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.
Url:
DOI: 10.1038/nsmb.1967
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<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>
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<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>
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<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>
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<istex:document><article id="nsmb.1967" language="eng" relation="no"><pubfm><jtl>Nature Structural & Molecular Biology</jtl>
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<doi>10.1038/nsmb.1967</doi>
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<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>
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<au><fnm>Leah</fnm>
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<au><fnm>Vincent H J</fnm>
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<cau><fnm>Roberto</fnm>
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<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>
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<hst><re year="2010" month="06" day="16"></re>
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<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>
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<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>
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<titleInfo type="alternative" lang="eng" contentType="CDATA"><title>The heads of the measles virus attachment protein move to transmit the fusion-triggering signal</title>
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<name type="personal"><namePart type="given">Chanakha K</namePart>
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<affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</affiliation>
<affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</affiliation>
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<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>
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<name type="personal"><namePart type="given">Levi</namePart>
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<affiliation>Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.</affiliation>
<affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</affiliation>
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<name type="personal"><namePart type="given">Leah</namePart>
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<affiliation>Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.</affiliation>
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<name type="personal"><namePart type="given">Vincent H J</namePart>
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<affiliation>Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas, USA.</affiliation>
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<name type="personal"><namePart type="given">Roberto</namePart>
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<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>
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