About: SARS-CoV fusion peptides induce membrane surface ordering and curvature

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About: SARS-CoV fusion peptides induce membrane surface ordering and curvature Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	SARS-CoV fusion peptides induce membrane surface ordering and curvature
Creator	Crusca, Edson Basso, Luis Cilli, Eduardo Costa-Filho, Antonio Vicente, Eduardo
source	Medline; PMC
abstract	Viral membrane fusion is an orchestrated process triggered by membrane-anchored viral fusion glycoproteins. The S2 subunit of the spike glycoprotein from severe acute respiratory syndrome (SARS) coronavirus (CoV) contains internal domains called fusion peptides (FP) that play essential roles in virus entry. Although membrane fusion has been broadly studied, there are still major gaps in the molecular details of lipid rearrangements in the bilayer during fusion peptide-membrane interactions. Here we employed differential scanning calorimetry (DSC) and electron spin resonance (ESR) to gather information on the membrane fusion mechanism promoted by two putative SARS FPs. DSC data showed the peptides strongly perturb the structural integrity of anionic vesicles and support the hypothesis that the peptides generate opposing curvature stresses on phosphatidylethanolamine membranes. ESR showed that both FPs increase lipid packing and head group ordering as well as reduce the intramembrane water content for anionic membranes. Therefore, bending moment in the bilayer could be generated, promoting negative curvature. The significance of the ordering effect, membrane dehydration, changes in the curvature properties and the possible role of negatively charged phospholipids in helping to overcome the high kinetic barrier involved in the different stages of the SARS-CoV-mediated membrane fusion are discussed.
has issue date	2016-11-28(xsd:dateTime)
bibo:doi	10.1038/srep37131
bibo:pmid	27892522
has license	cc-by
sha1sum (hex)	ddfd6e95ebc735146d0f0d6ea7faacaf99d9613c
schema:url	https://doi.org/10.1038/srep37131
resource representing a document's title	SARS-CoV fusion peptides induce membrane surface ordering and curvature
has PubMed Central identifier	PMC5125003
has PubMed identifier	27892522
schema:publication	Sci Rep
resource representing a document's body	covid:ddfd6e95ebc735146d0f0d6ea7faacaf99d9613c#body_text
is schema:about of	named entity 'interactions' named entity 'peptides' named entity 'group' named entity 'support' named entity 'OPEN' covid:arg/ddfd6e95ebc735146d0f0d6ea7faacaf99d9613c named entity 'membrane fusion' named entity 'differential scanning calorimetry' named entity 'domains' named entity 'bending moment' named entity 'anionic' named entity 'fusion' named entity 'peptides' named entity 'severe acute respiratory syndrome (SARS)' named entity 'fusion peptide' named entity 'membrane fusion' named entity 'severe acute respiratory syndrome' named entity 'kinetic barrier' named entity 'bending moment' named entity 'SARS' named entity 'peptides' named entity 'peptides' named entity 'phosphatidylethanolamine' named entity 'membrane fusion' named entity 'coronavirus' named entity 'ESR' named entity 'order parameter' named entity 'SARS' named entity 'spin labels' named entity 'PCSL' named entity 'physicochemical properties' named entity 'lipids' named entity 'Peptide' named entity 'head group' named entity 'spin label' named entity 'head group' named entity 'peptide' named entity 'peptides' named entity 'lipid' named entity 'hydroxyl' named entity 'zwitterionic' named entity 'DPPC' named entity 'computational studies' named entity 'peptide' named entity 'SARS' named entity 'acetylated' named entity 'membrane fusion' named entity 'helical' named entity 'peptide' named entity 'electron' named entity 'fusion pore' named entity 'POPA' named entity 'endothermic' named entity 'fluorescence' named entity 'vesicles' named entity 'sonicator' named entity 'peptide' named entity 'choline' named entity 'membrane fusion' named entity 'POPA' named entity 'palmitoyl' named entity 'Data analysis' named entity 'head group' named entity 'SARS' named entity 'correlation' named entity 'water density' named entity 'vesicles' named entity 'trimethyl' named entity '20:1' named entity 'moiety' named entity 'hydrophobic core' named entity 'lipids' named entity 'spectral density' named entity 'peptides' named entity 'spin label' named entity 'National Instruments' named entity 'distal'

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