About: The Membrane Protein of Severe Acute Respiratory Syndrome Coronavirus Functions as a Novel Cytosolic Pathogen-Associated Molecular Pattern To Promote Beta Interferon Induction via a Toll-Like-Receptor-Related TRAF3-Independent Mechanism

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About: The Membrane Protein of Severe Acute Respiratory Syndrome Coronavirus Functions as a Novel Cytosolic Pathogen-Associated Molecular Pattern To Promote Beta Interferon Induction via a Toll-Like-Receptor-Related TRAF3-Independent Mechanism Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	The Membrane Protein of Severe Acute Respiratory Syndrome Coronavirus Functions as a Novel Cytosolic Pathogen-Associated Molecular Pattern To Promote Beta Interferon Induction via a Toll-Like-Receptor-Related TRAF3-Independent Mechanism
Creator	Wang, Yi Meng, Jin Liu, Li
source	Medline; PMC
abstract	Most of the intracellular pattern recognition receptors (PRRs) reside in either the endolysosome or the cytoplasm to sense pathogen-derived RNAs, DNAs, or synthetic analogs of double-stranded RNA (dsRNA), such as poly(I:C). However, it remains elusive whether or not a pathogen-derived protein can function as a cytosolic pathogen-associated molecular pattern (PAMP). In this study, we demonstrate that delivering the membrane gene of severe acute respiratory syndrome coronavirus (SARS-CoV) into HEK293T, HEK293ET, and immobilized murine bone marrow-derived macrophage (J2-Mφ) cells significantly upregulates beta interferon (IFN-β) production. Both NF-κB and TBK1-IRF3 signaling cascades are activated by M gene products. M protein rather than M mRNA is responsible for M-mediated IFN-β induction that is preferentially associated with the activation of the Toll-like receptor (TLR) adaptor proteins MyD88, TIRAP, and TICAM2 but not the RIG-I signaling cascade. Blocking the secretion of M protein by brefeldin A (BFA) failed to reverse the M-mediated IFN-β induction. The antagonist of both TLR2 and TLR4 did not impede M-mediated IFN-β induction, indicating that the driving force for the activation of IFN-β production was generated from inside the cells. Inhibition of TRAF3 expression by specific small interfering RNA (siRNA) did not prevent M-mediated IFN-β induction. SARS-CoV pseudovirus could induce IFN-β production in an M rather than M(V68A) dependent manner, since the valine-to-alanine alteration at residue 68 in M protein markedly inhibited IFN-β production. Overall, our study indicates for the first time that a pathogen-derived protein is able to function as a cytosolic PAMP to stimulate type I interferon production by activating a noncanonical TLR signaling cascade in a TRAF3-independent manner.
has issue date	2016-02-09(xsd:dateTime)
bibo:doi	10.1128/mbio.01872-15
bibo:pmid	26861016
has license	cc-by-nc-sa
sha1sum (hex)	358d351a51c6f7f9ddb86ea3fb468c7fdc601e3d
schema:url	https://doi.org/10.1128/mbio.01872-15
resource representing a document's title	The Membrane Protein of Severe Acute Respiratory Syndrome Coronavirus Functions as a Novel Cytosolic Pathogen-Associated Molecular Pattern To Promote Beta Interferon Induction via a Toll-Like-Receptor-Related TRAF3-Independent Mechanism
has PubMed Central identifier	PMC4752600
has PubMed identifier	26861016
schema:publication	mBio
resource representing a document's body	covid:358d351a51c6f7f9ddb86ea3fb468c7fdc601e3d#body_text
is schema:about of	named entity 'VIRAL INFECTION' named entity 'INDUCED' named entity 'A POINT' named entity '28I' named entity 'FUNCTION' named entity 'PATTERN' named entity 'PROTEIN ' named entity 'MEMBRANE' named entity 'M GENE' named entity '90%' named entity 'CYTOSOLIC' named entity 'POLY' named entity 'DERIVED' named entity 'HEK293T' named entity 'CELLS' named entity 'TICAM2' named entity 'ASSOCIATED WITH' named entity 'pathogen-associated molecular pattern' named entity 'beta' named entity 'Most' named entity 'protein' named entity 'TLR' named entity 'activated' named entity 'signaling cascade' named entity 'viral infection' named entity 'PAMP' named entity 'time' named entity 'TRAF3' named entity 'Toll' named entity 'point mutation' named entity 'INDUCTION' named entity 'PATTERN' named entity 'MARKEDLY' named entity 'BETA INTERFERON' named entity 'DNAS' named entity 'PRODUCTION' named entity 'SYNTHETIC' named entity 'SARS-COV' named entity 'POINT MUTATION' named entity 'CONFIRMED' named entity 'PATHOGEN' named entity 'TRAF3' named entity 'ASSOCIATED' named entity 'MEDIATED' named entity 'PROTEINS' named entity 'IFN' named entity 'RESIDE' named entity 'INTERFERON ' named entity 'IFN' named entity 'FORCE' named entity 'NOVEL' named entity 'FUNCTION' named entity 'INHIBITED' named entity 'SIGNALING CASCADE' named entity 'MEMBRANE PROTEIN' named entity 'TLR' named entity 'MEDIATED' named entity 'CELLS' named entity 'RECEPTOR' named entity 'PROTEIN ' named entity 'LIKE' named entity 'PROMOTE' named entity '90%' named entity 'FUNCTIONS' named entity 'M PROTEIN' named entity 'LEVEL' named entity 'INTERFERON ' named entity 'MOST LIKELY' named entity 'MECHANISM' named entity 'RESIDUE' named entity 'RESULTS' named entity 'DRIVING' named entity 'ANALOGS' named entity 'PRODUCTS' named entity 'DOUBLE-STRANDED RNA' named entity 'MURINE BONE MARROW' named entity 'STUDY' named entity 'INDUCTION' named entity 'M PROTEIN'

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