The heads of the measles virus attachment protein move to transmit the fusion-triggering signal
Identifieur interne : 001A79 ( Istex/Corpus ); précédent : 001A78; suivant : 001A80The heads of the measles virus attachment protein move to transmit the fusion-triggering signal
Auteurs : Chanakha K. Navaratnarajah ; Numan Oezguen ; Levi Rupp ; Leah Kay ; Vincent H J. Leonard ; Werner Braun ; Roberto CattaneoSource :
- Nature Structural & Molecular Biology [ 1545-9993 ] ; 2011-02.
Abstract
The measles virus entry system, consisting of attachment (hemagglutinin, H) and fusion proteins, operates by means of a variety of natural and targeted receptors; however, the mechanism that triggers fusion of the viral envelope with the plasma membrane is not understood. Here, we tested a model proposing that the two heads of an H dimer, which are covalently linked at their base, after binding two receptor molecules, move relative to each other to transmit the fusion-triggering signal. Indeed, stabilizing the H-dimer interface with additional intermolecular disulfide bonds prevented membrane fusion, an effect that was reversed by a reducing agent. Moreover, a membrane-anchored designated receptor efficiently triggered fusion, provided that it engaged the H dimer at locations proximal to where the natural receptors bind and distal to the H-dimer interface. We discuss how receptors may force H-protein heads to switch partners and transmit the fusion-triggering signal.
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DOI: 10.1038/nsmb.1967
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Navaratnarajah</name><affiliation><mods:affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</mods:affiliation></affiliation><affiliation><mods:affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</mods:affiliation></affiliation></author><author><name sortKey="Oezguen, Numan" sort="Oezguen, Numan" uniqKey="Oezguen N" first="Numan" last="Oezguen">Numan Oezguen</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas, USA.</mods:affiliation></affiliation><affiliation><mods:affiliation>Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas, USA.</mods:affiliation></affiliation></author><author><name sortKey="Rupp, Levi" sort="Rupp, Levi" uniqKey="Rupp L" first="Levi" last="Rupp">Levi Rupp</name><affiliation><mods:affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</mods:affiliation></affiliation><affiliation><mods:affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</mods:affiliation></affiliation></author><author><name sortKey="Kay, Leah" sort="Kay, Leah" uniqKey="Kay L" first="Leah" last="Kay">Leah Kay</name><affiliation><mods:affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</mods:affiliation></affiliation><affiliation><mods:affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</mods:affiliation></affiliation></author><author><name sortKey="Leonard, Vincent H J" sort="Leonard, Vincent H J" uniqKey="Leonard V" first="Vincent H J" last="Leonard">Vincent H J. Leonard</name><affiliation><mods:affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</mods:affiliation></affiliation><affiliation><mods:affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</mods:affiliation></affiliation></author><author><name sortKey="Braun, Werner" sort="Braun, Werner" uniqKey="Braun W" first="Werner" last="Braun">Werner Braun</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas, USA.</mods:affiliation></affiliation><affiliation><mods:affiliation>Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas, USA.</mods:affiliation></affiliation></author><author><name sortKey="Cattaneo, Roberto" sort="Cattaneo, Roberto" uniqKey="Cattaneo R" first="Roberto" last="Cattaneo">Roberto Cattaneo</name><affiliation><mods:affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</mods:affiliation></affiliation><affiliation><mods:affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: cattaneo.roberto@mayo.edu</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:B8D1DB0332D5C4763449D8B5A6A2D3821B0C9BEC</idno><date when="2011" year="2011">2011</date><idno type="doi">10.1038/nsmb.1967</idno><idno type="url">https://api.istex.fr/document/B8D1DB0332D5C4763449D8B5A6A2D3821B0C9BEC/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001A79</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001A79</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">The heads of the measles virus attachment protein move to transmit the fusion-triggering signal</title><author><name sortKey="Navaratnarajah, Chanakha K" sort="Navaratnarajah, Chanakha K" uniqKey="Navaratnarajah C" first="Chanakha K" last="Navaratnarajah">Chanakha K. Navaratnarajah</name><affiliation><mods:affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</mods:affiliation></affiliation><affiliation><mods:affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</mods:affiliation></affiliation></author><author><name sortKey="Oezguen, Numan" sort="Oezguen, Numan" uniqKey="Oezguen N" first="Numan" last="Oezguen">Numan Oezguen</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas, USA.</mods:affiliation></affiliation><affiliation><mods:affiliation>Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas, USA.</mods:affiliation></affiliation></author><author><name sortKey="Rupp, Levi" sort="Rupp, Levi" uniqKey="Rupp L" first="Levi" last="Rupp">Levi Rupp</name><affiliation><mods:affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</mods:affiliation></affiliation><affiliation><mods:affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</mods:affiliation></affiliation></author><author><name sortKey="Kay, Leah" sort="Kay, Leah" uniqKey="Kay L" first="Leah" last="Kay">Leah Kay</name><affiliation><mods:affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</mods:affiliation></affiliation><affiliation><mods:affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</mods:affiliation></affiliation></author><author><name sortKey="Leonard, Vincent H J" sort="Leonard, Vincent H J" uniqKey="Leonard V" first="Vincent H J" last="Leonard">Vincent H J. Leonard</name><affiliation><mods:affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</mods:affiliation></affiliation><affiliation><mods:affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</mods:affiliation></affiliation></author><author><name sortKey="Braun, Werner" sort="Braun, Werner" uniqKey="Braun W" first="Werner" last="Braun">Werner Braun</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas, USA.