Insertion of a Coiled-Coil Peptide From Influenza Virus Hemagglutinin Into Membranes
The trimeric protein hemagglutinin (HA) of the influenza viral envelope is essential for cell entry. To investigate the interaction of HA with membranes, two 40-residue, cysteine-substituted peptides comprising the loop region and the first part of the coiled-coil stem were synthesized and modified...
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| Veröffentlicht in: | Science 1994-10, Vol.266 (5183), p.274-276 |
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| creator | Yu, Yeon Gyu King, David S. Shin, Yeon-Kyun |
| description | The trimeric protein hemagglutinin (HA) of the influenza viral envelope is essential for cell entry. To investigate the interaction of HA with membranes, two 40-residue, cysteine-substituted peptides comprising the loop region and the first part of the coiled-coil stem were synthesized and modified with a nitroxide spin label. Electron paramagnetic resonance analysis revealed that the peptide inserts reversibly into phospholipid vesicles under endosomal pH conditions. This result suggests that some or all of the long coiled-coil trimer of HA may insert into membranes, which could bring the viral and cell membranes closer together and facilitate fusion. |
| doi_str_mv | 10.1126/science.7939662 |
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To investigate the interaction of HA with membranes, two 40-residue, cysteine-substituted peptides comprising the loop region and the first part of the coiled-coil stem were synthesized and modified with a nitroxide spin label. Electron paramagnetic resonance analysis revealed that the peptide inserts reversibly into phospholipid vesicles under endosomal pH conditions. This result suggests that some or all of the long coiled-coil trimer of HA may insert into membranes, which could bring the viral and cell membranes closer together and facilitate fusion.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.7939662</identifier><identifier>PMID: 7939662</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Amino Acid Sequence ; BIOCHEMISTRY ; Biological and medical sciences ; BIOLOGY AND MEDICINE, BASIC STUDIES ; CELL MEMBRANES ; Electron Spin Resonance Spectroscopy ; Endocytosis ; Fundamental and applied biological sciences. Psychology ; Hemagglutinin Glycoproteins, Influenza Virus ; Hemagglutinins, Viral - chemistry ; Hemagglutinins, Viral - metabolism ; Hydrogen-Ion Concentration ; INFECTIVITY ; influenza virus ; INFLUENZA VIRUSES ; Line spectra ; Lipid Bilayers - metabolism ; Membrane Fusion ; Microbiology ; Molecular Sequence Data ; MOLECULAR STRUCTURE ; Orthomyxoviridae ; Orthomyxoviridae - physiology ; Oxygen ; P branes ; PEPTIDES ; Phospholipids ; Physiological aspects ; Protein Conformation ; Protein Structure, Secondary ; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains ; Spectral index ; Spin labels ; String theory ; Temperature ; Trimers ; Viral Envelope Proteins - chemistry ; Viral Envelope Proteins - metabolism ; Virology</subject><ispartof>Science, 1994-10, Vol.266 (5183), p.274-276</ispartof><rights>Copyright 1994 American Association for the Advancement of Science</rights><rights>1995 INIST-CNRS</rights><rights>COPYRIGHT 1994 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1994 American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c672t-8d6d5daa0dc8a8a21a71df771d055e7ca733f032bb3a7ee36054cba249e659783</citedby><cites>FETCH-LOGICAL-c672t-8d6d5daa0dc8a8a21a71df771d055e7ca733f032bb3a7ee36054cba249e659783</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2884771$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2884771$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,881,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3316667$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7939662$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/70335$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Yu, Yeon Gyu</creatorcontrib><creatorcontrib>King, David S.</creatorcontrib><creatorcontrib>Shin, Yeon-Kyun</creatorcontrib><title>Insertion of a Coiled-Coil Peptide From Influenza Virus Hemagglutinin Into Membranes</title><title>Science</title><addtitle>Science</addtitle><description>The trimeric protein hemagglutinin (HA) of the influenza viral envelope is essential for cell entry. To investigate the interaction of HA with membranes, two 40-residue, cysteine-substituted peptides comprising the loop region and the first part of the coiled-coil stem were synthesized and modified with a nitroxide spin label. Electron paramagnetic resonance analysis revealed that the peptide inserts reversibly into phospholipid vesicles under endosomal pH conditions. This result suggests that some or all of the long coiled-coil trimer of HA may insert into membranes, which could bring the viral and cell membranes closer together and facilitate fusion.</description><subject>Amino Acid Sequence</subject><subject>BIOCHEMISTRY</subject><subject>Biological and medical sciences</subject><subject>BIOLOGY AND MEDICINE, BASIC STUDIES</subject><subject>CELL MEMBRANES</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Endocytosis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus</subject><subject>Hemagglutinins, Viral - chemistry</subject><subject>Hemagglutinins, Viral - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>INFECTIVITY</subject><subject>influenza virus</subject><subject>INFLUENZA VIRUSES</subject><subject>Line spectra</subject><subject>Lipid Bilayers - metabolism</subject><subject>Membrane Fusion</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>MOLECULAR STRUCTURE</subject><subject>Orthomyxoviridae</subject><subject>Orthomyxoviridae - physiology</subject><subject>Oxygen</subject><subject>P branes</subject><subject>PEPTIDES</subject><subject>Phospholipids</subject><subject>Physiological