PandemieGrippaleV1, Hal, Curation, bibRecord, 000263

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

Identifieur interne : 000263 ( Hal/Curation ); précédent : 000262; suivant : 000264

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

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Hal:pasteur-01664348

Le document en format XML

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<profileDesc><textClass><keywords scheme="mix" xml:lang="en"><term>Cryoelectron microscopy</term>
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<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>
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<hal api="V3">          <titleStmt>            <title xml:lang="en">Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy</title>
            <author role="aut">              <persName>                <forename type="first">Alexandra</forename>
                <surname>Walls</surname>
              </persName>
              <idno type="halauthorid">1699541</idno>
              <affiliation ref="#struct-101259"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">M Alejandra</forename>
                <surname>Tortorici</surname>
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              <email type="md5">11e6d44f23b73947615ccf6cfa01505b</email>
              <email type="domain">pasteur.fr</email>
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            <author role="aut">              <persName>                <forename type="first">Brandon</forename>
                <surname>Frenz</surname>
              </persName>
              <idno type="halauthorid">1699543</idno>
              <affiliation ref="#struct-101259"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Joost</forename>
                <surname>Snijder</surname>
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              <idno type="halauthorid">1699545</idno>
              <affiliation ref="#struct-101259"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Wentao</forename>
                <surname>Li</surname>
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              <idno type="halauthorid">1699546</idno>
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            <author role="aut">              <persName>                <forename type="first">Félix A.</forename>
                <surname>Rey</surname>
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              <email type="md5">6b02472e652ac98383b25b6666310ddd</email>
              <email type="domain">pasteur.fr</email>
              <idno type="halauthorid">404280</idno>
              <affiliation ref="#struct-232693"></affiliation>
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            <author role="aut">              <persName>                <forename type="first">Frank</forename>
                <surname>DiMaio</surname>
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              <idno type="halauthorid">1668161</idno>
              <affiliation ref="#struct-101259"></affiliation>
            </author>
            <author role="crp">              <persName>                <forename type="first">Berend-Jan</forename>
                <surname>Bosch</surname>
              </persName>
              <email type="md5">2f2f96891f61a54928a16fbd7ca81da6</email>
              <email type="domain">uu.nl</email>
              <idno type="halauthorid">1699866</idno>
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            <author role="crp">              <persName>                <forename type="first">David</forename>
                <surname>Veesler</surname>
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              <email type="md5">a69250bae7cd738d65dbee08ff3c8649</email>
              <email type="domain">uw.edu</email>
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            <editor role="depositor">              <persName>                <forename>M. Alejandra</forename>
                <surname>Tortorici</surname>
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              <email type="md5">11e6d44f23b73947615ccf6cfa01505b</email>
              <email type="domain">pasteur.fr</email>
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            <funder>Research reported in this publication was supported by the National Institute of General Medical Sciences (NIGMS) of the National Institutes of Health (NIH) under award number 1R01GM120553-01 (D.V.) and T32GM008268 (A.C.W.). J.S. acknowledges support from the Netherlands Organization for Scientific Research (NWO, Rubicon 019.2015.2.310.006) and the European Molecular Biology Organisation (EMBO, ALTF 933-2015). M.A.T. and F.A.R. acknowledge support from the Institute Pasteur and the CNRS. The authors acknowledge the use of instruments at the Electron Imaging Center for NanoMachines supported by the NIH (1S10RR23057 and 1S10OD018111), NSF (DBI-1338135) and CNSI at UCLA. The authors are grateful to H. Choe (The Scripps Research Institute) for providing the HCoV-NL63 S gene, J. Labonte (Johns Hopkins School of Medicine) for providing the Rosetta code handling glycans and P.J.M. Rottier (Utrecht University) for scientific advice. This work was partly supported by the University of Washington's Proteomics Resource (UWPR95794), and the authors thank P.D. von Haller and J.K. Eng for their assistance and expertise. SPR experiments were performed with the help of J. Sumida at the University of Washington School of Pharmacy Analytical Biopharmacy Core. Part of this research was facilitated by the Hyak supercomputer system at the University of Washington.</funder>
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                <imprint>                  <publisher>Nature Publishing Group</publisher>
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                  <biblScope unit="issue">10</biblScope>
                  <biblScope unit="pp">899 - 905</biblScope>
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              <classCode scheme="mesh">Animals</classCode>
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              <classCode scheme="mesh">Polysaccharides</classCode>
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            <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>
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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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