About: Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides

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About: Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides Goto Sponge NotDistinct Permalink

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

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides
Creator	Horvat, Branka Mathieu, Cyrille Niewiesk, Stefan Augusto, Marcelo Palermo, Laura
source	PMC
abstract	Human paramyxoviruses include global causes of lower respiratory disease like the parainfluenza viruses, as well as agents of lethal encephalitis like Nipah virus. Infection is initiated by viral glycoprotein-mediated fusion between viral and host cell membranes. Paramyxovirus viral fusion proteins (F) insert into the target cell membrane, and form a transient intermediate that pulls the viral and cell membranes together as two heptad-repeat regions refold to form a six-helix bundle structure that can be specifically targeted by fusion-inhibitory peptides. Antiviral potency can be improved by sequence modification and lipid conjugation, and by adding linkers between the protein and lipid components. We exploit the uniquely broad spectrum antiviral activity of a parainfluenza F-derived peptide sequence that inhibits both parainfluenza and Nipah viruses, to investigate the influence of peptide orientation and intervening linker length on the peptides’ interaction with transitional states of F, solubility, membrane insertion kinetics, and protease sensitivity. We assessed the impact of these features on biodistribution and antiviral efficacy in vitro and in vivo. The engineering approach based on biophysical parameters resulted in a peptide that is a highly effective inhibitor of both paramyxoviruses and a set of criteria to be used for engineering broad spectrum antivirals for emerging paramyxoviruses.
has issue date	2017-03-08(xsd:dateTime)
bibo:doi	10.1038/srep43610
bibo:pmid	28344321
has license	cc-by
sha1sum (hex)	4800117f48b3a425e71f4271d450a1c07536765a
schema:url	https://doi.org/10.1038/srep43610
resource representing a document's title	Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides
has PubMed Central identifier	PMC5361215
has PubMed identifier	28344321
schema:publication	Sci Rep
resource representing a document's body	covid:4800117f48b3a425e71f4271d450a1c07536765a#body_text
is schema:about of	named entity 'TRANSITIONAL' named entity 'INSERTION' named entity 'THESE' named entity 'PEPTIDE SEQUENCE' named entity 'PARAINFLUENZA' »more»

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