</mods:affiliation></affiliation><affiliation><mods:affiliation>Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas, USA.</mods:affiliation></affiliation></author><author><name sortKey="Cattaneo, Roberto" sort="Cattaneo, Roberto" uniqKey="Cattaneo R" first="Roberto" last="Cattaneo">Roberto Cattaneo</name><affiliation><mods:affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</mods:affiliation></affiliation><affiliation><mods:affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: cattaneo.roberto@mayo.edu</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Nature Structural & Molecular Biology</title><idno type="ISSN">1545-9993</idno><idno type="eISSN">1545-9985</idno><imprint><publisher>Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.</publisher><date type="published" when="2011-02">2011-02</date><biblScope unit="volume">18</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="128">128</biblScope><biblScope unit="page" to="134">134</biblScope></imprint><idno type="ISSN">1545-9993</idno></series><idno type="istex">B8D1DB0332D5C4763449D8B5A6A2D3821B0C9BEC</idno><idno type="DOI">10.1038/nsmb.1967</idno><idno type="ArticleID">nsmb.1967</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1545-9993</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="eng">The measles virus entry system, consisting of attachment (hemagglutinin, H) and fusion proteins, operates by means of a variety of natural and targeted receptors; however, the mechanism that triggers fusion of the viral envelope with the plasma membrane is not understood. Here, we tested a model proposing that the two heads of an H dimer, which are covalently linked at their base, after binding two receptor molecules, move relative to each other to transmit the fusion-triggering signal. Indeed, stabilizing the H-dimer interface with additional intermolecular disulfide bonds prevented membrane fusion, an effect that was reversed by a reducing agent. Moreover, a membrane-anchored designated receptor efficiently triggered fusion, provided that it engaged the H dimer at locations proximal to where the natural receptors bind and distal to the H-dimer interface. We discuss how receptors may force H-protein heads to switch partners and transmit the fusion-triggering signal.</div></front></TEI><istex><corpusName>nature</corpusName><author><json:item><name>Chanakha K Navaratnarajah</name><affiliations><json:string>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</json:string><json:string>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</json:string></affiliations></json:item><json:item><name>Numan Oezguen</name><affiliations><json:string>Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas, USA.</json:string><json:string>Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas, USA.</json:string></affiliations></json:item><json:item><name>Levi Rupp</name><affiliations><json:string>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</json:string><json:string>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</json:string></affiliations></json:item><json:item><name>Leah Kay</name><affiliations><json:string>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</json:string><json:string>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</json:string></affiliations></json:item><json:item><name>Vincent H J Leonard</name><affiliations><json:string>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</json:string><json:string>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</json:string></affiliations></json:item><json:item><name>Werner Braun</name><affiliations><json:string>Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas, USA.</json:string><json:string>Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas, USA.</json:string></affiliations></json:item><json:item><name>Roberto Cattaneo</name><affiliations><json:string>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</json:string><json:string>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</json:string><json:string>E-mail: cattaneo.roberto@mayo.edu</json:string></affiliations></json:item></author><articleId><json:string>nsmb.1967</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>Article</json:string></originalGenre><abstract>The measles virus entry system, consisting of attachment (hemagglutinin, H) and fusion proteins, operates by means of a variety of natural and targeted receptors; however, the mechanism that triggers fusion of the viral envelope with the plasma membrane is not understood. Here, we tested a model proposing that the two heads of an H dimer, which are covalently linked at their base, after binding two receptor molecules, move relative to each other to transmit the fusion-triggering signal. Indeed, stabilizing the H-dimer interface with additional intermolecular disulfide bonds prevented membrane fusion, an effect that was reversed by a reducing agent. Moreover, a membrane-anchored designated receptor efficiently triggered fusion, provided that it engaged the H dimer at locations proximal to where the natural receptors bind and distal to the H-dimer interface. We discuss how receptors may force H-protein heads to switch partners and transmit the fusion-triggering signal.</abstract><qualityIndicators><score>8.24</score><pdfVersion>1.6</pdfVersion><pdfPageSize>594 x 783 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>0</keywordCount><abstractCharCount>981</abstractCharCount><pdfWordCount>6686</pdfWordCount><pdfCharCount>43030</pdfCharCount><pdfPageCount>8</pdfPageCount><abstractWordCount>145</abstractWordCount></qualityIndicators><title>The heads of the measles virus attachment protein move to transmit the fusion-triggering signal</title><refBibs><json:item><author><json:item><name>S.C. Harrison</name></json:item></author><host><volume>15</volume><pages><last>698</last><first>690</first></pages><author></author><title>Nat. Struct. Mol. Biol.