About: A Fusion-Inhibiting Peptide against Rift Valley Fever Virus Inhibits Multiple, Diverse Viruses

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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	A Fusion-Inhibiting Peptide against Rift Valley Fever Virus Inhibits Multiple, Diverse Viruses
Creator	Schmaljohn, Connie Wallqvist, Anders Grant, Rebecca Garry, Robert Badger, Catherine Guttieri, Mary Koehler, Jeffrey Ogg, Monica Ripoll, Daniel Smith, Jeffrey Spik, Kristin Taylor, Shannon
source	Medline; PMC
abstract	For enveloped viruses, fusion of the viral envelope with a cellular membrane is critical for a productive infection to occur. This fusion process is mediated by at least three classes of fusion proteins (Class I, II, and III) based on the protein sequence and structure. For Rift Valley fever virus (RVFV), the glycoprotein Gc (Class II fusion protein) mediates this fusion event following entry into the endocytic pathway, allowing the viral genome access to the cell cytoplasm. Here, we show that peptides analogous to the RVFV Gc stem region inhibited RVFV infectivity in cell culture by inhibiting the fusion process. Further, we show that infectivity can be inhibited for diverse, unrelated RNA viruses that have Class I (Ebola virus), Class II (Andes virus), or Class III (vesicular stomatitis virus) fusion proteins using this single peptide. Our findings are consistent with an inhibition mechanism similar to that proposed for stem peptide fusion inhibitors of dengue virus in which the RVFV inhibitory peptide first binds to both the virion and cell membranes, allowing it to traffic with the virus into the endocytic pathway. Upon acidification and rearrangement of Gc, the peptide is then able to specifically bind to Gc and prevent fusion of the viral and endocytic membranes, thus inhibiting viral infection. These results could provide novel insights into conserved features among the three classes of viral fusion proteins and offer direction for the future development of broadly active fusion inhibitors.
has issue date	2013-09-12(xsd:dateTime)
bibo:doi	10.1371/journal.pntd.0002430
bibo:pmid	24069485
has license	cc0
sha1sum (hex)	04cf308cfa2f72131ecbb07bacb894bab15aa66e
schema:url	https://doi.org/10.1371/journal.pntd.0002430
resource representing a document's title	A Fusion-Inhibiting Peptide against Rift Valley Fever Virus Inhibits Multiple, Diverse Viruses
has PubMed Central identifier	PMC3772029
has PubMed identifier	24069485
schema:publication	PLoS Negl Trop Dis
resource representing a document's body	covid:04cf308cfa2f72131ecbb07bacb894bab15aa66e#body_text
is schema:about of	named entity 'fusion proteins' named entity 'cell membranes' named entity 'sequence' named entity 'genome' named entity 'protein' named entity 'RIFT VALLEY FEVER VIRUS' named entity 'DIVERSE' named entity 'FUSION' named entity 'THESE' named entity 'FUTURE' named entity 'CELLULAR MEMBRANE' named entity 'INHIBITORY' named entity 'CELL CULTURE' named entity 'PREVENT' named entity 'CELL MEMBRANES' named entity 'CLASS I' named entity 'CONSERVED' named entity 'GLYCOPROTEIN' named entity 'ENDOCYTIC PATHWAY' named entity 'FOLLOWING' named entity 'PRODUCTIVE' named entity 'ENTRY' named entity 'SINGLE' named entity 'PROVIDE' named entity 'VIRUSES' named entity 'CONSISTENT WITH' named entity 'VIRAL INFECTION' named entity 'ACTIVE' named entity 'OFFER' named entity 'VIRUS' named entity 'VIRAL AND' named entity 'CYTOPLASM' named entity 'RNA VIRUSES' named entity 'CLASS III' named entity 'MULTIPLE' named entity 'INHIBITING' named entity 'REGION' named entity 'VIRAL GENOME' named entity 'EVENT' named entity 'TRAFFIC' named entity 'BIND' named entity 'PEPTIDE' named entity 'PEPTIDES' named entity 'VIRAL ENVELOPE' named entity 'CRITICAL' named entity 'INHIBITING' named entity 'HERE' named entity 'III' named entity 'INHIBITION' named entity 'INFECTIVITY' named entity 'FINDINGS' named entity 'DEVELOPMENT' named entity 'UNRELATED' named entity 'MEMBRANES' named entity 'MECHANISM' named entity 'PEPTIDE' named entity 'STRUCTURE' named entity 'STEM' named entity 'PROTEINS' named entity 'ACIDIFICATION' named entity 'DIRECTION' named entity 'HAVE' named entity 'ACCESS' named entity 'PROTEIN SEQUENCE' named entity 'FUSION' named entity 'OCCUR' named entity 'SIMILAR' named entity 'PROPOSED' named entity 'PROCESS' named entity 'INSIGHTS'

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