Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion.
Animals
Antibodies, Monoclonal
/ immunology
Antibodies, Neutralizing
/ immunology
Antibodies, Viral
/ immunology
Chlorocebus aethiops
Coronavirus
/ immunology
Coronavirus Infections
/ immunology
HEK293 Cells
Humans
Immunity, Humoral
/ immunology
Middle East Respiratory Syndrome Coronavirus
/ immunology
Molecular Mimicry
/ immunology
Protein Binding
Receptors, Virus
/ metabolism
Severe acute respiratory syndrome-related coronavirus
/ immunology
Spike Glycoprotein, Coronavirus
/ metabolism
Vero Cells
Virus Internalization
MERS-CoV
N-linked glycosylation
SARS-CoV
class I fusion protein
coronavirus
glycoproteomics
membrane fusion
neutralizing antibodies
spike glycoprotein
Journal
Cell
ISSN: 1097-4172
Titre abrégé: Cell
Pays: United States
ID NLM: 0413066
Informations de publication
Date de publication:
21 02 2019
21 02 2019
Historique:
received:
19
07
2018
revised:
29
10
2018
accepted:
17
12
2018
pubmed:
5
2
2019
medline:
7
1
2020
entrez:
5
2
2019
Statut:
ppublish
Résumé
Recent outbreaks of severe acute respiratory syndrome and Middle East respiratory syndrome, along with the threat of a future coronavirus-mediated pandemic, underscore the importance of finding ways to combat these viruses. The trimeric spike transmembrane glycoprotein S mediates entry into host cells and is the major target of neutralizing antibodies. To understand the humoral immune response elicited upon natural infections with coronaviruses, we structurally characterized the SARS-CoV and MERS-CoV S glycoproteins in complex with neutralizing antibodies isolated from human survivors. Although the two antibodies studied blocked attachment to the host cell receptor, only the anti-SARS-CoV S antibody triggered fusogenic conformational changes via receptor functional mimicry. These results provide a structural framework for understanding coronavirus neutralization by human antibodies and shed light on activation of coronavirus membrane fusion, which takes place through a receptor-driven ratcheting mechanism.
Identifiants
pubmed: 30712865
pii: S0092-8674(18)31642-8
doi: 10.1016/j.cell.2018.12.028
pmc: PMC6751136
mid: NIHMS1041755
pii:
doi:
Substances chimiques
Antibodies, Monoclonal
0
Antibodies, Neutralizing
0
Antibodies, Viral
0
Receptors, Virus
0
Spike Glycoprotein, Coronavirus
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1026-1039.e15Subventions
Organisme : NIAID NIH HHS
ID : HHSN272201700059C
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM120553
Pays : United States
Organisme : NIH HHS
ID : S10 OD021832
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM008268
Pays : United States
Commentaires et corrections
Type : ErratumIn
Informations de copyright
Copyright © 2018 Elsevier Inc. All rights reserved.
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