</title></host><title>Viral membrane fusion</title></json:item><json:item><author><json:item><name>M. Marsh</name></json:item><json:item><name>A. Helenius</name></json:item></author><host><volume>124</volume><pages><last>740</last><first>729</first></pages><author></author><title>Cell</title></host><title>Virus entry: open sesame</title></json:item><json:item><author><json:item><name>K. Chandran</name></json:item><json:item><name>N.J. Sullivan</name></json:item><json:item><name>U. Felbor</name></json:item><json:item><name>S.P. Whelan</name></json:item><json:item><name>J.M. Cunningham</name></json:item></author><host><volume>308</volume><pages><last>1645</last><first>1643</first></pages><author></author><title>Science</title></host><title>Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection</title></json:item><json:item><author><json:item><name>R.A. Lamb</name></json:item><json:item><name>G.D. Parks</name></json:item></author><host><pages><last>1340</last><first>1305</first></pages><author></author><title>Fields Virology</title></host><title>Paramyxovirus: The viruses and their replication</title></json:item><json:item><host><author></author><title>Measles viruses</title></host></json:item><json:item><author><json:item><name>W.J. Moss</name></json:item></author><host><volume>330</volume><pages><last>189</last><first>173</first></pages><author></author><title>Curr. Top. Microbiol. Immunol.</title></host><title>Measles control and the prospect of eradication</title></json:item><json:item><author><json:item><name>E.C. Smith</name></json:item><json:item><name>A. Popa</name></json:item><json:item><name>A. Chang</name></json:item><json:item><name>C. Masante</name></json:item><json:item><name>R.E. Dutch</name></json:item></author><host><volume>276</volume><pages><last>7227</last><first>7217</first></pages><author></author><title>FEBS J.</title></host><title>Viral entry mechanisms: the increasing diversity of paramyxovirus entry</title></json:item><json:item><author><json:item><name>R. Cattaneo</name></json:item><json:item><name>T. Miest</name></json:item><json:item><name>E.V. Shashkova</name></json:item><json:item><name>M.A. Barry</name></json:item></author><host><volume>6</volume><pages><last>540</last><first>529</first></pages><author></author><title>Nat. Rev. Microbiol.</title></host><title>Reprogrammed viruses as cancer therapeutics: targeted, armed and shielded</title></json:item><json:item><author><json:item><name>S.J. Russell</name></json:item><json:item><name>K.-W. Measlesvirus Peng</name></json:item></author><host><volume>330</volume><pages><last>241</last><first>213</first></pages><author></author><title>Curr. Top. Microbiol. Immunol.</title></host><title>for cancer therapy</title></json:item><json:item><author><json:item><name>R. Cattaneo</name></json:item></author><host><volume>6</volume><pages><first>1000973</first></pages><author></author><title>PLoS Pathog.</title></host><title>Paramyxovirus entry and targeted vectors for cancer therapy</title></json:item><json:item><author><json:item><name>C.K. Navaratnarajah</name></json:item><json:item><name>V.H.J. Leonard</name></json:item><json:item><name>R. Cattaneo</name></json:item></author><host><volume>329</volume><pages><last>76</last><first>59</first></pages><author></author><title>Curr. Top. Microbiol. Immunol.</title></host><title>Measles virus glycoprotein complex assembly, receptor attachment and cell entry</title></json:item><json:item><author><json:item><name>R.M. Iorio</name></json:item><json:item><name>V. Melanson</name></json:item><json:item><name>P. Mahon</name></json:item></author><host><volume>4</volume><pages><last>351</last><first>335</first></pages><author></author><title>Future Virol.</title></host><title>Glycoprotein interactions in paramyxovirus fusion</title></json:item><json:item><author><json:item><name>R.K. Plemper</name></json:item><json:item><name>A. Hammond</name></json:item><json:item><name>R. Cattaneo</name></json:item></author><host><volume>74</volume><pages><last>6493</last><first>6485</first></pages><author></author><title>J. Virol.</title></host><title>Characterization of a region of measles virus hemagglutinin sufficient for its dimerization</title></json:item><json:item><author><json:item><name>J.K. Lee</name></json:item></author><host><volume>283</volume><pages><last>16572</last><first>16561</first></pages><author></author><title>J. Biol. Chem.</title></host><title>Functional interaction between paramyxovirus fusion and attachment proteins</title></json:item><json:item><author><json:item><name>M.A. Brindley</name></json:item><json:item><name>R.K. Plemper</name></json:item></author><host><volume>84</volume><pages><last>12184</last><first>12174</first></pages><author></author><title>J. Virol.</title></host><title>Blue native PAGE and biomolecular complementation reveal a tetrameric or higher-order oligomer organization of the physiological measles virus attachment protein H</title></json:item><json:item><author><json:item><name>R. Cattaneo</name></json:item><json:item><name>J.K. Rose</name></json:item></author><host><volume>67</volume><pages><last>1502</last><first>1493</first></pages><author></author><title>J. Virol.</title></host><title>Cell fusion by the envelope glycoproteins of persistent measles viruses which caused lethal human brain disease</title></json:item><json:item><author><json:item><name>X.L. Hu</name></json:item><json:item><name>R. Ray</name></json:item><json:item><name>R.W. Compans</name></json:item></author><host><volume>66</volume><pages><last>1534</last><first>1528</first></pages><author></author><title>J. Virol.</title></host><title>Functional interactions between the fusion protein and hemagglutinin-neuraminidase of human parainfluenza viruses</title></json:item><json:item><author><json:item><name>T. Paal</name></json:item></author><host><volume>83</volume><pages><last>10493</last><first>10480</first></pages><author></author><title>J. Virol.