Conformational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomes
Incubation of X-31 influenza virus at 62° results in changes in hemagglutinin structure which cause the virus to fuse with liposomes at neutral pH. Mutants of X-31 which contain different hemagglutinins and as a consequence fuse with liposomes at higher pH than wild-type virus also fuse at a lower t...
Gespeichert in:
| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 1986-12, Vol.155 (2), p.484-497 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 497 |
|---|---|
| container_issue | 2 |
| container_start_page | 484 |
| container_title | Virology (New York, N.Y.) |
| container_volume | 155 |
| creator | Ruigrok, R.W.H. Martin, S.R. Wharton, S.A. Skehel, J.J. Bayley, P.M. Wiley, D.C. |
| description | Incubation of X-31 influenza virus at 62° results in changes in hemagglutinin structure which cause the virus to fuse with liposomes at neutral pH. Mutants of X-31 which contain different hemagglutinins and as a consequence fuse with liposomes at higher pH than wild-type virus also fuse at a lower temperature. The heat-induced changes in hemagglutinin structure were monitored by CD, fluorescence spectroscopy, electron microscopy, and proteolytic digestion and compared with the characteristic changes which occur at low pH required for hemagglutinin-mediated membrane fusion at physiological temperature. The results indicate that the heat-induced changes in hemagglutinin which allow fusion activity result in partial denaturation of the molecule. By comparison the changes in structure required for fusion at low pH and normal temperature are specifically restricted. |
| doi_str_mv | 10.1016/0042-6822(86)90210-2 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_77198980</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0042682286902102</els_id><sourcerecordid>14679185</sourcerecordid><originalsourceid>FETCH-LOGICAL-c417t-e7fc29cf060b7659e7b3961bff01a88e5c3223907a38baa2f8610e3f9a94c1fc3</originalsourceid><addsrcrecordid>eNqFkUuLFDEUhYMoYzv6DxRqIaKL0jyq89gI0viCATe6DrfSN12RqqRNqkZmfr1pu-ilrkLu_c7hcg4hzxl9yyiT7yjteCs156-1fGMoZ7TlD8iGUSNbKjr2kGwuyGPypJSftP6VolfkSiitqWQbcr9L0ac8wRxShLFxA8QDlibEZh6wGXCCw2Fc5hDrJPk69-OC8R6a25CX0vweghsacC5NR4h3VQBzG-J-cbhv_FKq60m2wmEemjEcU0kTlqfkkYex4LP1vSY_Pn38vvvS3nz7_HX34aZ1HVNzi8o7bpynkvZKbg2qXhjJeu8pA61x6wTnwlAFQvcA3GvJKApvwHSOeSeuyauz7zGnXwuW2U6hOBxHiJiWYpViRhtN_wuyTirD9LaC3Rl0OZWS0dtjDhPkO8uoPXVjT8HbU_BWS_u3G8ur7MXqv_QT7i-itYy6f7nuoTgYfYboQrlgmgnDlKrY-zOGNbTbgNkWFzDWwENGN9t9Cv--4w8uA6y8</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>14679185</pqid></control><display><type>article</type><title>Conformational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomes</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><creator>Ruigrok, R.W.H. ; Martin, S.R. ; Wharton, S.A. ; Skehel, J.J. ; Bayley, P.M. ; Wiley, D.C.</creator><creatorcontrib>Ruigrok, R.W.H. ; Martin, S.R. ; Wharton, S.A. ; Skehel, J.J. ; Bayley, P.M. ; Wiley, D.C.</creatorcontrib><description>Incubation of X-31 influenza virus at 62° results in changes in hemagglutinin structure which cause the virus to fuse with liposomes at neutral pH. Mutants of X-31 which contain different hemagglutinins and as a consequence fuse with liposomes at higher pH than wild-type virus also fuse at a lower temperature. The heat-induced changes in hemagglutinin structure were monitored by CD, fluorescence spectroscopy, electron microscopy, and proteolytic digestion and compared with the characteristic changes which occur at low pH required for hemagglutinin-mediated membrane fusion at physiological temperature. The results indicate that the heat-induced changes in hemagglutinin which allow fusion activity result in partial denaturation of the molecule. By comparison the changes in structure required for fusion at low pH and normal temperature are specifically restricted.