About: The ATF6 branch of unfolded protein response and apoptosis are activated to promote African swine fever virus infection

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About: The ATF6 branch of unfolded protein response and apoptosis are activated to promote African swine fever virus infection 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	The ATF6 branch of unfolded protein response and apoptosis are activated to promote African swine fever virus infection
Creator	Alonso, C Dalmau-Mena, I Galindo, I Hernáez, B Cuesta-Geijo, M Muñ Oz-Moreno, R
Source	Medline; PMC
abstract	African swine fever virus (ASFV) infection induces apoptosis in the infected cell; however, the consequences of this activation on virus replication have not been defined. In order to identify the role of apoptosis in ASFV infection, we analyzed caspase induction during the infection and the impact of caspase inhibition on viral production. Caspases 3, 9 and 12 were activated from 16 h post-infection, but not caspase 8. Indeed, caspase 3 activation during the early stages of the infection appeared to be crucial for efficient virus exit. In addition, the inhibition of membrane blebbing reduced the release of virus particles from the cell. ASFV uses the endoplasmic reticulum (ER) as a site of replication and this process can trigger ER stress and the unfolded protein response (UPR) of the host cell. In addition to caspase 12 activation, indicators of ER stress include the upregulation of the chaperones calnexin and calreticulin upon virus infection. Moreover, ASFV induces transcription factor 6 signaling pathway of the UPR, but not the protein kinase-like ER kinase or the inositol-requiring enzyme 1 pathways. Thus, the capacity of ASFV to regulate the UPR may prevent early apoptosis and ensure viral replication.
has issue date	2012-07-05(xsd:dateTime)
bibo:doi	10.1038/cddis.2012.81
bibo:pmid	22764100
has license	cc-by-nc-nd
sha1sum (hex)	d800e113c0f37fea4586a18115d07a7bbb3e5464
schema:url	https://doi.org/10.1038/cddis.2012.81
resource representing a document's title	The ATF6 branch of unfolded protein response and apoptosis are activated to promote African swine fever virus infection
has PubMed Central identifier	PMC3406580
has PubMed identifier	22764100
schema:publication	Cell Death Dis
resource representing a document's body	covid:d800e113c0f37fea4586a18115d07a7bbb3e5464#body_text
is schema:about of	named entity 'ER stress' named entity 'addition' named entity 'calreticulin' named entity 'cell' named entity 'African swine fever virus' covid:arg/d800e113c0f37fea4586a18115d07a7bbb3e5464 named entity 'infection' named entity 'early stages' named entity 'ER stress' named entity 'prevent' named entity 'caspase' named entity 'addition' named entity 'regulate' named entity 'site' named entity 'induces' named entity 'apoptosis' named entity 'upregulation' named entity 'African swine fever virus' named entity 'caspase 3' named entity 'membrane blebbing' named entity 'virus replication' named entity 'virus infection' named entity 'upregulation' named entity 'ASFV' named entity 'infection' named entity 'ASFV' named entity 'apoptosis' named entity 'apoptosis' named entity 'African swine fever virus' named entity 'apoptotic pathways' named entity 'sodium azide' named entity 'apoptosis' named entity 'Vero' named entity 'XBP1' named entity 'caspases' named entity 'feedback mechanism' named entity 'non-specific' named entity 'Horseradish peroxidase' named entity 'Virus' named entity 'abcam' named entity 'PBS' named entity 'Santa Cruz, CA' named entity 'virus' named entity 'Western blotting' named entity 'Franklin Lakes' named entity 'ASFV' named entity 'ASFV' named entity 'virus' named entity 'organelle' named entity 'Biovision' named entity 'similar manner' named entity 'mRNA' named entity 'calreticulin' named entity 'mRNA' named entity 'apoptotic pathways' named entity 'viral infection' named entity 'mitochondrial' named entity 'viruses' named entity 'caspase 8' named entity 'ATF6' named entity 'protein degradation' named entity 'fluorescence microscopy' named entity 'chaperones' named entity 'Calreticulin' named entity 'infection' named entity 'virus' named entity 'nitrocellulose' named entity 'dose-dependent manner' named entity 'PERK' named entity 'Dunnet' named entity 'active form' named entity 'infection' named entity 'apoptosis' named entity 'apoptotic' named entity 'apoptosis' named entity 'GRP78'

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