</title></host><title>Probing the spatial organization of measles virus fusion complexes</title></json:item><json:item><author><json:item><name>T. Hashiguchi</name></json:item></author><host><volume>104</volume><pages><last>19540</last><first>19535</first></pages><author></author><title>Proc. Natl. Acad. Sci. USA</title></host><title>Crystal structure of measles virus hemagglutinin provides insight into effective vaccines</title></json:item><json:item><author><json:item><name>S. Crennell</name></json:item><json:item><name>T. Takimoto</name></json:item><json:item><name>A. Portner</name></json:item><json:item><name>G. Taylor</name></json:item></author><host><volume>7</volume><pages><last>1074</last><first>1068</first></pages><author></author><title>Nat. Struct. Biol.</title></host><title>Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase</title></json:item><json:item><author><json:item><name>M.C. Lawrence</name></json:item></author><host><volume>335</volume><pages><last>1357</last><first>1343</first></pages><author></author><title>J. Mol. Biol.</title></host><title>Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III</title></json:item><json:item><author><json:item><name>P. Yuan</name></json:item></author><host><volume>13</volume><pages><last>815</last><first>803</first></pages><author></author><title>Structure</title></host><title>Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose</title></json:item><json:item><author><json:item><name>T.A. Bowden</name></json:item><json:item><name>M. Crispin</name></json:item><json:item><name>D. Harvey</name></json:item><json:item><name>E.Y. Jones</name></json:item><json:item><name>D. Stuard</name></json:item></author><host><volume>84</volume><pages><last>6217</last><first>6208</first></pages><author></author><title>J. Virol.</title></host><title>Dimeric architecture of the Hendra virus attachment glycoprotein: evidence for a conserved mode of assembly</title></json:item><json:item><author><json:item><name>L.A. Colf</name></json:item><json:item><name>Z.S. Juo</name></json:item><json:item><name>K.C. Garcia</name></json:item></author><host><volume>14</volume><pages><last>1228</last><first>1227</first></pages><author></author><title>Nat. Struct. Mol. Biol.</title></host><title>Structure of the measles virus hemagglutinin</title></json:item><json:item><author><json:item><name>R.K. Plemper</name></json:item><json:item><name>A.L. Hammond</name></json:item><json:item><name>R. Cattaneo</name></json:item></author><host><volume>276</volume><pages><last>44246</last><first>44239</first></pages><author></author><title>J. Biol. Chem.</title></host><title>Measles virus envelope glycoproteins hetero-oligomerize in the endoplasmic reticulum</title></json:item><json:item><author><json:item><name>S.A. Connolly</name></json:item><json:item><name>G.P. Leser</name></json:item><json:item><name>T.S. Jardetzky</name></json:item><json:item><name>R.A. Lamb</name></json:item></author><host><volume>83</volume><pages><last>10868</last><first>10857</first></pages><author></author><title>J. Virol.</title></host><title>Bimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: implications for the mechanism of fusion triggering</title></json:item><json:item><author><json:item><name>S. Vongpunsawad</name></json:item><json:item><name>N. Oezgun</name></json:item><json:item><name>W. Braun</name></json:item><json:item><name>R. Cattaneo</name></json:item></author><host><volume>78</volume><pages><last>313</last><first>302</first></pages><author></author><title>J. Virol.</title></host><title>Selectively receptor-blind measles viruses: identification of residues necessary for SLAM- or CD46-induced fusion and their localization on a new hemagglutinin structural model</title></json:item><json:item><author><json:item><name>N. Massé</name></json:item></author><host><volume>78</volume><pages><last>9063</last><first>9051</first></pages><author></author><title>J. Virol.</title></host><title>Measles virus (MV) hemagglutinin: evidence that attachment sites for MV receptors SLAM and CD46 overlap on the globular head</title></json:item><json:item><author><json:item><name>C.K. Navaratnarajah</name></json:item></author><host><volume>283</volume><pages><last>11771</last><first>11763</first></pages><author></author><title>J. Biol. Chem.</title></host><title>Dynamic interaction of the measles virus hemagglutinin with its receptor signaling lymphocytic activation molecule (SLAM, CD150)</title></json:item><json:item><author><json:item><name>V.H.J. Leonard</name></json:item></author><host><volume>118</volume><pages><last>2458</last><first>2448</first></pages><author></author><title>J. Clin. Invest.</title></host><title>Measles virus blind to its epithelial cell receptor remains virulent in rhesus monkeys but cannot cross the airway epithelium and is not shed</title></json:item><json:item><author><json:item><name>M. Tahara</name></json:item></author><host><volume>82</volume><pages><last>4637</last><first>4630</first></pages><author></author><title>J. Virol.</title></host><title>Measles virus infects both polarized epithelial and immune cells by using distinctive receptor-binding sites on its hemagglutinin</title></json:item><json:item><author><json:item><name>D. Naniche</name></json:item></author><host><volume>67</volume><pages><last>6032</last><first>6025</first></pages><author></author><title>J. Virol.</title></host><title>Human membrane cofactor protein (CD46) acts as a cellular receptor for measles virus</title></json:item><json:item><author><json:item><name>R.E. Dörig</name></json:item><json:item><name>A. Marcil</name></json:item><json:item><name>A. Chopra</name></json:item><json:item><name>C.D. Richardson</name></json:item></author><host><volume>75</volume><pages><last>305</last><first>295</first></pages><author></author><title>Cell</title></host><title>The human CD46 molecule is a receptor for measles virus (Edmonston strain)</title></json:item><json:item><author><json:item><name>H. Tatsuo</name></json:item><json:item><name>N. Ono</name></json:item><json:item><name>K. Tanaka</name></json:item><json:item><name>Y. Yanagi</name></json:item></author><host><volume>406</volume><pages><last>897</last><first>893</first></pages><author></author><title>Nature</title></host><title>SLAM (CDw150) is a cellular receptor for measles virus</title></json:item><json:item><author><json:item><name>N. Ono</name></json:item></author><host><volume>75</volume><pages><last>4401</last><first>4399</first></pages><author></author><title>J. Virol.