aspects</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</subject><subject>Spectral index</subject><subject>Spin labels</subject><subject>String theory</subject><subject>Temperature</subject><subject>Trimers</subject><subject>Viral Envelope Proteins - chemistry</subject><subject>Viral Envelope Proteins - metabolism</subject><subject>Virology</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqN0k9r2zAcBmAzNrq023mXDXwYZYe6la3oj49dWNNAtgzW9SoU-WdPRZYySYZtn34KMRmBwILAOryPJCO9WfamRNdlWdGboDRYBdesxjWl1bNsUqKaFHWF8PNsghCmBUeMvMzOQ3hCKGU1PsvORj7JHhY2gI_a2dy1ucxnThtoiu2Uf4VN1A3kd971-cK2ZgD7R-aP2g8hv4dedp0ZorbapjS6_DP0ay8thFfZi1aaAK_H-SL7fvfpYXZfLFfzxex2WSjKqljwhjakkRI1iksuq1KysmlZ-iBCgCnJMG4RrtZrLBkApohM1VpW0xooqRnHF1m-29eFqEW6igjqh3LWgoqCIYxJIpc7svHu5wAhil4HBcak_3RDEIwyznjJ_gtLWjNWk2mCVzvYSQNC29ZFL1UHFrw0zkKbLlDcloQTgvl23-IIT6OBXqtj_sOBTyTCr9jJIQSx-PblZLp6PJl-nJ9K-Xx5QK-OUeWMgQ5EeuvZ6oDf7LjyLgQPrdh43Uv_W5RIbNssxjaLsZ5pxbvxUYZ1D83e_8vfj7kMSpo2tU_psGcYl5TS7cFvd-wpROf3ccX5NLUN_wWHPQJs</recordid><startdate>19941014</startdate><enddate>19941014</enddate><creator>Yu, Yeon Gyu</creator><creator>King, David S.</creator><creator>Shin, Yeon-Kyun</creator><general>American Society for the Advancement of Science</general><general>American Association for the Advancement of Science</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>8GL</scope><scope>IBG</scope><scope>IOV</scope><scope>ISN</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>19941014</creationdate><title>Insertion of a Coiled-Coil Peptide From Influenza Virus Hemagglutinin Into Membranes</title><author>Yu, Yeon Gyu ; King, David S. ; Shin, Yeon-Kyun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c672t-8d6d5daa0dc8a8a21a71df771d055e7ca733f032bb3a7ee36054cba249e659783</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>BIOCHEMISTRY</topic><topic>Biological and medical sciences</topic><topic>BIOLOGY AND MEDICINE, BASIC STUDIES</topic><topic>CELL MEMBRANES</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Endocytosis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hemagglutinin Glycoproteins, Influenza Virus</topic><topic>Hemagglutinins, Viral - chemistry</topic><topic>Hemagglutinins, Viral - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>INFECTIVITY</topic><topic>influenza virus</topic><topic>INFLUENZA VIRUSES</topic><topic>Line spectra</topic><topic>Lipid Bilayers - metabolism</topic><topic>Membrane Fusion</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>MOLECULAR STRUCTURE</topic><topic>Orthomyxoviridae</topic><topic>Orthomyxoviridae - physiology</topic><topic>Oxygen</topic><topic>P branes</topic><topic>PEPTIDES</topic><topic>Phospholipids</topic><topic>Physiological aspects</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</topic><topic>Spectral index</topic><topic>Spin labels</topic><topic>String theory</topic><topic>Temperature</topic><topic>Trimers</topic><topic>Viral Envelope Proteins - chemistry</topic><topic>Viral Envelope Proteins - metabolism</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yu, Yeon Gyu</creatorcontrib><creatorcontrib>King, David S.</creatorcontrib><creatorcontrib>Shin, Yeon-Kyun</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>Gale In Context: High School</collection><collection>Gale In Context: Biography</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Canada</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yu, Yeon Gyu</au><au>King, David S.</au><au>Shin, Yeon-Kyun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Insertion of a Coiled-Coil Peptide From Influenza Virus Hemagglutinin Into Membranes</atitle><jtitle>Science</jtitle><addtitle>Science</addtitle><date>1994-10-14</date><risdate>1994</risdate><volume>266</volume><issue>5183</issue><spage>274</spage><epage>276</epage><pages>274-276</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>The trimeric protein hemagglutinin (HA) of the influenza viral envelope is essential for cell entry. To investigate the interaction of HA with membranes, two 40-residue, cysteine-substituted peptides comprising the loop region and the first part of the coiled-coil stem were synthesized and modified with a nitroxide spin label. Electron paramagnetic resonance analysis revealed that the peptide inserts reversibly into phospholipid vesicles under endosomal pH conditions. This result suggests that some or all of the long coiled-coil trimer of HA may insert into membranes, which could bring the viral and cell membranes closer together and facilitate fusion.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>7939662</pmid><doi>10.1126/science.7939662</doi><tpages>3</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science, 1994-10, Vol.266 (5183), p.274-276 |
| issn | 0036-8075 1095-9203 |
| language | eng |
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| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Amino Acid Sequence BIOCHEMISTRY Biological and medical sciences BIOLOGY AND MEDICINE, BASIC STUDIES CELL MEMBRANES Electron Spin Resonance Spectroscopy Endocytosis Fundamental and applied biological sciences. Psychology Hemagglutinin Glycoproteins, Influenza Virus Hemagglutinins, Viral - chemistry Hemagglutinins, Viral - metabolism Hydrogen-Ion Concentration INFECTIVITY influenza virus INFLUENZA VIRUSES Line spectra Lipid Bilayers - metabolism Membrane Fusion Microbiology Molecular Sequence Data MOLECULAR STRUCTURE Orthomyxoviridae Orthomyxoviridae - physiology Oxygen P branes PEPTIDES Phospholipids Physiological aspects Protein Conformation Protein Structure, Secondary Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Spectral index Spin labels String theory Temperature Trimers Viral Envelope Proteins - chemistry Viral Envelope Proteins - metabolism Virology |
| title | Insertion of a Coiled-Coil Peptide From Influenza Virus Hemagglutinin Into Membranes |
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