Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 23, Issue 10, Pages 899-905Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3293
Keywords
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Funding
- National Institute of General Medical Sciences (NIGMS) of the National Institutes of Health (NIH) [1R01GM120553-01, T32GM008268]
- Netherlands Organization for Scientific Research (NWO) [Rubicon 019.2015.2.310.006]
- European Molecular Biology Organisation (EMBO) [ALTF 933-2015]
- Institute Pasteur
- CNRS
- NIH [1S10RR23057, 1S10OD018111]
- NSF [DBI-1338135]
- CNSI at UCLA
- University of Washington's Proteomics Resource [UWPR95794]
- Direct For Biological Sciences [1338135] Funding Source: National Science Foundation
- Div Of Biological Infrastructure [1338135] Funding Source: National Science Foundation
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The threat of a major coronavirus pandemic urges the development of strategies to combat these pathogens. Human coronavirus NL63 (HCoV-NL63) is an a-coronavirus that can cause severe lower-respiratory-tract infections requiring hospitalization. We report here the 3.4-A-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.
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