</title></host><title>Measles viruses on throat swabs from measles patients use signaling lymphocytic activation molecule (CDw150) but not CD46 as a cellular receptor</title></json:item><json:item><author><json:item><name>C. Santiago</name></json:item><json:item><name>M.L. Celma</name></json:item><json:item><name>T. Stehle</name></json:item><json:item><name>J.M. Casasnovas</name></json:item></author><host><volume>17</volume><pages><last>129</last><first>124</first></pages><author></author><title>Nat. Struct. Mol. Biol.</title></host><title>Structure of the measles virus hemagglutinin bound to the CD46 receptor</title></json:item><json:item><author><json:item><name>K.C. El Kasmi</name></json:item></author><host><volume>81</volume><pages><last>735</last><first>729</first></pages><author></author><title>J. Gen. Virol.</title></host><title>Neutralization of measles virus wild-type isolates after immunization with a synthetic peptide vaccine which is not recognized by neutralizing passive antibodies</title></json:item><json:item><author><json:item><name>T. Nakamura</name></json:item></author><host><volume>23</volume><pages><last>214</last><first>209</first></pages><author></author><title>Nat. Biotechnol.</title></host><title>Rescue and propagation of fully retargeted oncolytic measles viruses</title></json:item><json:item><author><json:item><name>B.D. Persson</name></json:item></author><host><volume>6</volume><pages><first>1001122</first></pages><author></author><title>PLoS Pathog.</title></host><title>Structure of the extracellular portion of CD46 provides insights into its interactions with complement proteins and pathogens</title></json:item><json:item><author><json:item><name>P. Devaux</name></json:item></author><host><volume>71</volume><pages><last>4160</last><first>4157</first></pages><author></author><title>J. Virol.</title></host><title>CD46 short consensus repeats III and IV enhance measles virus binding but impair soluble hemagglutinin binding</title></json:item><json:item><author><json:item><name>J.M. Casasnovas</name></json:item><json:item><name>M. Larvie</name></json:item><json:item><name>T. Stehle</name></json:item></author><host><volume>18</volume><pages><last>2922</last><first>2911</first></pages><author></author><title>EMBO J.</title></host><title>Crystal structure of two CD46 domains reveals an extended measles virus-binding surface</title></json:item><json:item><author><json:item><name>P. Yuan</name></json:item><json:item><name>G.P. Leser</name></json:item><json:item><name>B. Demeler</name></json:item><json:item><name>R.A. Lamb</name></json:item><json:item><name>T.S. Jardetzky</name></json:item></author><host><volume>378</volume><pages><last>291</last><first>282</first></pages><author></author><title>Virology</title></host><title>Domain architecture and oligomerization properties of the paramyxovirus PIV 5 hemagglutinin-neuraminidase (HN) protein</title></json:item><json:item><author><json:item><name>C.J. Buchholz</name></json:item><json:item><name>U. Schneider</name></json:item><json:item><name>P. Devaux</name></json:item><json:item><name>D. Gerlier</name></json:item><json:item><name>R. Cattaneo</name></json:item></author><host><volume>70</volume><pages><last>3723</last><first>3716</first></pages><author></author><title>J. Virol.</title></host><title>Cell entry by measles virus: long hybrid receptors uncouple binding from membrane fusion</title></json:item><json:item><author><json:item><name>R. Chen</name></json:item><json:item><name>L. Li</name></json:item><json:item><name>Z. Weng</name></json:item></author><host><volume>52</volume><pages><last>87</last><first>80</first></pages><author></author><title>Proteins</title></host><title>ZDOCK: an initial-stage protein-docking algorithm</title></json:item><json:item><author><json:item><name>P.J. Mahon</name></json:item><json:item><name>A.M. Mirza</name></json:item><json:item><name>T.A. Musich</name></json:item><json:item><name>R.M. Iorio</name></json:item></author><host><volume>82</volume><pages><last>10396</last><first>10386</first></pages><author></author><title>J. Virol.</title></host><title>Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion</title></json:item><json:item><author><json:item><name>K. Ludwig</name></json:item></author><host><volume>82</volume><pages><last>3781</last><first>3775</first></pages><author></author><title>J. Virol.</title></host><title>Electron cryomicroscopy reveals different F1 + F2 protein states in intact parainfluenza virions</title></json:item><json:item><author><json:item><name>H.-S. Yin</name></json:item><json:item><name>X. Wen</name></json:item><json:item><name>R.G. Paterson</name></json:item><json:item><name>R.A. Lamb</name></json:item><json:item><name>T.S. Jardetzky</name></json:item></author><host><volume>439</volume><pages><last>44</last><first>38</first></pages><author></author><title>Nature</title></host><title>Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation</title></json:item><json:item><author><json:item><name>N. Ono</name></json:item><json:item><name>H. Tatsuo</name></json:item><json:item><name>K. Tanaka</name></json:item><json:item><name>H. Minagawa</name></json:item><json:item><name>Y. Yanagi</name></json:item></author><host><volume>75</volume><pages><last>1600</last><first>1594</first></pages><author></author><title>J. Virol.</title></host><title>V domain of human SLAM (CDw150) is essential for its function as a measles virus receptor</title></json:item><json:item><author><json:item><name>U.J. Buchholz</name></json:item><json:item><name>S. Finke</name></json:item><json:item><name>K.K. Conzelmann</name></json:item></author><host><volume>73</volume><pages><last>259</last><first>251</first></pages><author></author><title>J. Virol.</title></host><title>Generation of bovine respiratory syncytial virus (BRSV) from cDNA: BRSV NS2 is not essential for virus replication in tissue culture, and the human RSV leader region acts as a functional BRSV genome promoter</title></json:item><json:item><author><json:item><name>T. Cathomen</name></json:item><json:item><name>C.J. Buchholz</name></json:item><json:item><name>P. Spielhofer</name></json:item><json:item><name>R. Cattaneo</name></json:item></author><host><volume>214</volume><pages><last>632</last><first>628</first></pages><author></author><title>Virology</title></host><title>Preferential initiation at the second AUG of the measles virus F mRNA: a role for the long untranslated region</title></json:item><json:item><author><json:item><name>F. Radecke</name></json:item></author><host><volume>14</volume><pages><last>5784</last><first>5773</first></pages><author></author><title>EMBO J.