Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy
Identifieur interne : 000788 ( Main/Exploration ); précédent : 000787; suivant : 000789Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy
Auteurs : Alexandra Walls [États-Unis] ; M Alejandra Tortorici [France] ; Brandon Frenz [États-Unis] ; Joost Snijder [États-Unis] ; Wentao Li [Pays-Bas] ; Félix A. Rey [France] ; Frank Dimaio [États-Unis] ; Berend-Jan Bosch [Pays-Bas] ; David Veesler [États-Unis]Source :
- Nature Structural and Molecular Biology [ 1545-9993 ] ; 2016-10.
Descripteurs français
- Wicri :
- topic : Immunologie.
English descriptors
Abstract
The threat of a major coronavirus pandemic urges the development of strategies to combat these pathogens. Human coronavirus NL63 (HCoV-NL63) is an α-coronavirus that can cause severe lower-respiratory-tract infections requiring hospitalization. We report here the 3.4-Å-resolution cryo-EM reconstruction of the HCoV-NL63 coronavirus spike glycoprotein trimer, which mediates entry into host cells and is the main target of neutralizing antibodies during infection. The map resolves the extensive glycan shield obstructing the protein surface and, in combination with mass spectrometry, provides a structural framework to understand the accessibility to antibodies. The structure reveals the complete architecture of the fusion machinery including the triggering loop and the C-terminal domains, which contribute to anchoring the trimer to the viral membrane. Our data further suggest that HCoV-NL63 and other coronaviruses use molecular trickery, based on epitope masking with glycans and activating conformational changes, to evade the immune system of infected hosts.
Url:
DOI: 10.1038/nsmb.3293
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Hal, to step Corpus: 000263
- to stream Hal, to step Curation: 000263
- to stream Hal, to step Checkpoint: 000318
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- to stream Main, to step Curation: 000788
Le document en format XML
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<tutelles><tutelle active="#struct-300433" type="direct"><org type="institution" xml:id="struct-300433" status="VALID"> <orgName>University of Washington [Seattle]</orgName>
<desc> <address> <addrLine>Seattle, Washington 98105</addrLine>
<country key="US"></country>
</address>
<ref type="url">http://www.washington.edu/</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>États-Unis</country>
</affiliation>
</author>
</analytic>
<idno type="DOI">10.1038/nsmb.3293</idno>
<series><title level="j">Nature Structural and Molecular Biology</title>
<idno type="ISSN">1545-9993</idno>
<imprint><date type="datePub">2016-10</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="mix" xml:lang="en"><term>Cryoelectron microscopy</term>
<term>Glycoproteins</term>
<term>Immunology</term>
<term>Viral membrane fusion</term>
</keywords>
<keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Immunologie</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"> <p>The threat of a major coronavirus pandemic urges the development of strategies to combat these pathogens. Human coronavirus NL63 (HCoV-NL63) is an α-coronavirus that can cause severe lower-respiratory-tract infections requiring hospitalization. We report here the 3.4-Å-resolution cryo-EM reconstruction of the HCoV-NL63 coronavirus spike glycoprotein trimer, which mediates entry into host cells and is the main target of neutralizing antibodies during infection. The map resolves the extensive glycan shield obstructing the protein surface and, in combination with mass spectrometry, provides a structural framework to understand the accessibility to antibodies. The structure reveals the complete architecture of the fusion machinery including the triggering loop and the C-terminal domains, which contribute to anchoring the trimer to the viral membrane. Our data further suggest that HCoV-NL63 and other coronaviruses use molecular trickery, based on epitope masking with glycans and activating conformational changes, to evade the immune system of infected hosts.</p>
</div>
</front>
</TEI>
<affiliations><list><country><li>France</li>
<li>Pays-Bas</li>
<li>États-Unis</li>
</country>
</list>
<tree><country name="États-Unis"><noRegion><name sortKey="Walls, Alexandra" sort="Walls, Alexandra" uniqKey="Walls A" first="Alexandra" last="Walls">Alexandra Walls</name>
</noRegion>
<name sortKey="Dimaio, Frank" sort="Dimaio, Frank" uniqKey="Dimaio F" first="Frank" last="Dimaio">Frank Dimaio</name>
<name sortKey="Frenz, Brandon" sort="Frenz, Brandon" uniqKey="Frenz B" first="Brandon" last="Frenz">Brandon Frenz</name>
<name sortKey="Snijder, Joost" sort="Snijder, Joost" uniqKey="Snijder J" first="Joost" last="Snijder">Joost Snijder</name>
<name sortKey="Veesler, David" sort="Veesler, David" uniqKey="Veesler D" first="David" last="Veesler">David Veesler</name>
</country>
<country name="France"><noRegion><name sortKey="Tortorici, M Alejandra" sort="Tortorici, M Alejandra" uniqKey="Tortorici M" first="M Alejandra" last="Tortorici">M Alejandra Tortorici</name>
</noRegion>
<name sortKey="Rey, Felix A" sort="Rey, Felix A" uniqKey="Rey F" first="Félix A." last="Rey">Félix A. Rey</name>
</country>
<country name="Pays-Bas"><noRegion><name sortKey="Li, Wentao" sort="Li, Wentao" uniqKey="Li W" first="Wentao" last="Li">Wentao Li</name>
</noRegion>
<name sortKey="Bosch, Berend Jan" sort="Bosch, Berend Jan" uniqKey="Bosch B" first="Berend-Jan" last="Bosch">Berend-Jan Bosch</name>
</country>
</tree>
</affiliations>
</record>
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