Structure of a flavivirus envelope glycoprotein in its low‐pH‐induced membrane fusion conformation
Identifieur interne : 000216 ( France/Analysis ); précédent : 000215; suivant : 000217Structure of a flavivirus envelope glycoprotein in its low‐pH‐induced membrane fusion conformation
Auteurs : Stéphane Bressanelli [France, Autriche] ; Karin Stiasny [Autriche] ; Steven L. Allison [Autriche] ; Enrico A. Stura [France] ; Stéphane Duquerroy [France] ; Julien Lescar [France] ; Franz X. Heinz [Autriche] ; Félix A. Rey [France, Autriche]Source :
- The EMBO Journal [ 0261-4189 ] ; 2004-02-25.
English descriptors
- Teeft :
- Acta crystallogr, Additional functions, Adjacent subunit, Alphavirus, Amino, Amino acids, Avivirus, Avivirus envelope glycoprotein, Aviviruses, Bilayer, Biology organization, Biology organization structure, Bottom sheet, Bressanelli, Cell biol, Color coding, Conformation, Conformational, Conformational change, Conformational rearrangement, Contact area, Dengue, Dengue virus, Diffraction data, Diii, Dimer, Dimer interface, Ectodomain, Embo, Embo journal, Encephalitis, Encephalitis virus, Fusion, Fusion peptide, Fusion peptide loop, Fusion peptide loops, Fusion protein, Fusion proteins, Gibbon, Glycoprotein, Heinz, Helix, Hemifusion, Hydrogen bonds, Insertion, Interface, Kielian, Kuhn, Linker, Lipid, Lipid bilayer, Lipid heads, Liposome, Lower panel, Main chain, Membrane, Membrane fusion, Membrane fusion reaction, Molecular replacement, Open conformation, Peptide, Polypeptide, Polypeptide chain, Postfusion, Postfusion form, Rearrangement, Relative orientation, Residue, Ribbon diagram, Semliki forest virus, Side chains, Side view, Stiasny, Structural alignment, Subunit, Target membrane, Tbev, Trimer, Trimer contacts, Trimeric, Trimeric conformation, Trimeric form, Vertical axis, Viral, Viral membrane, Viral surface, Virion, Virol, Zhang.
Abstract
Enveloped viruses enter cells via a membrane fusion reaction driven by conformational changes of specific viral envelope proteins. We report here the structure of the ectodomain of the tick‐borne encephalitis virus envelope glycoprotein, E, a prototypical class II fusion protein, in its trimeric low‐pH‐induced conformation. We show that, in the conformational transition, the three domains of the neutral‐pH form are maintained but their relative orientation is altered. Similar to the postfusion class I proteins, the subunits rearrange such that the fusion peptide loops cluster at one end of an elongated molecule and the C‐terminal segments, connecting to the viral transmembrane region, run along the sides of the trimer pointing toward the fusion peptide loops. Comparison with the low‐pH‐induced form of the alphavirus class II fusion protein reveals striking differences at the end of the molecule bearing the fusion peptides, suggesting an important conformational effect of the missing membrane connecting segment.
Url:
DOI: 10.1038/sj.emboj.7600064
Affiliations:
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Rey</name><affiliation wicri:level="1"><country xml:lang="fr">France</country><wicri:regionArea>Virologie Moléculaire & Structurale, CNRS UMR 2472/INRA UMR 1157, IFR 115, Gif‐sur‐Yvette</wicri:regionArea><wicri:noRegion>Gif‐sur‐Yvette</wicri:noRegion><wicri:noRegion>Gif‐sur‐Yvette</wicri:noRegion></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Autriche</country></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">The EMBO Journal</title><title level="j" type="alt">THE EMBO JOURNAL</title><idno type="ISSN">0261-4189</idno><idno type="eISSN">1460-2075</idno><imprint><biblScope unit="vol">23</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="728">728</biblScope><biblScope unit="page" to="738">738</biblScope><biblScope unit="page-count">11</biblScope><publisher>John Wiley & Sons, Ltd</publisher><pubPlace>Chichester, UK</pubPlace><date type="published" when="2004-02-25">2004-02-25</date></imprint><idno type="ISSN">0261-4189</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0261-4189</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acta crystallogr</term><term>Additional functions</term><term>Adjacent subunit</term><term>Alphavirus</term><term>Amino</term><term>Amino acids</term><term>Avivirus</term><term>Avivirus envelope glycoprotein</term><term>Aviviruses</term><term>Bilayer</term><term>Biology organization</term><term>Biology organization structure</term><term>Bottom sheet</term><term>Bressanelli</term><term>Cell biol</term><term>Color coding</term><term>Conformation</term><term>Conformational</term><term>Conformational change</term><term>Conformational