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Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structure
The HIV-1 spike is a trimer of the transmembrane gp41 and the peripheral gp120 subunit pair. It is activated for virus–cell membrane fusion by binding sequentially to CD4 and to a chemokine receptor. Here we have studied the structural transition of the trimeric spike during the activation process....
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| Published in: | Proceedings of the National Academy of Sciences - PNAS 2010-11, Vol.107 (44), p.18844-18849 |
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| container_issue | 44 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Wu, Shang-Rung Löving, Robin Lindqvist, Birgitta Hebert, Hans Koeck, Philip J. B. Sjöberg, Mathilda Garoff, Henrik Goff, Stephen P. |
| description | The HIV-1 spike is a trimer of the transmembrane gp41 and the peripheral gp120 subunit pair. It is activated for virus–cell membrane fusion by binding sequentially to CD4 and to a chemokine receptor. Here we have studied the structural transition of the trimeric spike during the activation process. We solubilized and isolated unliganded and CD4-bound spikes from virus-like particles and used cryoelectron microscopy to reconstruct their 3D structures. In order to increase the yield and stability of the spike, we used an endodomain deleted and gp120-gp41 disulfide-linked variant. The unliganded spike displayed a hollow cage-like structure where the gp120-gp41 protomeric units formed a roof and bottom, and separated lobes and legs on the sides. The tripod structure was verified by fitting the recent atomic core structure of gp120 with intact N- and C-terminal ends into the spike density map. This defined the lobe as gp120 core, showed that the legs contained the polypeptide termini, and suggested the deleted variable loops V1/V2 and V3 to occupy the roof and gp41 the bottom. CD4 binding shifted the roof density peripherally and condensed the bottom density centrally. Fitting with a V3 containing gp120 core suggested that the V1/V2 loops in the roof were displaced laterally and the V3 lifted up, while the core and leg were kept in place. The loop displacements probably prepared the spike for coreceptor interaction and roof opening so that a new fusion-active gp41 structure, assembled at the center of the cage bottom, could reach the target membrane. |
| doi_str_mv | 10.1073/pnas.1007227107 |
| format | article |
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B. ; Sjöberg, Mathilda ; Garoff, Henrik ; Goff, Stephen P.</creator><creatorcontrib>Wu, Shang-Rung ; Löving, Robin ; Lindqvist, Birgitta ; Hebert, Hans ; Koeck, Philip J. B. ; Sjöberg, Mathilda ; Garoff, Henrik ; Goff, Stephen P.</creatorcontrib><description>The HIV-1 spike is a trimer of the transmembrane gp41 and the peripheral gp120 subunit pair. It is activated for virus–cell membrane fusion by binding sequentially to CD4 and to a chemokine receptor. Here we have studied the structural transition of the trimeric spike during the activation process. We solubilized and isolated unliganded and CD4-bound spikes from virus-like particles and used cryoelectron microscopy to reconstruct their 3D structures. In order to increase the yield and stability of the spike, we used an endodomain deleted and gp120-gp41 disulfide-linked variant. The unliganded spike displayed a hollow cage-like structure where the gp120-gp41 protomeric units formed a roof and bottom, and separated lobes and legs on the sides. The tripod structure was verified by fitting the recent atomic core structure of gp120 with intact N- and C-terminal ends into the spike density map. This defined the lobe as gp120 core, showed that the legs contained the polypeptide termini, and suggested the deleted variable loops V1/V2 and V3 to occupy the roof and gp41 the bottom. CD4 binding shifted the roof density peripherally and condensed the bottom density centrally. Fitting with a V3 containing gp120 core suggested that the V1/V2 loops in the roof were displaced laterally and the V3 lifted up, while the core and leg were kept in place. The loop displacements probably prepared the spike for coreceptor interaction and roof opening so that a new fusion-active gp41 structure, assembled at the center of the cage bottom, could reach the target membrane.</description><identifier>ISSN: 0027-8424</identifier><identifier>ISSN: 1091-6490</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1007227107</identifier><identifier>PMID: 20956336</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Atomic structure ; Binding sites ; Biochemistry ; Biological Sciences ; CD4 antigen ; CD4 Antigens ; Cell membranes ; Chemokine receptors ; cryo-EM ; Cryoelectron Microscopy ; Cytokines ; Electron microscopes ; EMAN ; Glycoprotein gp120 ; glycoprotein gp41 ; Glycoproteins ; HIV ; HIV 1 ; HIV Envelope Protein gp120 ; HIV Envelope Protein gp41 ; HIV-1 - chemistry ; HIV-1 - ultrastructure ; Human immunodeficiency virus ; Human immunodeficiency virus 1 ; Humans ; Imaging, Three-Dimensional ; Leg ; Medicin och hälsovetenskap ; Membrane fusion ; Membranes ; Microscopy ; Models, Molecular ; Peptides ; receptor triggering ; retrovirus spike ; Roofs ; single particle imaging ; Trimers ; Tripods ; Viral morphology ; Virus-like particles ; Viruses</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2010-11, Vol.107 (44), p.18844-18849</ispartof><rights>Copyright National Academy of Sciences Nov 2, 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c685t-18abe75866870f917102690e4b4c9c627aec5ac1dfbd512c1820151bf0628dea3</citedby><cites>FETCH-LOGICAL-c685t-18abe75866870f917102690e4b4c9c627aec5ac1dfbd512c1820151bf0628dea3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/107/44.