Structure of a Human Rhinovirus Complexed with its Receptor Molecule
Cryoelectron microscopy has been used to determine the structure of a virus when complexed with its glycoprotein cellular receptor. Human rhinovirus 16 complexed with the two amino-terminal, immunoglobulin-like domains of the intercellular adhesion molecule 1 shows that the intercellular adhesion mo...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1993-01, Vol.90 (2), p.507-511 |
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container_title | Proceedings of the National Academy of Sciences - PNAS |
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creator | Olson, Norman H. Kolatkar, Prasanna R. Oliveira, Marcos A. Cheng, R. Holland Greve, Jeffrey M. McClelland, Alan Baker, Timothy S. Rossman, Michael G. |
description | Cryoelectron microscopy has been used to determine the structure of a virus when complexed with its glycoprotein cellular receptor. Human rhinovirus 16 complexed with the two amino-terminal, immunoglobulin-like domains of the intercellular adhesion molecule 1 shows that the intercellular adhesion molecule 1 binds into the 12-Å deep "canyon" on the viral surface. This result confirms the prediction that the viral-receptor attachment site lies in a cavity inaccessible to the host's antibodies. The atomic structures of human rhinovirus 14 and CD4, homologous to human rhinovirus 16 and intercellular adhesion molecule 1, showed excellent correspondence with observed density, thus establishing the virus-receptor interactions. |
doi_str_mv | 10.1073/pnas.90.2.507 |
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Holland ; Greve, Jeffrey M. ; McClelland, Alan ; Baker, Timothy S. ; Rossman, Michael G.</creator><creatorcontrib>Olson, Norman H. ; Kolatkar, Prasanna R. ; Oliveira, Marcos A. ; Cheng, R. Holland ; Greve, Jeffrey M. ; McClelland, Alan ; Baker, Timothy S. ; Rossman, Michael G.</creatorcontrib><description>Cryoelectron microscopy has been used to determine the structure of a virus when complexed with its glycoprotein cellular receptor. Human rhinovirus 16 complexed with the two amino-terminal, immunoglobulin-like domains of the intercellular adhesion molecule 1 shows that the intercellular adhesion molecule 1 binds into the 12-Å deep "canyon" on the viral surface. This result confirms the prediction that the viral-receptor attachment site lies in a cavity inaccessible to the host's antibodies. The atomic structures of human rhinovirus 14 and CD4, homologous to human rhinovirus 16 and intercellular adhesion molecule 1, showed excellent correspondence with observed density, thus establishing the virus-receptor interactions.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.90.2.507</identifier><identifier>PMID: 8093643</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Antigens, CD - metabolism ; Antigens, CD - ultrastructure ; Atomic structure ; Biochemistry ; Biological and medical sciences ; Canyons ; CD4 Antigens - metabolism ; CD4 Antigens - ultrastructure ; Cell adhesion molecules ; Cell Adhesion Molecules - metabolism ; Cell Adhesion Molecules - ultrastructure ; complex ; Cryopreservation ; crystal structure ; Fundamental and applied biological sciences. Psychology ; Humans ; Image Processing, Computer-Assisted ; Intercellular Adhesion Molecule-1 ; Microbiology ; Microscopy ; Microscopy, Electron ; Models, Molecular ; Molecules ; Morphology, structure, chemical composition, physicochemical properties ; Poliovirus ; Receptors ; Receptors, Virus - metabolism ; Receptors, Virus - ultrastructure ; Rhinovirus ; rhinovirus (humans) 16 ; Rhinovirus - metabolism ; Rhinovirus - ultrastructure ; Viral morphology ; Virology ; Viruses</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1993-01, Vol.90 (2), p.507-511</ispartof><rights>Copyright 1993 The National Academy of Sciences of the United States of America</rights><rights>1993 INIST-CNRS</rights><rights>Copyright National Academy of Sciences Jan 15, 1993</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c539t-1ffc2dccb8b0319a27a168174863d56463b630ca0f8ba2fde9e7da0946f7fcbd3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/90/2.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2361084$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2361084$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53769,53771,57995,58228</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4656839$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8093643$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Olson, Norman H.</creatorcontrib><creatorcontrib>Kolatkar, Prasanna R.</creatorcontrib><creatorcontrib>Oliveira, Marcos A.</creatorcontrib><creatorcontrib>Cheng, R. Holland</creatorcontrib><creatorcontrib>Greve, Jeffrey M.</creatorcontrib><creatorcontrib>McClelland, Alan</creatorcontrib><creatorcontrib>Baker, Timothy S.</creatorcontrib><creatorcontrib>Rossman, Michael G.</creatorcontrib><title>Structure of a Human Rhinovirus Complexed with its Receptor Molecule</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Cryoelectron microscopy has been used to determine the structure of a virus when complexed with its glycoprotein cellular receptor. Human rhinovirus 16 complexed with the two amino-terminal, immunoglobulin-like domains of the intercellular adhesion molecule 1 shows that the intercellular adhesion molecule 1 binds into the 12-Å deep "canyon" on the viral surface. This result confirms the prediction that the viral-receptor attachment site lies in a cavity inaccessible to the host's antibodies. The atomic structures of human rhinovirus 14 and CD4, homologous to human rhinovirus 16 and intercellular adhesion molecule 1, showed excellent correspondence with observed density, thus establishing the virus-receptor interactions.