rearrangement</term><term>Contact area</term><term>Dengue</term><term>Dengue virus</term><term>Diffraction data</term><term>Diii</term><term>Dimer</term><term>Dimer interface</term><term>Ectodomain</term><term>Embo</term><term>Embo journal</term><term>Encephalitis</term><term>Encephalitis virus</term><term>Fusion</term><term>Fusion peptide</term><term>Fusion peptide loop</term><term>Fusion peptide loops</term><term>Fusion protein</term><term>Fusion proteins</term><term>Gibbon</term><term>Glycoprotein</term><term>Heinz</term><term>Helix</term><term>Hemifusion</term><term>Hydrogen bonds</term><term>Insertion</term><term>Interface</term><term>Kielian</term><term>Kuhn</term><term>Linker</term><term>Lipid</term><term>Lipid bilayer</term><term>Lipid heads</term><term>Liposome</term><term>Lower panel</term><term>Main chain</term><term>Membrane</term><term>Membrane fusion</term><term>Membrane fusion reaction</term><term>Molecular replacement</term><term>Open conformation</term><term>Peptide</term><term>Polypeptide</term><term>Polypeptide chain</term><term>Postfusion</term><term>Postfusion form</term><term>Rearrangement</term><term>Relative orientation</term><term>Residue</term><term>Ribbon diagram</term><term>Semliki forest virus</term><term>Side chains</term><term>Side view</term><term>Stiasny</term><term>Structural alignment</term><term>Subunit</term><term>Target membrane</term><term>Tbev</term><term>Trimer</term><term>Trimer contacts</term><term>Trimeric</term><term>Trimeric conformation</term><term>Trimeric form</term><term>Vertical axis</term><term>Viral</term><term>Viral membrane</term><term>Viral surface</term><term>Virion</term><term>Virol</term><term>Zhang</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract">Enveloped viruses enter cells via a membrane fusion reaction driven by conformational changes of specific viral envelope proteins. We report here the structure of the ectodomain of the tick‐borne encephalitis virus envelope glycoprotein, E, a prototypical class II fusion protein, in its trimeric low‐pH‐induced conformation. We show that, in the conformational transition, the three domains of the neutral‐pH form are maintained but their relative orientation is altered. Similar to the postfusion class I proteins, the subunits rearrange such that the fusion peptide loops cluster at one end of an elongated molecule and the C‐terminal segments, connecting to the viral transmembrane region, run along the sides of the trimer pointing toward the fusion peptide loops. Comparison with the low‐pH‐induced form of the alphavirus class II fusion protein reveals striking differences at the end of the molecule bearing the fusion peptides, suggesting an important conformational effect of the missing membrane connecting segment.</div></front></TEI><affiliations><list><country><li>Autriche</li><li>France</li></country><region><li>Vienne (Autriche)</li></region><settlement><li>Vienne (Autriche)</li></settlement></list><tree><country name="France"><noRegion><name sortKey="Bressanelli, Stephane" sort="Bressanelli, Stephane" uniqKey="Bressanelli S" first="Stéphane" last="Bressanelli">Stéphane Bressanelli</name></noRegion><name sortKey="Duquerroy, Stephane" sort="Duquerroy, Stephane" uniqKey="Duquerroy S" first="Stéphane" last="Duquerroy">Stéphane Duquerroy</name><name sortKey="Lescar, Julien" sort="Lescar, Julien" uniqKey="Lescar J" first="Julien" last="Lescar">Julien Lescar</name><name sortKey="Rey, Felix A" sort="Rey, Felix A" uniqKey="Rey F" first="Félix A" last="Rey">Félix A. Rey</name><name sortKey="Stura, Enrico A" sort="Stura, Enrico A" uniqKey="Stura E" first="Enrico A" last="Stura">Enrico A. Stura</name></country><country name="Autriche"><region name="Vienne (Autriche)"><name sortKey="Bressanelli, Stephane" sort="Bressanelli, Stephane" uniqKey="Bressanelli S" first="Stéphane" last="Bressanelli">Stéphane Bressanelli</name></region><name sortKey="Allison, Steven L" sort="Allison, Steven L" uniqKey="Allison S" first="Steven L" last="Allison">Steven L. Allison</name><name sortKey="Heinz, Franz X" sort="Heinz, Franz X" uniqKey="Heinz F" first="Franz X" last="Heinz">Franz X. Heinz</name><name sortKey="Heinz, Franz X" sort="Heinz, Franz X" uniqKey="Heinz F" first="Franz X" last="Heinz">Franz X. Heinz</name><name sortKey="Rey, Felix A" sort="Rey, Felix A" uniqKey="Rey F" first="Félix A" last="Rey">Félix A. Rey</name><name sortKey="Stiasny, Karin" sort="Stiasny, Karin" uniqKey="Stiasny K" first="Karin" last="Stiasny">Karin Stiasny</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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