Visualization of a missing link in retrovirus capsid assembly
For a retrovirus such as HIV to be infectious, a properly formed capsid is needed; however, unusually among viruses, retrovirus capsids are highly variable in structure. According to the fullerene conjecture, they are composed of hexamers and pentamers of capsid protein (CA), with the shape of a cap...
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description | For a retrovirus such as HIV to be infectious, a properly formed capsid is needed; however, unusually among viruses, retrovirus capsids are highly variable in structure. According to the fullerene conjecture, they are composed of hexamers and pentamers of capsid protein (CA), with the shape of a capsid varying according to how the twelve pentamers are distributed and its size depending on the number of hexamers. Hexamers have been studied in planar and tubular arrays, but the predicted pentamers have not been observed. Here we report cryo-electron microscopic analyses of two
in-vitro
-assembled capsids of Rous sarcoma virus. Both are icosahedrally symmetric: one is composed of 12 pentamers, and the other of 12 pentamers and 20 hexamers. Fitting of atomic models of the two CA domains into the reconstructions shows three distinct inter-subunit interactions. These observations substantiate the fullerene conjecture, show how pentamers are accommodated at vertices, support the inference that nucleation is a crucial morphologic determinant, and imply that electrostatic interactions govern the differential assembly of pentamers and hexamers.
Retrovirus fullerene-like architecture confirmed
Retrovirus capsids are polymorphic, consisting of variable hexamer and pentamer aggregates with structures thought to resemble fullerenes. A cryo-electon microscopy/molecular modelling study of capsids assembled from the full-length Rous sarcoma virus capsid protein now confirms the existence of fullerene-like capsid architecture. Two different forms were observed, one composed of 12 pentamers and the other of 12 pentamers and 20 hexamers.
Retrovirus capsids are polymorphic, consisting of variable hexamer and pentamer aggregates that are thought to reflect fullerenes. This paper reports the cryo-electron microscopy analysis of RSV capsid protein visualizing pentamers, and confirms that retrovirus capsid has a fullerene-based architecture. |
doi_str_mv | 10.1038/nature07724 |
format | Article |
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in-vitro
-assembled capsids of Rous sarcoma virus. Both are icosahedrally symmetric: one is composed of 12 pentamers, and the other of 12 pentamers and 20 hexamers. Fitting of atomic models of the two CA domains into the reconstructions shows three distinct inter-subunit interactions. These observations substantiate the fullerene conjecture, show how pentamers are accommodated at vertices, support the inference that nucleation is a crucial morphologic determinant, and imply that electrostatic interactions govern the differential assembly of pentamers and hexamers.
Retrovirus fullerene-like architecture confirmed
Retrovirus capsids are polymorphic, consisting of variable hexamer and pentamer aggregates with structures thought to resemble fullerenes. A cryo-electon microscopy/molecular modelling study of capsids assembled from the full-length Rous sarcoma virus capsid protein now confirms the existence of fullerene-like capsid architecture. Two different forms were observed, one composed of 12 pentamers and the other of 12 pentamers and 20 hexamers.