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/25748584$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/25748584$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,733,786,790,891,27957,27958,53827,53829,58593,58826</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20956336$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-82934$$DView record from Swedish Publication Index$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:121531688$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Wu, Shang-Rung</creatorcontrib><creatorcontrib>Löving, Robin</creatorcontrib><creatorcontrib>Lindqvist, Birgitta</creatorcontrib><creatorcontrib>Hebert, Hans</creatorcontrib><creatorcontrib>Koeck, Philip J. B.</creatorcontrib><creatorcontrib>Sjöberg, Mathilda</creatorcontrib><creatorcontrib>Garoff, Henrik</creatorcontrib><creatorcontrib>Goff, Stephen P.</creatorcontrib><title>Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structure</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The HIV-1 spike is a trimer of the transmembrane gp41 and the peripheral gp120 subunit pair. It is activated for virus–cell membrane fusion by binding sequentially to CD4 and to a chemokine receptor. Here we have studied the structural transition of the trimeric spike during the activation process. We solubilized and isolated unliganded and CD4-bound spikes from virus-like particles and used cryoelectron microscopy to reconstruct their 3D structures. In order to increase the yield and stability of the spike, we used an endodomain deleted and gp120-gp41 disulfide-linked variant. The unliganded spike displayed a hollow cage-like structure where the gp120-gp41 protomeric units formed a roof and bottom, and separated lobes and legs on the sides. The tripod structure was verified by fitting the recent atomic core structure of gp120 with intact N- and C-terminal ends into the spike density map. This defined the lobe as gp120 core, showed that the legs contained the polypeptide termini, and suggested the deleted variable loops V1/V2 and V3 to occupy the roof and gp41 the bottom. CD4 binding shifted the roof density peripherally and condensed the bottom density centrally. Fitting with a V3 containing gp120 core suggested that the V1/V2 loops in the roof were displaced laterally and the V3 lifted up, while the core and leg were kept in place. The loop displacements probably prepared the spike for coreceptor interaction and roof opening so that a new fusion-active gp41 structure, assembled at the center of the cage bottom, could reach the target membrane.</description><subject>Atomic structure</subject><subject>Binding sites</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>CD4 antigen</subject><subject>CD4 Antigens</subject><subject>Cell membranes</subject><subject>Chemokine receptors</subject><subject>cryo-EM</subject><subject>Cryoelectron Microscopy</subject><subject>Cytokines</subject><subject>Electron microscopes</subject><subject>EMAN</subject><subject>Glycoprotein gp120</subject><subject>glycoprotein gp41</subject><subject>Glycoproteins</subject><subject>HIV</subject><subject>HIV 1</subject><subject>HIV Envelope Protein gp120</subject><subject>HIV Envelope Protein gp41</subject><subject>HIV-1 - chemistry</subject><subject>HIV-1 - ultrastructure</subject><subject>Human immunodeficiency virus</subject><subject>Human immunodeficiency virus 1</subject><subject>Humans</subject><subject>Imaging, Three-Dimensional</subject><subject>Leg</subject><subject>Medicin och hälsovetenskap</subject><subject>Membrane fusion</subject><subject>Membranes</subject><subject>Microscopy</subject><subject>Models, Molecular</subject><subject>Peptides</subject><subject>receptor triggering</subject><subject>retrovirus spike</subject><subject>Roofs</subject><subject>single particle imaging</subject><subject>Trimers</subject><subject>Tripods</subject><subject>Viral morphology</subject><subject>Virus-like particles</subject><subject>Viruses</subject><issn>0027-8424</issn><issn>1091-6490</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><recordid>eNqNkk1v1DAQhiMEokvhzAlkcYEDobbj-OOCVJWPVqrEAegRy3Fmd72bjVPbKdp_j8MuXYoE4mB5NH7mHc34LYqnBL8hWFQnQ29ijrCgVOTEvWJGsCIlZwrfL2YYU1FKRtlR8SjGFcZY1RI_LI5oDnhV8Vnx7bPrFx2UgwnJ2Q6QDVsPHdgUfI82zgYfrR-2yPSm20YXUYAbMF1EaQno_OKqJCgObg3IRGRQCm7wLYopjDaNAR4XD-YZhif7-7j4-uH9l7Pz8vLTx4uz08vSclmnkkjTgKgl51LguSJ5FsoVBtYwqyynwoCtjSXtvGlrQi2RFJOaNHPMqWzBVMeF2unG7zCMjR6C25iw1d64HPtW7_NrNx0dQRNK6opwKXPt67_WvnNXp9qHhV6npZZUVSzjb3d4ZjfQWuhTMN3djndeerfUC3-jqRKVFFO_l3uB4K9HiElvXLTQdaYHP0YtOGUSMzaRr_5J5i1hWWW8-l-UcJXRF3-gKz-G_L0_WwsimJpan-ygyQAxwPx2QIL1ZD09WU8frJcrnv--l1v-l9cygPbAVHmQE5oxTaRk026f7ZBVTD4cJGrBZC1Z9QMQUeoo</recordid><startdate>20101102</startdate><enddate>20101102</enddate><creator>Wu, Shang-Rung</creator><creator>Löving, Robin</creator><creator>Lindqvist, Birgitta</creator><creator>Hebert, Hans</creator><creator>Koeck, Philip J. B.