Single-Molecule FRET Imaging of Virus Spike-Host Interactions.
Förster resonance energy transfer (FRET)
HIV-1
SARS-CoV-2
conformational dynamics
influenza and Ebola
single-molecule imaging
spike proteins
viral membrane fusion
virus entry
virus–host interactions
Journal
Viruses
ISSN: 1999-4915
Titre abrégé: Viruses
Pays: Switzerland
ID NLM: 101509722
Informations de publication
Date de publication:
21 02 2021
21 02 2021
Historique:
received:
31
01
2021
revised:
18
02
2021
accepted:
18
02
2021
entrez:
6
3
2021
pubmed:
7
3
2021
medline:
18
3
2021
Statut:
epublish
Résumé
As a major surface glycoprotein of enveloped viruses, the virus spike protein is a primary target for vaccines and anti-viral treatments. Current vaccines aiming at controlling the COVID-19 pandemic are mostly directed against the SARS-CoV-2 spike protein. To promote virus entry and facilitate immune evasion, spikes must be dynamic. Interactions with host receptors and coreceptors trigger a cascade of conformational changes/structural rearrangements in spikes, which bring virus and host membranes in proximity for membrane fusion required for virus entry. Spike-mediated viral membrane fusion is a dynamic, multi-step process, and understanding the structure-function-dynamics paradigm of virus spikes is essential to elucidate viral membrane fusion, with the ultimate goal of interventions. However, our understanding of this process primarily relies on individual structural snapshots of endpoints. How these endpoints are connected in a time-resolved manner, and the order and frequency of conformational events underlying virus entry, remain largely elusive. Single-molecule Förster resonance energy transfer (smFRET) has provided a powerful platform to connect structure-function in motion, revealing dynamic aspects of spikes for several viruses: SARS-CoV-2, HIV-1, influenza, and Ebola. This review focuses on how smFRET imaging has advanced our understanding of virus spikes' dynamic nature, receptor-binding events, and mechanism of antibody neutralization, thereby informing therapeutic interventions.
Identifiants
pubmed: 33669922
pii: v13020332
doi: 10.3390/v13020332
pmc: PMC7924862
pii:
doi:
Substances chimiques
Antibodies, Neutralizing
0
Antibodies, Viral
0
Receptors, Virus
0
Spike Glycoprotein, Coronavirus
0
spike protein, SARS-CoV-2
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : amfAR, The Foundation for AIDS Research
ID : 109998-67-RKVA
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