PandemieGrippaleV1, France, Analysis, bibRecord, 000307

Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy

Identifieur interne : 000307 ( France/Analysis ); précédent : 000306; suivant : 000308

Glycan 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.

RBID : Hal:pasteur-01664348

Descripteurs français

Wicri :
- topic : Immunologie.

English descriptors

mix :
- Cryoelectron microscopy, Glycoproteins, Immunology, Viral membrane fusion.

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:

https://hal-pasteur.archives-ouvertes.fr/pasteur-01664348

DOI: 10.1038/nsmb.3293

Affiliations:

France, Pays-Bas, États-Unis

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
to stream Main, to step Merge: 000790
to stream Main, to step Curation: 000788
to stream Main, to step Exploration: 000788
to stream France, to step Extraction: 000307

Links to Exploration step

Hal:pasteur-01664348

Le document en format XML

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          </desc>
        </org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>États-Unis</country>
</affiliation>
</author>
<author><name sortKey="Bosch, Berend Jan" sort="Bosch, Berend Jan" uniqKey="Bosch B" first="Berend-Jan" last="Bosch">Berend-Jan Bosch</name>
<affiliation wicri:level="1"><hal:affiliation type="institution" xml:id="struct-300572" status="VALID">          <orgName>Utrecht University [Utrecht]</orgName>
          <desc>            <address>              <addrLine>Heidelberglaan 8, 3584 CS Utrecht</addrLine>
              <country key="NL"></country>
            </address>
            <ref type="url">http://www.uu.nl/en</ref>
          </desc>
        </hal:affiliation>
<country>Pays-Bas</country>
</affiliation>
</author>
<author><name sortKey="Veesler, David" sort="Veesler, David" uniqKey="Veesler D" first="David" last="Veesler">David Veesler</name>
<affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-101259" status="VALID">          <orgName>Department of Biochemistry [Washington ]</orgName>
          <desc>            <address>              <addrLine>Campus Box 351700 Seattle, Washington 98195</addrLine>
              <country key="US"></country>
            </address>
            <ref type="url">http://depts.washington.edu/biowww/</ref>
          </desc>
          <listRelation>            <relation active="#struct-300433" type="direct"></relation>
          </listRelation>
        <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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Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy

Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy

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