About: Infectivity inhibition by overlapping synthetic peptides derived from the gH/gL heterodimer of herpes simplex virus type 1

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About: Infectivity inhibition by overlapping synthetic peptides derived from the gH/gL heterodimer of herpes simplex virus type 1 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
has title	Infectivity inhibition by overlapping synthetic peptides derived from the gH/gL heterodimer of herpes simplex virus type 1
Creator	Annarita, Falanga Carla, Zannella Francesca, Martora Giancarlo, Morelli Gianluigi, Franci Marilena, Galdiero Massimiliano, Galdiero Stefania, Galdiero Veronica, Folliero
Source	Medline; PMC
abstract	Herpes simplex virus (HSV) is a human pathogen that infects epithelial cells. The cutaneous lesions, caused by the virus, spread to the nervous system creating several complications. Fusion of host membranes with the viral envelope is mandatory and mediated by a group of glycoproteins conserved in all Herpesviridae subfamilies, such as the glycoproteins B (gB), H (gH), L (gL) and D (gD). We investigated the inhibitory activity mediated by synthetic overlapping peptides spanning the entire ectodomains of gH and gL glycoproteins. We have performed a brute analysis of the complete gH/gL heterodimer in order to explore the inhibitory activity of peptides modelled on these glycoproteins against HSV‐1 infection. Twenty‐four of the gH peptides at a concentration of 150 μM reached the 50% of inhibition cut‐off. Interestingly, they are mainly located in the gH carboxy‐terminal domain. None of the gL peptides had a clear inhibiting effect. No peptide toxicity was observed by lactate dehydrogenase assay at the concentrations used in our experimental conditions. HSV‐1 therapy is based on acyclovir treatment, but some resistant strains are emerging. In this scenario, innovative approaches for HSV‐1 treatment are necessary. Our data support the direct involvement of the described domains in the process of virus penetration; therefore, these results are of relevance to the potential development of novel therapeutic compounds to prevent HSV‐1 infections. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.
has issue date	2017-02-14(xsd:dateTime)
bibo:doi	10.1002/psc.2979
bibo:pmid	28194842
has license	no-cc
sha1sum (hex)	8e9ec593501eb947b603fe7fa6272e036b3b6f87
schema:url	https://doi.org/10.1002/psc.2979
resource representing a document's title	Infectivity inhibition by overlapping synthetic peptides derived from the gH/gL heterodimer of herpes simplex virus type 1
has PubMed Central identifier	PMC7168125
has PubMed identifier	28194842
schema:publication	J Pept Sci
resource representing a document's body	covid:8e9ec593501eb947b603fe7fa6272e036b3b6f87#body_text
is schema:about of	named entity 'involvement' named entity 'HSV-1 infection' named entity 'compounds' named entity 'synthetic' named entity 'subfamilies' named entity 'inhibitory' named entity 'based' named entity 'virus' named entity 'concentrations' named entity 'derived' named entity 'domains' named entity 'concentration' named entity 'viral envelope' named entity 'support' named entity 'None' named entity 'virus' named entity 'Herpesviridae' named entity 'strains' named entity 'inhibition' named entity 'HSV-1' named entity 'peptide' named entity 'assay' named entity 'epithelial cells' named entity 'peptides' named entity 'cut-off' named entity 'peptides' named entity 'heterodimer' named entity 'glycoproteins' named entity 'virus' named entity 'virus' named entity 'human pathogen' named entity 'peptides' named entity 'carboxy-terminal domain' named entity 'herpes simplex virus type 1' named entity 'heterodimer' named entity 'peptides' named entity 'nectin' named entity 'peptides' named entity 'fusion inhibitor' named entity 'X-gal' named entity 'peptides' named entity 'heterodimer' named entity 'Fmoc' named entity 'peptides' named entity 'protein' named entity 'Varicella-Zoster virus' named entity 'peptides' named entity 'cell fusion' named entity 'ectodomain' named entity 'interact' named entity 'fusion proteins' named entity 'cytosol' named entity 'thioanisole' named entity 'glycoprotein' named entity 'brain infection' named entity 'synthetic peptides' named entity 'peptides' named entity 'entry inhibitors' named entity 'peptides' named entity 'secondary structure' named entity 'DMEM' named entity 'peptides' named entity 'antiviral' named entity 'isoelectric point' named entity 'antiviral' named entity 'sequence homology' named entity 'viral fusion proteins' named entity 'infectivity' named entity 'lacZ' named entity 'H97' named entity 'C-terminal' named entity 'P-value' named entity 'hepatitis C virus'

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