ArticleBiochimica et biophysica acta. Biomembranes2018
NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion.
Article in Biochimica et biophysica acta. Biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Resurrection of the Helical Hairpin Hypothesis for Understanding Coronavirus Fusion.The Journal of membrane biology · 2025Review
- A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization.Biomolecules · 2023Review
- Role of cholesterol-recognition motifs in the infectivity of SARS-CoV-2 variants.Colloids and surfaces. B, Biointerfaces · 2023Article
- Full-Length Computational Model of the SARS-CoV-2 Spike Protein and Its Implications for a Viral Membrane Fusion Mechanism.Viruses · 2021Article
- Computational insights into the membrane fusion mechanism of SARS-CoV-2 at the cellular level.Computational and structural biotechnology journal · 2021Article
- Exploring novel and potent cell penetrating peptides in the proteome of SARS-COV-2 using bioinformatics approaches.PloS one · 2021Article
- Host-membrane interacting interface of the SARS coronavirus envelope protein: Immense functional potential of C-terminal domain.Biophysical chemistry · 2020Review
- Mechanistic insights of host cell fusion of SARS-CoV-1 and SARS-CoV-2 from atomic resolution structure and membrane dynamics.Biophysical chemistry · 2020Review
- Analysis of clinical features and outcomes of 161 patients with severe and critical COVID-19: A multicenter descriptive study.Journal of clinical laboratory analysis · 2020Article
- Structure determination of UL49.5 transmembrane protein from bovine herpesvirus 1 by NMR spectroscopy and molecular dynamics.Biochimica et biophysica acta. Biomembranes · 2019Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lethal Coronaviruses (CoVs), Severe Acute Respiratory Syndrome-associated Coronavirus (SARS-CoV) and most recently Middle East Respiratory Syndrome Coronavirus, (MERS-CoV) are serious human health hazard. A successful viral infection requires fusion between virus and host cells carried out by the surface spike glycoprotein or S protein of CoV. Current models propose that the S2 subunit of S protein assembled into a hexameric helical bundle exposing hydrophobic fusogenic peptides or fusion peptides (FPs) for membrane insertion. The N-terminus of S2 subunit of SARS-CoV reported to be active in cell fusion whereby FPs have been identified. Atomic-resolution structure of FPs derived either in model membranes or in membrane mimic environment would glean insights toward viral cell fusion mechanism. Here, we have solved 3D structure, dynamics and micelle localization of a 64-residue long fusion peptide or LFP in DPC detergent micelles by NMR methods. Micelle bound structure of LFP is elucidated by the presence of discretely folded helical and intervening loops. The C-terminus region, residues F42-Y62, displays a long hydrophobic helix, whereas the N-terminus is defined by a short amphipathic helix, residues R4-Q12. The intervening residues of LFP assume stretches of loops and helical turns. The N-terminal helix is sustained by close aromatic and aliphatic sidechain packing interactions at the non-polar face.
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