Binding mode of SARS-CoV-2 fusion peptide to human cellular membrane.
TLDR
In this article, the authors used an array of molecular dynamics simulations that take advantage of the highly mobile membrane mimetic model to investigate the interaction of the SARS-CoV2 FP with a lipid bilayer representing mammalian cellular membranes at an atomic level and to characterize the membrane-bound form of the peptide.About:
This article is published in Biophysical Journal.The article was published on 2021-03-04 and is currently open access. It has received 28 citations till now. The article focuses on the topics: Host cell membrane & Lipid bilayer fusion.read more
Citations
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Ca2+-dependent mechanism of membrane insertion and destabilization by the SARS-CoV-2 fusion peptide.
TL;DR: In this article, the authors predicted the preferred positions of Ca2+ binding to the SARS-CoV-2-FP, the role of ca2+ ions in mediating peptide-membrane interactions, and the preferred mode of insertion of the Ca2-bound SARS CoV2-2FP, and consequent effects on the lipid bilayer from extensive atomistic molecular dynamics simulations and trajectory analyses.
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Could metabolomics drive the fate of COVID-19 pandemic? A narrative review on lights and shadows.
Michele Mussap,Vassilios Fanos +1 more
TL;DR: In this paper, a limited number of metabolomics-and lipidomics-based clinical studies in COVID-19 patients have been published and are discussed in this review, where remarkable alterations in the lipid and amino acid metabolism depict the molecular phenotype of subjects infected by SARS-CoV-2.
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Binding of SARS-CoV-2 Fusion Peptide to Host Endosome and Plasma Membrane.
TL;DR: In this paper, the SARS-CoV-2 virus fuses its viral envelope with cellular membranes of its human host and forms an anchor strong enough to withstand the mechanical force during membrane fusion.
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Sterically confined rearrangements of SARS-CoV-2 Spike protein control cell invasion.
TL;DR: In this paper, an all-atom model with simplified energetics was used to perform thousands of simulations in which the protein transitions between the prefusion and post-fusion conformations.
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COVID-19 and Neurodegenerative Diseases: Prion-Like Spread and Long-Term Consequences.
TL;DR: It is hypothesized that people with neurodegenerative diseases, Parkinson's disease, and aged people are at higher risk of getting the COVID-19 than normal adults and that the risk of having the infection increases with dementia and that infected people with severe symptoms could develop dementia as a long-term consequence.
References
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SARS-CoV fusion peptides induce membrane surface ordering and curvature.
TL;DR: Differential scanning calorimetry and electron spin resonance data showed that both FPs increase lipid packing and head group ordering as well as reduce the intramembrane water content for anionic membranes, suggesting bending moment in the bilayer could be generated, promoting negative curvature.
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SARS-coronavirus spike S2 domain flanked by cysteine residues C822 and C833 is important for activation of membrane fusion.
TL;DR: It is proposed that the conserved domain flanked by cysteines 822 and 833 forms a loop structure that interacts with components of the SARS-CoV S trimer to control the activation of membrane fusion.
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Conformational Reorganization of the SARS Coronavirus Spike Following Receptor Binding: Implications for Membrane Fusion
Daniel R. Beniac,Shauna L. deVarennes,Anton Andonov,Anton Andonov,Runtao He,Runtao He,Timothy F. Booth,Timothy F. Booth +7 more
TL;DR: This study has produced purified, irradiated SARS-CoV virions that retain their morphology, and are fusogenic in cell culture, and precisely localized the receptor-binding and fusion core domains within the entire spike.
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Structural characterizations of fusion peptide analogs of influenza virus hemagglutinin. Implication of the necessity of a helix-hinge-helix motif in fusion activity.
TL;DR: A model is proposed that illustrates the structural change of the HA2 fusion peptide analog and explains how the analog interacts with the lipid bilayer at different pH values.
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Partitioning of amino acids into a model membrane: capturing the interface.
TL;DR: The free energy profiles for partitioning of 10 protein side chain analogues into a HMMM membrane show excellent agreement with profiles previously reported for conventional membranes with full-tail lipids.