About: The three lives of viral fusion peptides

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	The three lives of viral fusion peptides
Creator	Huarte, Nerea Nieva, José Apellániz, Beatriz Largo, Eneko
source	Elsevier; Medline; PMC
abstract	Fusion peptides comprise conserved hydrophobic domains absolutely required for the fusogenic activity of glycoproteins from divergent virus families. After 30 years of intensive research efforts, the structures and functions underlying their high degree of sequence conservation are not fully elucidated. The long-hydrophobic viral fusion peptide (VFP) sequences are structurally constrained to access three successive states after biogenesis. Firstly, the VFP sequence must fulfill the set of native interactions required for (meta) stable folding within the globular ectodomains of glycoprotein complexes. Secondly, at the onset of the fusion process, they get transferred into the target cell membrane and adopt specific conformations therein. According to commonly accepted mechanistic models, membrane-bound states of the VFP might promote the lipid bilayer remodeling required for virus-cell membrane merger. Finally, at least in some instances, several VFPs co-assemble with transmembrane anchors into membrane integral helical bundles, following a locking movement hypothetically coupled to fusion-pore expansion. Here we review different aspects of the three major states of the VFPs, including the functional assistance by other membrane-transferring glycoprotein regions, and discuss briefly their potential as targets for clinical intervention.
has issue date	2014-07-01(xsd:dateTime)
bibo:doi	10.1016/j.chemphyslip.2014.03.003
bibo:pmid	24704587
has license	green-oa
sha1sum (hex)	62ea1b52436f5020dfa97ac7f381c697cb291054
schema:url	https://doi.org/10.1016/j.chemphyslip.2014.03.003
resource representing a document's title	The three lives of viral fusion peptides
has PubMed Central identifier	PMC4061400
has PubMed identifier	24704587
schema:publication	Chemistry and Physics of Lipids
resource representing a document's body	covid:62ea1b52436f5020dfa97ac7f381c697cb291054#body_text
is schema:about of	named entity 'VFP' named entity 'VIRAL' named entity 'YEARS' named entity 'MAJOR' named entity 'CONSTRAINED' named entity 'FULFILL' named entity 'HIGH' named entity 'PROMOTE' named entity 'STRUCTURES' named entity 'ACCEPTED' named entity 'INTERACTIONS' named entity 'PORE' named entity 'FUNCTIONAL' named entity 'FULLY' named entity 'COUPLED' named entity 'PROCESS' named entity 'REVIEW' named entity 'HERE' named entity 'CLINICAL INTERVENTION' named entity 'VIRUS' named entity 'GLYCOPROTEIN' named entity 'FUSION PEPTIDE' named entity 'STABLE' named entity 'MOVEMENT' named entity 'NATIVE' named entity 'FOLDING' named entity 'LOCKING' named entity 'TRANSMEMBRANE' named entity 'DEGREE' named entity 'ANCHORS' named entity 'LIPID BILAYER' named entity 'CONSERVED' named entity 'ONSET OF' named entity 'MODELS' named entity 'SEQUENCES' named entity 'FAMILIES' named entity 'THEIR' named entity 'RESEARCH' named entity 'FUNCTIONS' named entity 'ACCESS' named entity 'DISCUSS' named entity 'FUSION' named entity 'STATES' named entity 'SUCCESSIVE' named entity 'LIVES' named entity 'BIOGENESIS' named entity 'GLYCOPROTEINS' named entity 'ADOPT' named entity 'INCLUDING' named entity 'INTEGRAL' named entity 'HELICAL' named entity 'ASSISTANCE' named entity 'GLOBULAR' named entity 'ACCORDING' named entity 'REMODELING' named entity 'SET' named entity 'BOUND' named entity 'UNDERLYING' named entity 'LONG' named entity 'HYDROPHOBIC' named entity 'SECONDLY' named entity 'VIRAL' named entity 'PEPTIDES' named entity 'FUSION' named entity 'CELL MEMBRANE' named entity 'SPECIFIC' named entity 'TRANSFERRING' named entity 'TRANSFERRED' named entity 'REQUIRED' named entity 'COMPLEXES' named entity 'MEMBRANE' named entity 'SEQUENCE' named entity 'FIRSTLY' named entity 'POTENTIAL' named entity 'DIFFERENT' named entity 'FOLLOWING' named entity 'REGIONS' named entity 'CONSERVATION'

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