</title></host><title>Rescue of measles viruses from cloned DNA</title></json:item><json:item><author><json:item><name>M. Takeda</name></json:item></author><host><volume>74</volume><pages><last>6647</last><first>6643</first></pages><author></author><title>J. Virol.</title></host><title>Recovery of pathogenic measles virus from cloned cDNA</title></json:item><json:item><author><json:item><name>R. Fraczkiewicz</name></json:item><json:item><name>W. Braun</name></json:item></author><host><volume>19</volume><pages><last>333</last><first>319</first></pages><author></author><title>J. Comput. Chem.</title></host><title>Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules</title></json:item><json:item><author><json:item><name>T. Cathomen</name></json:item><json:item><name>H.Y. Naim</name></json:item><json:item><name>R. Cattaneo</name></json:item></author><host><volume>72</volume><pages><last>1234</last><first>1224</first></pages><author></author><title>J. Virol.</title></host><title>Measles viruses with altered envelope protein cytoplasmic tails gain cell fusion competence</title></json:item></refBibs><genre><json:string>research-article</json:string></genre><host><volume>18</volume><pages><total>7</total><last>134</last><first>128</first></pages><issn><json:string>1545-9993</json:string></issn><issue>2</issue><subject><json:item><value>npg_subject_143</value></json:item><json:item><value>npg_subject_312</value></json:item></subject><genre><json:string>journal</json:string></genre><language><json:string>unknown</json:string></language><eissn><json:string>1545-9985</json:string></eissn><title>Nature Structural & Molecular Biology</title></host><categories><wos><json:string>science</json:string><json:string>cell biology</json:string><json:string>biophysics</json:string><json:string>biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>health sciences</json:string><json:string>biomedical research</json:string><json:string>developmental biology</json:string></scienceMetrix></categories><publicationDate>2011</publicationDate><copyrightDate>2011</copyrightDate><doi><json:string>10.1038/nsmb.1967</json:string></doi><id>B8D1DB0332D5C4763449D8B5A6A2D3821B0C9BEC</id><score>0.032538224</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/B8D1DB0332D5C4763449D8B5A6A2D3821B0C9BEC/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/B8D1DB0332D5C4763449D8B5A6A2D3821B0C9BEC/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/B8D1DB0332D5C4763449D8B5A6A2D3821B0C9BEC/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">The heads of the measles virus attachment protein move to transmit the fusion-triggering signal</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.</publisher><availability><p>©2011 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.</p></availability><date>2011</date></publicationStmt><notesStmt><note>Supplementary Text and Figures : Supplementary Tables 1 and 2 [nsmb.1967-S1]</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">The heads of the measles virus attachment protein move to transmit the fusion-triggering signal</title><author xml:id="author-1"><persName><forename type="first">Chanakha K</forename><surname>Navaratnarajah</surname></persName><affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</affiliation><affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</affiliation></author><author xml:id="author-2"><persName><forename type="first">Numan</forename><surname>Oezguen</surname></persName><affiliation>Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas, USA.</affiliation><affiliation>Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas, USA.</affiliation></author><author xml:id="author-3"><persName><forename type="first">Levi</forename><surname>Rupp</surname></persName><affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</affiliation><affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</affiliation></author><author xml:id="author-4"><persName><forename type="first">Leah</forename><surname>Kay</surname></persName><affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</affiliation><affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</affiliation></author><author xml:id="author-5"><persName><forename type="first">Vincent H J</forename><surname>Leonard</surname></persName><affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</affiliation><affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</affiliation></author><author xml:id="author-6"><persName><forename type="first">Werner</forename><surname>Braun</surname></persName><affiliation>Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas, USA.</affiliation><affiliation>Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas, USA.</affiliation></author><author xml:id="author-7"><persName><forename type="first">Roberto</forename><surname>Cattaneo</surname></persName><email>cattaneo.roberto@mayo.edu</email><affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</affiliation><affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</affiliation></author></analytic><monogr><title level="j">Nature Structural & Molecular Biology</title><idno type="pISSN">1545-9993</idno><idno type="eISSN">1545-9985</idno><imprint><publisher>Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.