The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy
Open accessAbstract
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.
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Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC
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Self-citationIsolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor
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Self-citationStructure of RSV Fusion Glycoprotein Trimer Bound to a Prefusion-Specific Neutralizing Antibody
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Pre-fusion structure of a human coronavirus spike protein
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Cited by
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Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein
Walls, A. C., Park, Y.-J., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020) · doi:10.1101/2020.02.19.956581 · Cited by 8,586
Self-citationCoronavirus biology and replication: implications for SARS-CoV-2
V’kovski, P., Kratzel, A., Steiner, S., Stalder, H., & Thiel, V. (2021) · Nature Reviews Microbiology · doi:10.1038/s41579-020-00468-6 · Cited by 3,197
Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2349-y · Cited by 1,885
Self-citationStructural and functional analysis of a potent sarbecovirus neutralizing antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · doi:10.1101/2020.04.07.023903 · Cited by 1,752
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Metadata
- Authors
- Walls, A. C., Tortorici, M. A., Frenz, B., Snijder, J., Li, W., Rey, F. A., DiMaio, F., Bosch, B.-J., & Veesler, D.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2016-09-12
- Volume
- 23
- Issue
- 10
- Pages
- 899-905
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2520033800
- Cited by
- 412
- References
- 8
- FWCI
- 19.32
- Type
- journal article
- Language
- en
- Open access
- bronze
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