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/0042-6822(86)90210-2</identifier><identifier>PMID: 3788061</identifier><identifier>CODEN: VIRLAX</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; hemagglutinins ; Hemagglutinins, Viral - physiology ; Hydrogen-Ion Concentration ; influenza virus ; Liposomes ; Membrane Fusion ; Microbiology ; Microscopy, Electron ; Models, Molecular ; Mutation ; Orthomyxoviridae - physiology ; Peptide Fragments ; Protein Conformation ; Protein Denaturation ; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains ; Temperature ; Trypsin - metabolism ; Virology</subject><ispartof>Virology (New York, N.Y.), 1986-12, Vol.155 (2), p.484-497</ispartof><rights>1986</rights><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-e7fc29cf060b7659e7b3961bff01a88e5c3223907a38baa2f8610e3f9a94c1fc3</citedby><cites>FETCH-LOGICAL-c417t-e7fc29cf060b7659e7b3961bff01a88e5c3223907a38baa2f8610e3f9a94c1fc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0042-6822(86)90210-2$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8139177$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3788061$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ruigrok, R.W.H.</creatorcontrib><creatorcontrib>Martin, S.R.</creatorcontrib><creatorcontrib>Wharton, S.A.</creatorcontrib><creatorcontrib>Skehel, J.J.</creatorcontrib><creatorcontrib>Bayley, P.M.</creatorcontrib><creatorcontrib>Wiley, D.C.</creatorcontrib><title>Conformational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomes</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>Incubation of X-31 influenza virus at 62° results in changes in hemagglutinin structure which cause the virus to fuse with liposomes at neutral pH. Mutants of X-31 which contain different hemagglutinins and as a consequence fuse with liposomes at higher pH than wild-type virus also fuse at a lower temperature. The heat-induced changes in hemagglutinin structure were monitored by CD, fluorescence spectroscopy, electron microscopy, and proteolytic digestion and compared with the characteristic changes which occur at low pH required for hemagglutinin-mediated membrane fusion at physiological temperature. The results indicate that the heat-induced changes in hemagglutinin which allow fusion activity result in partial denaturation of the molecule. By comparison the changes in structure required for fusion at low pH and normal temperature are specifically restricted.</description><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>hemagglutinins</subject><subject>Hemagglutinins, Viral - physiology</subject><subject>Hydrogen-Ion Concentration</subject><subject>influenza virus</subject><subject>Liposomes</subject><subject>Membrane Fusion</subject><subject>Microbiology</subject><subject>Microscopy, Electron</subject><subject>Models, Molecular</subject><subject>Mutation</subject><subject>Orthomyxoviridae - physiology</subject><subject>Peptide Fragments</subject><subject>Protein Conformation</subject><subject>Protein Denaturation</subject><subject>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</subject><subject>Temperature</subject><subject>Trypsin - metabolism</subject><subject>Virology</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUuLFDEUhYMoYzv6DxRqIaKL0jyq89gI0viCATe6DrfSN12RqqRNqkZmfr1pu-ilrkLu_c7hcg4hzxl9yyiT7yjteCs156-1fGMoZ7TlD8iGUSNbKjr2kGwuyGPypJSftP6VolfkSiitqWQbcr9L0ac8wRxShLFxA8QDlibEZh6wGXCCw2Fc5hDrJPk69-OC8R6a25CX0vweghsacC5NR4h3VQBzG-J-cbhv_FKq60m2wmEemjEcU0kTlqfkkYex4LP1vSY_Pn38vvvS3nz7_HX34aZ1HVNzi8o7bpynkvZKbg2qXhjJeu8pA61x6wTnwlAFQvcA3GvJKApvwHSOeSeuyauz7zGnXwuW2U6hOBxHiJiWYpViRhtN_wuyTirD9LaC3Rl0OZWS0dtjDhPkO8uoPXVjT8HbU_BWS_u3G8ur7MXqv_QT7i-itYy6f7nuoTgYfYboQrlgmgnDlKrY-zOGNbTbgNkWFzDWwENGN9t9Cv--4w8uA6y8</recordid><startdate>19861201</startdate><enddate>19861201</enddate><creator>Ruigrok, R.W.H.</creator><creator>Martin, S.R.</creator><creator>Wharton, S.A.</creator><creator>Skehel, J.J.</creator><creator>Bayley, P.M.</creator><creator>Wiley, D.C.