About: Peptide inhibitors of tembusu virus infection derived from the envelope protein

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Peptide inhibitors of tembusu virus infection derived from the envelope protein 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
has title	Peptide inhibitors of tembusu virus infection derived from the envelope protein
Creator	Yang, Jing Zhao, Peng Han, Kaikai Huang, Xinmei Li, Yin Liu, Qingtao Liu, Yuzhuo Zhang, Lijiao Zhao, Dongmin Li, Y Liu, Huang
Source	Elsevier; Medline; PMC
abstract	Abstract The outbreak and spread of Tembusu virus (TMUV) has caused very large losses in the waterfowl-breeding industry since 2010. The viral envelope (E) protein, the principal surface protein of viral particles, plays a vital role in viral entry and fusion. In this study, two peptides derived from domain II (DII) and the stem of the TMUV envelope protein, TP1 and TP2, respectively, were tested for their antiviral activity. TP1 and TP2 inhibited TMUV infection in BHK-21 cells, and their 50% inhibitory concentrations (IC50) were 14.19 mg/L and 7.64 mg/L, respectively. Viral inhibition assays in different cell lines of avian origin showed that the inhibitory effects of TP1 and TP2 are not cell type dependent. Moreover, TP2 also exhibited inhibitory activity against Japanese encephalitis virus (JEV) infection. The two peptides inhibited antibody-mediated TMUV infection of duck peripheral blood lymphocytes. Co-immunoprecipitation assays and indirect enzyme-linked immunosorbent assays (ELISAs) indicated that both peptides interact with the surface of the TMUV virion. RNase digestion assays confirmed the release of viral RNA following incubation with TP1, while incubation with TP1 or TP2 interfered with the binding between TMUV and cells. Taken together, these results show that TP1 and TP2 may be developed into antiviral treatments against TMUV infection.
has issue date	2020-05-07(xsd:dateTime)
bibo:doi	10.1016/j.vetmic.2020.108708
bibo:pmid	32456819
has license	els-covid
sha1sum (hex)	bfcbf976574f0084a1f4c4d72a769c94c912c23a
schema:url	https://doi.org/10.1016/j.vetmic.2020.108708
resource representing a document's title	Peptide inhibitors of tembusu virus infection derived from the envelope protein
has PubMed Central identifier	PMC7204726
has PubMed identifier	32456819
schema:publication	Vet Microbiol
resource representing a document's body	covid:bfcbf976574f0084a1f4c4d72a769c94c912c23a#body_text
is schema:about of	named entity 'TP1' named entity 'surface' named entity 'incubation' named entity 'virus' named entity 'virus' named entity 'CELLS' named entity 'RELEASE' named entity 'DUCK' named entity 'TP1 AND TP2' named entity 'INHIBITORS' named entity 'CROSS' named entity 'BINDING' named entity 'peripheral blood lymphocytes' named entity 'infection' named entity 'Both' named entity 'Microbiology' named entity 'incubation' named entity 'inhibited' named entity 'virion' named entity 'activity' named entity 'binding' named entity 'interacted' named entity 'TP2' named entity 'PR China' named entity 'Peptide' named entity 'Microbiology' named entity 'infection' named entity 'virus infection' named entity 'antibody-dependent enhancement' named entity 'incubation' named entity 'infection' named entity 'peripheral blood lymphocytes' named entity 'peptides' named entity '37°C' named entity 'peptides' named entity 'inhibitory activity' named entity 'microplate reader' named entity 'infection' named entity 'tetramethyl' named entity 'JEV' named entity 'TP2' named entity 'TP2' named entity 'ectodomain' named entity 'monomeric' named entity 'antiserum' named entity 'Japan' named entity 'non-enveloped' named entity 'paramyxoviruses' named entity 'streptavidin' named entity 'RPMI' named entity 'viral load' named entity 'TP1' named entity 'Biotechnology Company' named entity 'peptides' named entity 'West Nile' named entity 'neutral red' named entity 'infection' named entity 'GenBank' named entity 'digestion' named entity 'CCK-8' named entity 'peptides' named entity 'lysates' named entity 'TP2' named entity 'peptide' named entity 'TP2' named entity '37°C' named entity 'China' named entity 'viral membrane' named entity 'IC50' named entity 'peptides' named entity 'virus'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software