ArticleScience advances2021
Transient lipid-bound states of spike protein heptad repeats provide insights into SARS-CoV-2 membrane fusion.
Article in Science advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Insights into the self-assembly and interaction of sars-cov-2 fusion peptides with biomimetic plasma membranes.Nature communications · 2025Article
- Efficiency enhancement in main path extraction in mRNA vaccine field: A novel approach leveraging intermediate patents, with shielding origin and terminus patent edges.Human vaccines & immunotherapeutics · 2025Article
- Hydrophobic residues in the D-domain of a plasminogen-binding M-protein modulate α-helicity, oligomerization, and surface anchoring in Streptococcus pyogenes.Protein science : a publication of the Protein Society · 2025Article
- Article
- Probing Biomolecular Interactions with Paramagnetic Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2025Review
- SARS-CoV-2 spike fusion peptidemBio · 2024Article
- S2 Peptide-Conjugated SARS-CoV-2 Virus-like Particles Provide Broad Protection against SARS-CoV-2 Variants of Concern.Vaccines · 2024Article
- Representing structures of the multiple conformational states of proteins.Current opinion in structural biology · 2023Review
- Inconspicuous Yet Indispensable: The Coronavirus Spike Transmembrane Domain.International journal of molecular sciences · 2023Review
- N4-hydroxycytidine, the active compound of Molnupiravir, promotes SARS-CoV-2 mutagenesis and escape from a neutralizing nanobody.iScience · 2023Article
- SARS-CoV-2 fusion peptide sculpting of a membrane with insertion of charged and polar groups.Structure (London, England : 1993) · 2023Article
- A Suitable Membrane Distance Regulated by the RBD_ACE2 Interaction is Critical for SARS-CoV-2 Spike-Mediated Viral Invasion.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- SARS-CoV-2 omicron variants harbor spike protein mutations responsible for their attenuated fusogenic phenotype.Communications biology · 2023Article
- High-throughput identification of prefusion-stabilizing mutations in SARS-CoV-2 spike.Nature communications · 2023Article
- SARS-CoV-2 spike protein as a bacterial lipopolysaccharide delivery system in an overzealous inflammatory cascade.Journal of molecular cell biology · 2023Article
- Toxin-like Peptides from the Bacterial Cultures Derived from Gut Microbiome Infected by SARS-CoV-2-New Data for a Possible Role in the Long COVID Pattern.Biomedicines · 2022Article
- Exploring Highly Conserved Regions of SARS-CoV-2 Spike S2 Subunit as Targets for Fusion Inhibition Using Chimeric Proteins.International journal of molecular sciences · 2022Article
- A variant-proof SARS-CoV-2 vaccine targeting HR1 domain in S2 subunit of spike protein.Cell research · 2022Article
- Synthesis and structure-activity relationship study of saponin-based membrane fusion inhibitors against SARS-CoV-2.Bioorganic chemistry · 2022Article
- High-throughput identification of prefusion-stabilizing mutations in SARS-CoV-2 spike.bioRxiv : the preprint server for biology · 2022Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Entry of SARS-CoV-2 into a host cell is mediated by spike, a class I viral fusion protein responsible for merging the viral and host cell membranes. Recent studies have revealed atomic-resolution models for both the postfusion 6-helix bundle (6HB) and the prefusion state of spike. However, a mechanistic understanding of the molecular basis for the intervening structural transition, important for the design of fusion inhibitors, has remained elusive. Using nuclear magnetic resonance spectroscopy and other biophysical methods, we demonstrate the presence of α-helical, membrane-bound, intermediate states of spike’s heptad repeat (HR1 and HR2) domains that are embedded at the lipid-water interface while in a slow dynamic equilibrium with the postfusion 6HB state. These results support a model where the HR domains lower the large energy barrier associated with membrane fusion by destabilizing the host and viral membranes, while 6HB formation actively drives their fusion by forcing physical proximity.
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