Retrovirus capsids are polymorphic, consisting of variable hexamer and pentamer aggregates that are thought to reflect fullerenes. This paper reports the cryo-electron microscopy analysis of RSV capsid protein visualizing pentamers, and confirms that retrovirus capsid has a fullerene-based architecture.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>EISSN: 1476-4679</identifier><identifier>DOI: 10.1038/nature07724</identifier><identifier>PMID: 19194444</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Atoms & subatomic particles ; Biological and medical sciences ; Blood lipoproteins ; Capsid - chemistry ; Capsid - metabolism ; Capsid - ultrastructure ; Capsid Proteins - chemistry ; Capsid Proteins - genetics ; Capsid Proteins - metabolism ; Capsid Proteins - ultrastructure ; Cryoelectron Microscopy ; Electron microscopes ; Fundamental and applied biological sciences. Psychology ; Genetic aspects ; Health aspects ; HIV ; HIV - chemistry ; HIV - genetics ; HIV - ultrastructure ; Human immunodeficiency virus ; Humanities and Social Sciences ; Lipoproteins ; Microbiology ; Models, Molecular ; Morphology, structure, chemical composition, physicochemical properties ; multidisciplinary ; Mutant Proteins - chemistry ; Mutant Proteins - genetics ; Mutant Proteins - metabolism ; Mutant Proteins - ultrastructure ; Mutation ; Polymorphism, Genetic ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Subunits - chemistry ; Protein Subunits - metabolism ; Proteins ; Proteolipids ; Retroviruses ; Rous sarcoma virus ; Rous sarcoma virus - chemistry ; Rous sarcoma virus - genetics ; Rous sarcoma virus - ultrastructure ; Sarcoma ; Science ; Science (multidisciplinary) ; Static Electricity ; Structure ; Virology ; Virus Assembly ; Visualization</subject><ispartof>Nature, 2009-02, Vol.457 (7230), p.694-698</ispartof><rights>Macmillan Publishers Limited. All rights reserved 2009</rights><rights>2009 INIST-CNRS</rights><rights>COPYRIGHT 2009 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Feb 5, 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c678t-29a1997c33d27c8a457e4136296b36732568bc17257c033bead900d7e34b84a43</citedby><cites>FETCH-LOGICAL-c678t-29a1997c33d27c8a457e4136296b36732568bc17257c033bead900d7e34b84a43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nature07724$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nature07724$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21059526$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19194444$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cardone, Giovanni</creatorcontrib><creatorcontrib>Purdy, John G.</creatorcontrib><creatorcontrib>Cheng, Naiqian</creatorcontrib><creatorcontrib>Craven, Rebecca C.</creatorcontrib><creatorcontrib>Steven, Alasdair C.</creatorcontrib><title>Visualization of a missing link in retrovirus capsid assembly</title><title>Nature</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>For a retrovirus such as HIV to be infectious, a properly formed capsid is needed; however, unusually among viruses, retrovirus capsids are highly variable in structure. According to the fullerene conjecture, they are composed of hexamers and pentamers of capsid protein (CA), with the shape of a capsid varying according to how the twelve pentamers are distributed and its size depending on the number of hexamers. Hexamers have been studied in planar and tubular arrays, but the predicted pentamers have not been observed. Here we report cryo-electron microscopic analyses of two
in-vitro
-assembled capsids of Rous sarcoma virus. Both are icosahedrally symmetric: one is composed of 12 pentamers, and the other of 12 pentamers and 20 hexamers. Fitting of atomic models of the two CA domains into the reconstructions shows three distinct inter-subunit interactions. These observations substantiate the fullerene conjecture, show how pentamers are accommodated at vertices, support the inference that nucleation is a crucial morphologic determinant, and imply that electrostatic interactions govern the differential assembly of pentamers and hexamers.
Retrovirus fullerene-like architecture confirmed
Retrovirus capsids are polymorphic, consisting of variable hexamer and pentamer aggregates with structures thought to resemble fullerenes. A cryo-electon microscopy/molecular modelling study of capsids assembled from the full-length Rous sarcoma virus capsid protein now confirms the existence of fullerene-like capsid architecture. Two different forms were observed, one composed of 12 pentamers and the other of 12 pentamers and 20 hexamers.