</description><subject>Antigens, CD - metabolism</subject><subject>Antigens, CD - ultrastructure</subject><subject>Atomic structure</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Canyons</subject><subject>CD4 Antigens - metabolism</subject><subject>CD4 Antigens - ultrastructure</subject><subject>Cell adhesion molecules</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Cell Adhesion Molecules - ultrastructure</subject><subject>complex</subject><subject>Cryopreservation</subject><subject>crystal structure</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Image Processing, Computer-Assisted</subject><subject>Intercellular Adhesion Molecule-1</subject><subject>Microbiology</subject><subject>Microscopy</subject><subject>Microscopy, Electron</subject><subject>Models, Molecular</subject><subject>Molecules</subject><subject>Morphology, structure, chemical composition, physicochemical properties</subject><subject>Poliovirus</subject><subject>Receptors</subject><subject>Receptors, Virus - metabolism</subject><subject>Receptors, Virus - ultrastructure</subject><subject>Rhinovirus</subject><subject>rhinovirus (humans) 16</subject><subject>Rhinovirus - metabolism</subject><subject>Rhinovirus - ultrastructure</subject><subject>Viral morphology</subject><subject>Virology</subject><subject>Viruses</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAURi0EKkNhyQ6kCAG7DNfPxBIbNDyKVIRUYG05js1k5ImDH6X8ezJqGAoLWHlxzv3s6w-hhxjWGBr6Yhp1WktYkzWH5hZaYZC4FkzCbbQCIE3dMsLuonsp7QBA8hZO0EkLkgpGV-j1pxyLySXaKrhKV2dlr8fqYjuM4XKIJVWbsJ-8vbJ99X3I22rIqbqwxk45xOpD8NYUb--jO077ZB8s5yn68vbN581Zff7x3fvNq_PacCpzjZ0zpDemazugWGrSaCxa3LBW0J4LJmgnKBgNru00cb2Vtuk1SCZc40zX01P08jp3Kt3e9saOOWqvpjjsdfyhgh7Un2QctupruFSMC0nm8efLeAzfik1Z7YdkrPd6tKEk1XDOKRHtf0UsGDAq-Cw--UvchRLH-Q8UAUwEI_Qg1deSiSGlaN3xwRjUoUJ1qFBJUETNFc7-45tbHu2ls5k_XbhORnsX9WiGdNSY4PMKctYeLdoh_Re9ccuzf2DlivfZXuXfMbs0V34UCRUYWkZ_Aj7mxW0</recordid><startdate>19930115</startdate><enddate>19930115</enddate><creator>Olson, Norman H.</creator><creator>Kolatkar, Prasanna R.</creator><creator>Oliveira, Marcos A.</creator><creator>Cheng, R. Holland</creator><creator>Greve, Jeffrey M.</creator><creator>McClelland, Alan</creator><creator>Baker, Timothy S.</creator><creator>Rossman, Michael G.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>M7Z</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19930115</creationdate><title>Structure of a Human Rhinovirus Complexed with its Receptor Molecule</title><author>Olson, Norman H. ; Kolatkar, Prasanna R. ; Oliveira, Marcos A. ; Cheng, R. 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Psychology</topic><topic>Humans</topic><topic>Image Processing, Computer-Assisted</topic><topic>Intercellular Adhesion Molecule-1</topic><topic>Microbiology</topic><topic>Microscopy</topic><topic>Microscopy, Electron</topic><topic>Models, Molecular</topic><topic>Molecules</topic><topic>Morphology, structure, chemical composition, physicochemical properties</topic><topic>Poliovirus</topic><topic>Receptors</topic><topic>Receptors, Virus - metabolism</topic><topic>Receptors, Virus - ultrastructure</topic><topic>Rhinovirus</topic><topic>rhinovirus (humans) 16</topic><topic>Rhinovirus - metabolism</topic><topic>Rhinovirus - ultrastructure</topic><topic>Viral morphology</topic><topic>Virology</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Olson, Norman H.</creatorcontrib><creatorcontrib>Kolatkar, Prasanna R.</creatorcontrib><creatorcontrib>Oliveira, Marcos A.</creatorcontrib><creatorcontrib>Cheng, R. 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Holland</au><au>Greve, Jeffrey M.</au><au>McClelland, Alan</au><au>Baker, Timothy S.</au><au>Rossman, Michael G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure of a Human Rhinovirus Complexed with its Receptor Molecule</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1993-01-15</date><risdate>1993</risdate><volume>90</volume><issue>2</issue><spage>507</spage><epage>511</epage><pages>507-511</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>Cryoelectron microscopy has been used to determine the structure of a virus when complexed with its glycoprotein cellular receptor. Human rhinovirus 16 complexed with the two amino-terminal, immunoglobulin-like domains of the intercellular adhesion molecule 1 shows that the intercellular adhesion molecule 1 binds into the 12-Å deep "canyon" on the viral surface. This result confirms the prediction that the viral-receptor attachment site lies in a cavity inaccessible to the host's antibodies. The atomic structures of human rhinovirus 14 and CD4, homologous to human rhinovirus 16 and intercellular adhesion molecule 1, showed excellent correspondence with observed density, thus establishing the virus-receptor interactions.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>8093643</pmid><doi>10.1073/pnas.90.2.507</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
subjects | Antigens, CD - metabolism Antigens, CD - ultrastructure Atomic structure Biochemistry Biological and medical sciences Canyons CD4 Antigens - metabolism CD4 Antigens - ultrastructure Cell adhesion molecules Cell Adhesion Molecules - metabolism Cell Adhesion Molecules - ultrastructure complex Cryopreservation crystal structure Fundamental and applied biological sciences. Psychology Humans Image Processing, Computer-Assisted Intercellular Adhesion Molecule-1 Microbiology Microscopy Microscopy, Electron Models, Molecular Molecules Morphology, structure, chemical composition, physicochemical properties Poliovirus Receptors Receptors, Virus - metabolism Receptors, Virus - ultrastructure Rhinovirus rhinovirus (humans) 16 Rhinovirus - metabolism Rhinovirus - ultrastructure Viral morphology Virology Viruses |
title | Structure of a Human Rhinovirus Complexed with its Receptor Molecule |
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