About: Lymphocystis Disease Virus (Iridoviridae) Enters Flounder (Paralichthys olivaceus) Gill Cells via a Caveolae-Mediated Endocytosis Mechanism Facilitated by Viral Receptors

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

About: Lymphocystis Disease Virus (Iridoviridae) Enters Flounder (Paralichthys olivaceus) Gill Cells via a Caveolae-Mediated Endocytosis Mechanism Facilitated by Viral Receptors 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	Lymphocystis Disease Virus (Iridoviridae) Enters Flounder (Paralichthys olivaceus) Gill Cells via a Caveolae-Mediated Endocytosis Mechanism Facilitated by Viral Receptors
Creator	Zhong, Ying Zeng, Jing Sheng, Xiuzhen Tang, Xiaoqian Xing, Jing Zhan, Wenbin Chi, Heng
Source	PMC
abstract	In previous research, voltage-dependent anion channel protein 2 (VDAC2) and the receptor of activated protein C kinase 1 (RACK1) in flounder (Paralichthys olivaceus) were confirmed as functional receptors for lymphocystis disease virus (LCDV) entry; however, the underlying mechanism of VDAC2- and RACK1-mediated LCDV entry remains unclear. In this study, we elucidated the endocytosis pathway of LCDV entry into flounder gill (FG) cells by treatment with specific inhibitory agents, siRNAs, and co-localization analysis. LCDV entry was significantly inhibited by the disruption of caveolae-mediated endocytosis, dynamin, and microtubules, and the knockdown of caveoline-1 and dynamin expression, but was not inhibited by the disruption of clathrin-mediated endocytosis, micropinocytosis, or low-pH conditions. The disruption of caveolae-mediated and clathrin-mediated endocytosis was verified by the internalization of cholera toxin subunit B (CTB) and transferrin, respectively. Confocal immunofluorescence assay demonstrated that LCDV was co-localized with VDAC2 and RACK1, CTB was co-localized with VDAC2 and RACK1 and partially with LCDV, but transferrin was not co-localized with LCDV, VDAC2, or RACK1, indicating that LCDV utilized the same pathway as CTB, i.e., caveolae-mediated endocytosis. This was different from the pathway of transferrin, which used clathrin-mediated endocytosis. Furthermore, caveolin-1 was co-localized with LCDV, VDAC2, and RACK1, suggesting that caveolin-1 was involved in LCDV entry. These results revealed for the first time that LCDV entered into FG cells via caveolae-mediated endocytosis facilitated by VDAC2 and RACK1 receptors, relying on dynamin and microtubules in a pH-independent manner, which provided new insight into the molecular mechanisms of LCDV entry and potential for the development of antiviral agents, expanding our understanding of iridovirus infection.
has issue date	2020-07-02(xsd:dateTime)
bibo:doi	10.3390/ijms21134722
bibo:pmid	32630682
has license	cc-by
sha1sum (hex)	2c1e7fafd2bcfa66702cf2159ff053abef62ff63
schema:url	https://doi.org/10.3390/ijms21134722
resource representing a document's title	Lymphocystis Disease Virus (Iridoviridae) Enters Flounder (Paralichthys olivaceus) Gill Cells via a Caveolae-Mediated Endocytosis Mechanism Facilitated by Viral Receptors
has PubMed Central identifier	PMC7370161
has PubMed identifier	32630682
schema:publication	Int J Mol Sci
resource representing a document's body	covid:2c1e7fafd2bcfa66702cf2159ff053abef62ff63#body_text
is schema:about of	named entity 'RACK1' named entity 'voltage-dependent anion channel' named entity 'microtubules' named entity 'mediated endocytosis' named entity 'VDAC2' named entity 'RACK1' named entity 'transferrin' named entity 'VDAC2' named entity 'VDAC2' named entity 'infection' named entity 'caveolae' named entity 'Paralichthys olivaceus' named entity 'mediated endocytosis' named entity 'cholera toxin' named entity 'iridovirus' named entity 'VDAC2' named entity 'polyclonal antibodies' named entity 'cholesterol' named entity 'mice' named entity 'lipid rafts' named entity 'caveolae' named entity 'mediated endocytosis' named entity 'molecular mechanism' named entity 'NH 4' named entity 'gene' named entity 'siRNAs' named entity 'DMSO' named entity 'CTB' named entity 'plasma membrane' named entity 'clathrin' named entity 'scatter plots' named entity 'nystatin' named entity 'VDAC2' named entity 'transferrin' named entity 'primers' named entity 'CTB' named entity 'RT-PCR' named entity 'ImageJ' named entity 'transfected' named entity 'infection' named entity 'RACK1' named entity 'virus' named entity 'caveolae' named entity 'CTB' named entity 'RACK1' named entity 'cholesterol' named entity 'clathrin-mediated endocytosis' named entity 'dynamin' named entity 'caveolin-1' named entity 'immune serum' named entity 'cytoplasm' named entity 'PBS' named entity 'host cells' named entity 'Java' named entity 'PBS' named entity 'recombinant' named entity 'clathrin' named entity 'dynamin' named entity 'molecular mechanism' named entity 'CTB' named entity 'PKC' named entity 'CTB' named entity 'microtubules' named entity 'caveolin' named entity 'cholesterol' named entity 'immune serum' named entity 'VDAC2' named entity 'viruses' named entity 'NH 4' named entity 'transfected' named entity 'Megalocytivirus' named entity 'rhabdomyosarcoma' named entity 'qPCR' named entity 'CTB' named entity 'reverse-transcribed'

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