variable module of the antibody. We interpret this result to imply that association
with antigen can induce changes in the quaternary structure of the Fab, through a sliding of domains at the variable light/
variable heavy chains (V$_L$-V$_H$) interface. In addition, Fab binding has altered the conformation
of some of the surface loops of the antigen. The structure of the NC10 Fab-neuraminidase complex has now also been solved.
It binds an epitope that overlaps the NC41 epitope. In this structure, there is no electron density for the C-module of the
Fab fragment, implying it is disordered in the crystal lattice. The implications of these, and other antibody-antigen structures,
for immune recognition are discussed.</abstract><cop>London</cop><pub>The Royal Society</pub><pmid>2569208</pmid><doi>10.1098/rstb.1989.0028</doi><tpages>8</tpages></addata></record> |
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| identifier | ISSN: 0962-8436 |
| ispartof | Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 1989-06, Vol.323 (1217), p.511-518 |
| issn | 0962-8436 0080-4622 1471-2970 2054-0280 |
| language | eng |
| recordid | cdi_pascalfrancis_primary_19292259 |
| source | Jstor Complete Legacy; MEDLINE |
| subjects | Amino acids Antibodies Antigen-Antibody Complex Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation Antigens Biological and medical sciences Crystals Electron density Epitopes Fundamental and applied biological sciences. Psychology Fundamental immunology Immunoglobulin Fab Fragments Immunoglobulins Macromolecular Substances Models, Molecular Molecular immunology Neuraminidase - immunology Orthomyxoviridae Orthomyxoviridae - enzymology Protein Conformation Viral morphology Viruses X-Ray Diffraction |
| title | Three-Dimensional Structures of Influenza Virus Neuraminidase-Antibody Complexes |
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