About: African swine fever virus-cell interactions: From virus entry to cell survival

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	African swine fever virus-cell interactions: From virus entry to cell survival
Creator	Alonso, Covadonga Galindo, Inmaculada Muñoz-Moreno, Raquel Hernaez, Bruno Angel Cuesta-Geijo, Miguel Cabezas, Marta
source	Elsevier; Medline; PMC
abstract	Abstract Viruses have adapted to evolve complex and dynamic interactions with their host cell. The viral entry mechanism determines viral tropism and pathogenesis. The entry of African swine fever virus (ASFV) is dynamin-dependent and clathrin-mediated, but other pathways have been described such as macropinocytosis. During endocytosis, ASFV viral particles undergo disassembly in various compartments that the virus passes through en route to the site of replication. This disassembly relies on the acid pH of late endosomes and on microtubule cytoskeleton transport. ASFV interacts with several regulatory pathways to establish an optimal environment for replication. Examples of these pathways include small GTPases, actin-related signaling, and lipid signaling. Cellular cholesterol, the entire cholesterol biosynthesis pathway, and phosphoinositides are central molecular networks required for successful infection. Here we report new data on the conformation of the viral replication site or viral factory and the remodeling of the subcellular structures. We review the virus-induced regulation of ER stress, apoptosis and autophagy as key mechanisms of cell survival and determinants of infection outcome. Finally, future challenges for the development of new preventive strategies against this virus are proposed on the basis of current knowledge about ASFV-host interactions.
has issue date	2013-04-30(xsd:dateTime)
bibo:doi	10.1016/j.virusres.2012.12.006
bibo:pmid	23262167
has license	els-covid
sha1sum (hex)	b89ea968cf71f4e19a038e4a8442b6b5515525de
schema:url	https://doi.org/10.1016/j.virusres.2012.12.006
resource representing a document's title	African swine fever virus-cell interactions: From virus entry to cell survival
has PubMed Central identifier	PMC7114420
has PubMed identifier	23262167
schema:publication	Virus Research
resource representing a document's body	covid:b89ea968cf71f4e19a038e4a8442b6b5515525de#body_text
is schema:about of	named entity 'INTERACTIONS' named entity 'AFRICAN SWINE FEVER VIRUS' named entity 'CELL' named entity 'VIRUS ENTRY' named entity 'CELL SURVIVAL' named entity 'swine fever' named entity 'macropinocytosis' named entity 'HDAC6' named entity 'cell shrinkage' named entity 'Epidermal growth factor receptor' named entity 'virions' named entity 'plasma membrane' named entity 'aggresomes' named entity 'ammonium chloride' named entity 'cytoplasmic' named entity 'phosphorylation' named entity 'cell lines' named entity 'ER stress' named entity 'hybridization' named entity 'macrophages' named entity 'PGE2' named entity 'nucleus' named entity 'structural studies' named entity 'PI3K' named entity 'virus' named entity 'DNA repair enzymes' named entity 'staining' named entity 'Rab GTPases' named entity 'autophagosomal membrane' named entity 'viral protein' named entity 'virus' named entity 'viral fusion proteins' named entity 'recombinant' named entity 'caspase 3' named entity 'protein aggregates' named entity 'proteolysis' named entity 'nucleic acid' named entity 'actin' named entity 'Cytoplasmic' named entity 'macropinocytosis' named entity 'endosome' named entity 'macropinocytosis' named entity 'infection' named entity 'Autophagy' named entity 'ULK2' named entity 'cytoplasmic' named entity 'HSV-1' named entity 'HDAC6' named entity 'dynein motors' named entity 'microtubule' named entity 'organelles' named entity 'structural protein' named entity 'HSV1' named entity 'dynein' named entity 'Rab7' named entity 'Bcl2 family' named entity 'viral replication' named entity 'protein' named entity 'ICP34.5' named entity 'Vero cells' named entity 'pathogenesis' named entity 'aggresomes' named entity 'Vero' named entity 'endocytic' named entity 'chaperones' named entity 'VFs' named entity 'porcine' named entity 'UPR' named entity 'digestion' named entity 'vaccine design' named entity 'Clathrin' named entity 'virion' named entity 'Valproic acid' named entity 'swine' named entity 'perinuclear' named entity 'hpi'

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