</creator><general>Elsevier Inc</general><general>Elsevier</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>7QL</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19861201</creationdate><title>Conformational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomes</title><author>Ruigrok, R.W.H. ; Martin, S.R. ; Wharton, S.A. ; Skehel, J.J. ; Bayley, P.M. ; Wiley, D.C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-e7fc29cf060b7659e7b3961bff01a88e5c3223907a38baa2f8610e3f9a94c1fc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>hemagglutinins</topic><topic>Hemagglutinins, Viral - physiology</topic><topic>Hydrogen-Ion Concentration</topic><topic>influenza virus</topic><topic>Liposomes</topic><topic>Membrane Fusion</topic><topic>Microbiology</topic><topic>Microscopy, Electron</topic><topic>Models, Molecular</topic><topic>Mutation</topic><topic>Orthomyxoviridae - physiology</topic><topic>Peptide Fragments</topic><topic>Protein Conformation</topic><topic>Protein Denaturation</topic><topic>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</topic><topic>Temperature</topic><topic>Trypsin - metabolism</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ruigrok, R.W.H.</creatorcontrib><creatorcontrib>Martin, S.R.</creatorcontrib><creatorcontrib>Wharton, S.A.</creatorcontrib><creatorcontrib>Skehel, J.J.</creatorcontrib><creatorcontrib>Bayley, P.M.</creatorcontrib><creatorcontrib>Wiley, D.C.</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>Bacteriology Abstracts (Microbiology B)</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>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ruigrok, R.W.H.</au><au>Martin, S.R.</au><au>Wharton, S.A.</au><au>Skehel, J.J.</au><au>Bayley, P.M.</au><au>Wiley, D.C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Conformational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomes</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>1986-12-01</date><risdate>1986</risdate><volume>155</volume><issue>2</issue><spage>484</spage><epage>497</epage><pages>484-497</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><coden>VIRLAX</coden><abstract>Incubation of X-31 influenza virus at 62° results in changes in hemagglutinin structure which cause the virus to fuse with liposomes at neutral pH. Mutants of X-31 which contain different hemagglutinins and as a consequence fuse with liposomes at higher pH than wild-type virus also fuse at a lower temperature. The heat-induced changes in hemagglutinin structure were monitored by CD, fluorescence spectroscopy, electron microscopy, and proteolytic digestion and compared with the characteristic changes which occur at low pH required for hemagglutinin-mediated membrane fusion at physiological temperature. The results indicate that the heat-induced changes in hemagglutinin which allow fusion activity result in partial denaturation of the molecule. By comparison the changes in structure required for fusion at low pH and normal temperature are specifically restricted.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>3788061</pmid><doi>10.1016/0042-6822(86)90210-2</doi><tpages>14</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0042-6822 |
| ispartof | Virology (New York, N.Y.), 1986-12, Vol.155 (2), p.484-497 |
| issn | 0042-6822 1096-0341 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77198980 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Biological and medical sciences Fundamental and applied biological sciences. Psychology hemagglutinins Hemagglutinins, Viral - physiology Hydrogen-Ion Concentration influenza virus Liposomes Membrane Fusion Microbiology Microscopy, Electron Models, Molecular Mutation Orthomyxoviridae - physiology Peptide Fragments Protein Conformation Protein Denaturation Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Temperature Trypsin - metabolism Virology |
| title | Conformational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomes |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T18%3A21%3A20IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Conformational%20changes%20in%20the%20hemagglutinin%20of%20influenza%20virus%20which%20accompany%20heat-induced%20fusion%20of%20virus%20with%20liposomes&rft.jtitle=Virology%20(New%20York,%20N.Y.)&rft.au=Ruigrok,%20R.W.H.&rft.date=1986-12-01&rft.volume=155&rft.issue=2&rft.spage=484&rft.epage=497&rft.pages=484-497&rft.issn=0042-6822&rft.eissn=1096-0341&rft.coden=VIRLAX&rft_id=info:doi/10.1016/0042-6822(86)90210-2&rft_dat=%3Cproquest_cross%3E14679185%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=14679185&rft_id=info:pmid/3788061&rft_els_id=0042682286902102&rfr_iscdi=true |