Retrovirus capsids are polymorphic, consisting of variable hexamer and pentamer aggregates that are thought to reflect fullerenes. This paper reports the cryo-electron microscopy analysis of RSV capsid protein visualizing pentamers, and confirms that retrovirus capsid has a fullerene-based architecture.</description><subject>Atoms & subatomic particles</subject><subject>Biological and medical sciences</subject><subject>Blood lipoproteins</subject><subject>Capsid - chemistry</subject><subject>Capsid - metabolism</subject><subject>Capsid - ultrastructure</subject><subject>Capsid Proteins - chemistry</subject><subject>Capsid Proteins - genetics</subject><subject>Capsid Proteins - metabolism</subject><subject>Capsid Proteins - ultrastructure</subject><subject>Cryoelectron Microscopy</subject><subject>Electron microscopes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic aspects</subject><subject>Health aspects</subject><subject>HIV</subject><subject>HIV - chemistry</subject><subject>HIV - genetics</subject><subject>HIV - ultrastructure</subject><subject>Human immunodeficiency virus</subject><subject>Humanities and Social Sciences</subject><subject>Lipoproteins</subject><subject>Microbiology</subject><subject>Models, Molecular</subject><subject>Morphology, structure, chemical composition, physicochemical properties</subject><subject>multidisciplinary</subject><subject>Mutant Proteins - chemistry</subject><subject>Mutant Proteins - genetics</subject><subject>Mutant Proteins - metabolism</subject><subject>Mutant Proteins - ultrastructure</subject><subject>Mutation</subject><subject>Polymorphism, Genetic</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Subunits - chemistry</subject><subject>Protein Subunits - metabolism</subject><subject>Proteins</subject><subject>Proteolipids</subject><subject>Retroviruses</subject><subject>Rous sarcoma virus</subject><subject>Rous sarcoma virus - chemistry</subject><subject>Rous sarcoma virus - genetics</subject><subject>Rous sarcoma virus - ultrastructure</subject><subject>Sarcoma</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Static Electricity</subject><subject>Structure</subject><subject>Virology</subject><subject>Virus Assembly</subject><subject>Visualization</subject><issn>0028-0836</issn><issn>1476-4687</issn><issn>1476-4679</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqF0tuL1DAUB-AgijuuPvkuRVhBtGtuzeVBYRi8LCwKuupjSNO0Zm2T2aRdXP96M8ywMyMjtg-F5usvpycHgMcIniJIxCuvxylayDmmd8AMUc5KygS_C2YQYlFCQdgReJDSJYSwQpzeB0dIIknzNQOvv7k06d791qMLvghtoYvBpeR8V_TO_yycL6IdY7h2cUqF0cvkmkKnZIe6v3kI7rW6T_bR5nkMvr57e7H4UJ5_en-2mJ-XhnExllhqJCU3hDSYG6FpxS1FhGHJasI4wRUTtUEcV9xAQmqrGwlhwy2htaCakmPwZp27nOrBNsb6MepeLaMbdLxRQTu1v-LdD9WFa4U5RlySHPBsExDD1WTTqPJPGtv32tswJcWYEBxy-l-IIcGrQjN8-he8DFP0uQvZ0IoRTllG5Rp1urfK-Tbk6kxnvc1FBm9bl1_PkSRSiNyNbeieN0t3pXbR6QGU78YOzhxMfb73QTaj_TV2ekpJnX35vG9f_NvOL74vPh7UJoaUom1vjwRBtRpOtTOcWT_ZPcWt3UxjBicboJPRfRu1Ny7dOoxgJSu8auvLtUt5yXc2bnt_aN8_71D4Kg</recordid><startdate>20090205</startdate><enddate>20090205</enddate><creator>Cardone, Giovanni</creator><creator>Purdy, John G.</creator><creator>Cheng, Naiqian</creator><creator>Craven, Rebecca C.</creator><creator>Steven, Alasdair C.</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</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>ATWCN</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>S0X</scope><scope>SOI</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090205</creationdate><title>Visualization of a missing link in retrovirus capsid assembly</title><author>Cardone, Giovanni ; 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nature</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cardone, Giovanni</au><au>Purdy, John G.</au><au>Cheng, Naiqian</au><au>Craven, Rebecca C.</au><au>Steven, Alasdair C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Visualization of a missing link in retrovirus capsid assembly</atitle><jtitle>Nature</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>2009-02-05</date><risdate>2009</risdate><volume>457</volume><issue>7230</issue><spage>694</spage><epage>698</epage><pages>694-698</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><eissn>1476-4679</eissn><coden>NATUAS</coden><abstract>For a retrovirus such as HIV to be infectious, a properly formed capsid is needed; however, unusually among viruses, retrovirus capsids are highly variable in structure. According to the fullerene conjecture, they are composed of hexamers and pentamers of capsid protein (CA), with the shape of a capsid varying according to how the twelve pentamers are distributed and its size depending on the number of hexamers. Hexamers have been studied in planar and tubular arrays, but the predicted pentamers have not been observed. Here we report cryo-electron microscopic analyses of two
in-vitro
-assembled capsids of Rous sarcoma virus. Both are icosahedrally symmetric: one is composed of 12 pentamers, and the other of 12 pentamers and 20 hexamers. Fitting of atomic models of the two CA domains into the reconstructions shows three distinct inter-subunit interactions. These observations substantiate the fullerene conjecture, show how pentamers are accommodated at vertices, support the inference that nucleation is a crucial morphologic determinant, and imply that electrostatic interactions govern the differential assembly of pentamers and hexamers.