</publisher><date type="published" when="2011-02"></date><biblScope unit="volume">18</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="128">128</biblScope><biblScope unit="page" to="134">134</biblScope></imprint></monogr><idno type="istex">B8D1DB0332D5C4763449D8B5A6A2D3821B0C9BEC</idno><idno type="DOI">10.1038/nsmb.1967</idno><idno type="ArticleID">nsmb.1967</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>2011</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>The measles virus entry system, consisting of attachment (hemagglutinin, H) and fusion proteins, operates by means of a variety of natural and targeted receptors; however, the mechanism that triggers fusion of the viral envelope with the plasma membrane is not understood. Here, we tested a model proposing that the two heads of an H dimer, which are covalently linked at their base, after binding two receptor molecules, move relative to each other to transmit the fusion-triggering signal. Indeed, stabilizing the H-dimer interface with additional intermolecular disulfide bonds prevented membrane fusion, an effect that was reversed by a reducing agent. Moreover, a membrane-anchored designated receptor efficiently triggered fusion, provided that it engaged the H dimer at locations proximal to where the natural receptors bind and distal to the H-dimer interface. We discuss how receptors may force H-protein heads to switch partners and transmit the fusion-triggering signal.</p></abstract><abstract xml:lang="en" style="editorial-summary"><p>Binding of measles virus hemagglutinin (MVH) to its cellular receptors triggers the activation of the fusion protein. The conformational changes of MVH upon receptor binding are now examined by locking the dimers using disulfide bonds, or by pulling on appropriately positioned hexahistidine tags. The results indicate that the dimer interface is pulled apart after receptor binding by twisting of the MVH heads.</p></abstract><textClass><keywords scheme="Journal Subject"><list><head>category</head><item><term>npg_subject_143</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>category</head><item><term>npg_subject_312</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2010-06-16">Received</change><change when="2010-10-25">Registration</change><change when="2011-02">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/B8D1DB0332D5C4763449D8B5A6A2D3821B0C9BEC/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="corpus nature" wicri:toSee="no header"><istex:xmlDeclaration>version="1.0"</istex:xmlDeclaration><istex:docType PUBLIC="-//NPG//DTD XML Article//EN" URI="NPG_XML_Article.dtd" name="istex:docType"><istex:entity PUBLIC="-//NatureAmerica//FICI nsmb.1967-F1//EN" URL="nsmb.1967-F1" NDATA="ITEM" name="figf1"></istex:entity><istex:entity PUBLIC="-//NatureAmerica//FICI nsmb.1967-F2//EN" URL="nsmb.1967-F2" NDATA="ITEM" name="figf2"></istex:entity><istex:entity PUBLIC="-//NatureAmerica//FICI nsmb.1967-F3//EN" URL="nsmb.1967-F3" NDATA="ITEM" name="figf3"></istex:entity><istex:entity PUBLIC="-//NatureAmerica//FICI nsmb.1967-F4//EN" URL="nsmb.1967-F4" NDATA="ITEM" name="figf4"></istex:entity><istex:entity PUBLIC="-//NatureAmerica//FICI nsmb.1967-F5//EN" URL="nsmb.1967-F5" NDATA="ITEM" name="figf5"></istex:entity><istex:entity PUBLIC="-//NatureAmerica//FICI nsmb.1967-T1//EN" URL="nsmb.1967-T1" NDATA="ITEM" name="tbl1"></istex:entity></istex:docType><istex:document><article id="nsmb.1967" language="eng" relation="no"><pubfm><jtl>Nature Structural & Molecular Biology</jtl><vol>18</vol><iss>2</iss><idt>201102</idt><categ id="af"></categ><pp><spn>128</spn><epn>134</epn><cnt>7</cnt></pp><issn type="print">1545-9993</issn><issn type="electronic">1545-9985</issn><cpg><cpy>2011</cpy><cpn>Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.</cpn></cpg><nvid extrefid="nsmb0211-115"></nvid><suppinfo id="S1"><suppobj extrefid="nsmb.1967-S1" format="pdf" filesize="92K"><title>Supplementary Text and Figures</title><descrip><p>Supplementary Tables 1 and 2</p></descrip></suppobj></suppinfo><subject code="npg_subject_143"></subject><subject code="npg_subject_312"></subject><doi>10.1038/nsmb.1967</doi></pubfm><fm><atl>The heads of the measles virus attachment protein move to transmit the fusion-triggering signal</atl><aug><au><fnm>Chanakha K</fnm><snm>Navaratnarajah</snm><inits>C K</inits><orf rid="a1"></orf><orf rid="a2"></orf></au><au><fnm>Numan</fnm><snm>Oezguen</snm><inits>N</inits><orf rid="a3"></orf><orf rid="a4"></orf></au><au><fnm>Levi</fnm><snm>Rupp</snm><inits>L</inits><orf rid="a1"></orf><orf rid="a2"></orf></au><au><fnm>Leah</fnm><snm>Kay</snm><inits>L</inits><orf rid="a1"></orf><orf rid="a2"></orf></au><au><fnm>Vincent H J</fnm><snm>Leonard</snm><inits>V H J</inits><orf rid="a1"></orf><orf rid="a2"></orf></au><au><fnm>Werner</fnm><snm>Braun</snm><inits>W</inits><orf rid="a3"></orf><orf rid="a4"></orf></au><cau><fnm>Roberto</fnm><snm>Cattaneo</snm><inits>R</inits><orf rid="a1"></orf><orf rid="a2"></orf><corf rid="c1"></corf></cau><aff><oid id="a1"></oid><org>Department of Molecular Medicine, Mayo Clinic</org>, <cty>Rochester</cty>, <st>Minnesota</st>, <cny>USA</cny>.</aff><aff><oid id="a2"></oid><org>Virology and Gene Therapy Track, Mayo Graduate School</org>, <cty>Rochester</cty>, <st>Minnesota</st>, <cny>USA</cny>.</aff><aff><oid id="a3"></oid><org>Department of Biochemistry and Molecular Biology, University of Texas Medical Branch</org>, <cty>Galveston</cty>, <st>Texas</st>, <cny>USA</cny>.</aff><aff><oid id="a4"></oid><org>Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch</org>, <cty>Galveston</cty>, <st>Texas</st>, <cny>USA</cny>.</aff><caff><coid id="c1"></coid><email>cattaneo.roberto@mayo.edu</email></caff></aug><hst><re year="2010" month="06" day="16"></re><acc year="2010" month="10" day="25"></acc><pubdate type="aop" year="2011" month="01" day="09"></pubdate></hst><edsumm type="standfirst" publish="aop"><title></title><p>Binding of measles virus hemagglutinin (MVH) to its cellular receptors triggers the activation of the fusion protein. The conformational changes of MVH upon receptor binding are now examined by locking the dimers using disulfide bonds, or by pulling on appropriately positioned hexahistidine tags. The results indicate that the dimer interface is pulled apart after receptor binding by twisting of the MVH heads.</p></edsumm><edsumm type="standfirst" publish="issue"><title></title><p>Binding of measles virus hemagglutinin (MVH) to its cellular receptors triggers the activation of the fusion protein. The conformational changes of MVH upon receptor binding are now examined by locking the dimers using disulfide bonds, or by pulling on appropriately positioned hexahistidine tags. The results indicate that the dimer interface is pulled apart after receptor binding by twisting of the MVH heads.