</creator><creator>Sjöberg, Mathilda</creator><creator>Garoff, Henrik</creator><creator>Goff, Stephen P.</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><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>7X8</scope><scope>5PM</scope><scope>ADTPV</scope><scope>AOWAS</scope><scope>D8V</scope><scope>D8T</scope><scope>ZZAVC</scope></search><sort><creationdate>20101102</creationdate><title>Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structure</title><author>Wu, Shang-Rung ; Löving, Robin ; Lindqvist, Birgitta ; Hebert, Hans ; Koeck, Philip J. 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B.</creatorcontrib><creatorcontrib>Sjöberg, Mathilda</creatorcontrib><creatorcontrib>Garoff, Henrik</creatorcontrib><creatorcontrib>Goff, Stephen P.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>SwePub</collection><collection>SwePub Articles</collection><collection>SWEPUB Kungliga Tekniska Högskolan</collection><collection>SWEPUB Freely available online</collection><collection>SwePub Articles full text</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wu, Shang-Rung</au><au>Löving, Robin</au><au>Lindqvist, Birgitta</au><au>Hebert, Hans</au><au>Koeck, Philip J. B.</au><au>Sjöberg, Mathilda</au><au>Garoff, Henrik</au><au>Goff, Stephen P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structure</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2010-11-02</date><risdate>2010</risdate><volume>107</volume><issue>44</issue><spage>18844</spage><epage>18849</epage><pages>18844-18849</pages><issn>0027-8424</issn><issn>1091-6490</issn><eissn>1091-6490</eissn><notes>ObjectType-Article-2</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-1</notes><notes>content type line 23</notes><notes>ObjectType-Article-1</notes><notes>ObjectType-Feature-2</notes><notes>Edited by Stephen P. Goff, Columbia University College of Physicians and Surgeons, New York, NY, and approved September 9, 2010 (received for review May 27, 2010)</notes><notes>Author contributions: S.-R.W., R.L., H.H., P.J.B.K., M.S., and H.G. designed research; S.-R.W., R.L., B.L., and M.S. performed research; S.-R.W., R.L., H.H., P.J.B.K., M.S., and H.G. analyzed data; and S.-R.W., R.L., M.S., and H.G. wrote the paper.</notes><notes>1S.-R.W. and R.L. contributed equally to this work.</notes><abstract>The HIV-1 spike is a trimer of the transmembrane gp41 and the peripheral gp120 subunit pair. It is activated for virus–cell membrane fusion by binding sequentially to CD4 and to a chemokine receptor. Here we have studied the structural transition of the trimeric spike during the activation process. We solubilized and isolated unliganded and CD4-bound spikes from virus-like particles and used cryoelectron microscopy to reconstruct their 3D structures. In order to increase the yield and stability of the spike, we used an endodomain deleted and gp120-gp41 disulfide-linked variant. The unliganded spike displayed a hollow cage-like structure where the gp120-gp41 protomeric units formed a roof and bottom, and separated lobes and legs on the sides. The tripod structure was verified by fitting the recent atomic core structure of gp120 with intact N- and C-terminal ends into the spike density map. This defined the lobe as gp120 core, showed that the legs contained the polypeptide termini, and suggested the deleted variable loops V1/V2 and V3 to occupy the roof and gp41 the bottom. CD4 binding shifted the roof density peripherally and condensed the bottom density centrally. Fitting with a V3 containing gp120 core suggested that the V1/V2 loops in the roof were displaced laterally and the V3 lifted up, while the core and leg were kept in place. The loop displacements probably prepared the spike for coreceptor interaction and roof opening so that a new fusion-active gp41 structure, assembled at the center of the cage bottom, could reach the target membrane.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>20956336</pmid><doi>10.1073/pnas.1007227107</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2010-11, Vol.107 (44), p.18844-18849 |
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| source | JSTOR Archival Journals and Primary Sources Collection; PubMed Central |
| subjects | Atomic structure Binding sites Biochemistry Biological Sciences CD4 antigen CD4 Antigens Cell membranes Chemokine receptors cryo-EM Cryoelectron Microscopy Cytokines Electron microscopes EMAN Glycoprotein gp120 glycoprotein gp41 Glycoproteins HIV HIV 1 HIV Envelope Protein gp120 HIV Envelope Protein gp41 HIV-1 - chemistry HIV-1 - ultrastructure Human immunodeficiency virus Human immunodeficiency virus 1 Humans Imaging, Three-Dimensional Leg Medicin och hälsovetenskap Membrane fusion Membranes Microscopy Models, Molecular Peptides receptor triggering retrovirus spike Roofs single particle imaging Trimers Tripods Viral morphology Virus-like particles Viruses |
| title | Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structure |
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