ArticleBiochimica et biophysica acta2015
NMR structures and localization of the potential fusion peptides and the pre-transmembrane region of SARS-CoV: Implications in membrane fusion.
Article in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 42 citations in OpenAlex.
- Article
- Resurrection of the Helical Hairpin Hypothesis for Understanding Coronavirus Fusion.The Journal of membrane biology · 2025Review
- A spike-based mRNA vaccine that induces durable and broad protection against porcine deltacoronavirus in piglets.Journal of virology · 2024Article
- Inconspicuous Yet Indispensable: The Coronavirus Spike Transmembrane Domain.International journal of molecular sciences · 2023Review
- A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization.Biomolecules · 2023Review
- Blood pH Analysis in Combination with Molecular Medical Tools in Relation to COVID-19 Symptoms.Biomedicines · 2023Article
- Role of cholesterol-recognition motifs in the infectivity of SARS-CoV-2 variants.Colloids and surfaces. B, Biointerfaces · 2023Article
- A Uniquely Stable Trimeric Model of SARS-CoV-2 Spike Transmembrane Domain.International journal of molecular sciences · 2022Article
- A Stochastic SEIRS Epidemic Model with Infection Forces and Intervention Strategies.Journal of healthcare engineering · 2022Article
- Membranotropic and biological activities of the membrane fusion peptides from SARS-CoV spike glycoprotein: The importance of the complete internal fusion peptide domain.Biochimica et biophysica acta. Biomembranes · 2021Article
- Transient lipid-bound states of spike protein heptad repeats provide insights into SARS-CoV-2 membrane fusion.Science advances · 2021Article
- 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
- Lipidomics Issues on Human Positive ssRNA Virus Infection: An Update.Metabolites · 2020Review
- A comprehensive overview of proteomics approach for COVID 19: new perspectives in target therapy strategies.Journal of proteins and proteomics · 2020Review
- Membrane Composition Modulates Fusion by Altering Membrane Properties and Fusion Peptide Structure.The Journal of membrane biology · 2019Review
- Membranotropic peptides mediating viral entry.Peptide science (Hoboken, N.J.) · 2018Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) poses a serious public health hazard. The S2 subunit of the S glycoprotein of SARS-CoV carries out fusion between the virus and the host cells. However, the exact mechanism of the cell fusion process is not well understood. Current model suggests that a conformational transition, upon receptor recognition, of the two heptad core regions of S2 may expose the hydrophobic fusogenic peptide or fusion peptide for membrane insertion. Three regions of the S2 subunit have been proposed to be involved in cell-cell fusion. The N-terminal fusion peptide (FP, residues 770-788), an internal fusion peptide (IFP, residues 873-888) and the pre-transmembrane region (PTM, residues 1185-1202) demonstrated interactions with model lipid membranes and potentially involved in the fusion process. Here, we have determined atomic resolution structures of these three peptides in DPC detergent micelles by solution NMR. FP assumes α-helical conformation with significant distortion at the central Gly residues; enabling a close packing among sidechains of aromatic residues including W, Y and F. The 3-D structure of PMT is characterized by a helix-loop-helix with extensive aromatic interactions within the helices. IFP adopts a rather straight α-helical conformation defined by packing among sidechains of aromatic and aliphatic residues. Paramagnetic spin labeled NMR has demonstrated surface localization of PMT whereas FP and IFP inserted into the micelles. Collectively, data presented in this study will aid in understanding fusion mechanism of SARS-CoV.
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