Retrovirus fullerene-like architecture confirmed
Retrovirus capsids are polymorphic, consisting of variable hexamer and pentamer aggregates with structures thought to resemble fullerenes. A cryo-electon microscopy/molecular modelling study of capsids assembled from the full-length Rous sarcoma virus capsid protein now confirms the existence of fullerene-like capsid architecture. Two different forms were observed, one composed of 12 pentamers and the other of 12 pentamers and 20 hexamers.
Retrovirus capsids are polymorphic, consisting of variable hexamer and pentamer aggregates that are thought to reflect fullerenes. This paper reports the cryo-electron microscopy analysis of RSV capsid protein visualizing pentamers, and confirms that retrovirus capsid has a fullerene-based architecture.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>19194444</pmid><doi>10.1038/nature07724</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2721793 |
source | MEDLINE; Springer Nature - Complete Springer Journals; Nature Journals Online |
subjects | Atoms & subatomic particles Biological and medical sciences Blood lipoproteins Capsid - chemistry Capsid - metabolism Capsid - ultrastructure Capsid Proteins - chemistry Capsid Proteins - genetics Capsid Proteins - metabolism Capsid Proteins - ultrastructure Cryoelectron Microscopy Electron microscopes Fundamental and applied biological sciences. Psychology Genetic aspects Health aspects HIV HIV - chemistry HIV - genetics HIV - ultrastructure Human immunodeficiency virus Humanities and Social Sciences Lipoproteins Microbiology Models, Molecular Morphology, structure, chemical composition, physicochemical properties multidisciplinary Mutant Proteins - chemistry Mutant Proteins - genetics Mutant Proteins - metabolism Mutant Proteins - ultrastructure Mutation Polymorphism, Genetic Protein Multimerization Protein Structure, Quaternary Protein Subunits - chemistry Protein Subunits - metabolism Proteins Proteolipids Retroviruses Rous sarcoma virus Rous sarcoma virus - chemistry Rous sarcoma virus - genetics Rous sarcoma virus - ultrastructure Sarcoma Science Science (multidisciplinary) Static Electricity Structure Virology Virus Assembly Visualization |
title | Visualization of a missing link in retrovirus capsid assembly |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-13T19%3A33%3A06IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Visualization%20of%20a%20missing%20link%20in%20retrovirus%20capsid%20assembly&rft.jtitle=Nature&rft.au=Cardone,%20Giovanni&rft.date=2009-02-05&rft.volume=457&rft.issue=7230&rft.spage=694&rft.epage=698&rft.pages=694-698&rft.issn=0028-0836&rft.eissn=1476-4687&rft.coden=NATUAS&rft_id=info:doi/10.1038/nature07724&rft_dat=%3Cgale_pubme%3EA193988629%3C/gale_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=204563746&rft_id=info:pmid/19194444&rft_galeid=A193988629&rfr_iscdi=true |