</p></edsumm><abs><p>The measles virus entry system, consisting of attachment (<named-entity id="named-entity-1">hemagglutinin</named-entity>, <named-entity id="named-entity-2">H</named-entity>) and fusion proteins, operates by means of a variety of natural and targeted receptors; however, the mechanism that triggers fusion of the viral envelope with the plasma membrane is not understood. Here, we tested a model proposing that the two heads of an <named-entity id="named-entity-3">H</named-entity> dimer, which are covalently linked at their base, after binding two receptor molecules, move relative to each other to transmit the fusion-triggering signal. Indeed, stabilizing the <named-entity id="named-entity-4">H</named-entity>-dimer interface with additional intermolecular disulfide bonds prevented membrane fusion, an effect that was reversed by a reducing agent. Moreover, a membrane-anchored designated receptor efficiently triggered fusion, provided that it engaged the <named-entity id="named-entity-5">H</named-entity> dimer at locations proximal to where the natural receptors bind and distal to the <named-entity id="named-entity-6">H</named-entity>-dimer interface. We discuss how receptors may force <named-entity id="named-entity-7">H-protein</named-entity> heads to switch partners and transmit the fusion-triggering signal.</p></abs></fm></article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="eng"><title>The heads of the measles virus attachment protein move to transmit the fusion-triggering signal</title></titleInfo><titleInfo type="alternative" lang="eng" contentType="CDATA"><title>The heads of the measles virus attachment protein move to transmit the fusion-triggering signal</title></titleInfo><name type="personal"><namePart type="given">Chanakha K</namePart><namePart type="family">Navaratnarajah</namePart><affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</affiliation><affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Numan</namePart><namePart type="family">Oezguen</namePart><affiliation>Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas, USA.</affiliation><affiliation>Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Levi</namePart><namePart type="family">Rupp</namePart><affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</affiliation><affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Leah</namePart><namePart type="family">Kay</namePart><affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</affiliation><affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Vincent H J</namePart><namePart type="family">Leonard</namePart><affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</affiliation><affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Werner</namePart><namePart type="family">Braun</namePart><affiliation>Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas, USA.</affiliation><affiliation>Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Roberto</namePart><namePart type="family">Cattaneo</namePart><affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</affiliation><affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</affiliation><affiliation>E-mail: cattaneo.roberto@mayo.edu</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Article"></genre><originInfo><publisher>Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.</publisher><dateIssued encoding="w3cdtf">2011-02</dateIssued><dateCaptured encoding="w3cdtf">2010-06-16</dateCaptured><dateValid encoding="w3cdtf">2010-10-25</dateValid><copyrightDate encoding="w3cdtf">2011</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="eng">The measles virus entry system, consisting of attachment (hemagglutinin, H) and fusion proteins, operates by means of a variety of natural and targeted receptors; however, the mechanism that triggers fusion of the viral envelope with the plasma membrane is not understood. Here, we tested a model proposing that the two heads of an H dimer, which are covalently linked at their base, after binding two receptor molecules, move relative to each other to transmit the fusion-triggering signal. Indeed, stabilizing the H-dimer interface with additional intermolecular disulfide bonds prevented membrane fusion, an effect that was reversed by a reducing agent. Moreover, a membrane-anchored designated receptor efficiently triggered fusion, provided that it engaged the H dimer at locations proximal to where the natural receptors bind and distal to the H-dimer interface. We discuss how receptors may force H-protein heads to switch partners and transmit the fusion-triggering signal.</abstract><abstract type="editorial-summary" lang="eng">Binding of measles virus hemagglutinin (MVH) to its cellular receptors triggers the activation of the fusion protein. The conformational changes of MVH upon receptor binding are now examined by locking the dimers using disulfide bonds, or by pulling on appropriately positioned hexahistidine tags. The results indicate that the dimer interface is pulled apart after receptor binding by twisting of the MVH heads.</abstract><note type="additional-physical-form">Supplementary Text and Figures : Supplementary Tables 1 and 2 [nsmb.1967-S1]</note><relatedItem type="host"><titleInfo><title>Nature Structural & Molecular Biology</title></titleInfo><genre type="journal" displayLabel="journal"></genre><subject displayLabel="npg_subject_143"><genre>category</genre><topic>npg_subject_143</topic></subject><subject displayLabel="npg_subject_312"><genre>category</genre><topic>npg_subject_312</topic></subject><identifier type="ISSN">1545-9993</identifier><identifier type="eISSN">1545-9985</identifier><part><date>2011</date><detail type="volume"><caption>vol.</caption><number>18</number></detail><detail type="issue"><caption>no.</caption><number>2</number></detail><extent unit="pages"><start>128</start><end>134</end><total>7</total></extent></part></relatedItem><identifier type="istex">B8D1DB0332D5C4763449D8B5A6A2D3821B0C9BEC</identifier><identifier type="DOI">10.1038/nsmb.1967</identifier><identifier type="ArticleID">nsmb.1967</identifier><accessCondition type="use and reproduction" contentType="copyright">©2011 Nature Publishing Group, a division of Macmillan Publishers Limited. 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