Structural Variability in the RLR-MAVS Pathway and Sensitive Detection of Viral RNAs.
Cryo-electron microscopy
NMR technique
RLR and MAVS
X-ray crystallography
exogenous microorganisms
viral RNAs.
Journal
Medicinal chemistry (Shariqah (United Arab Emirates))
ISSN: 1875-6638
Titre abrégé: Med Chem
Pays: Netherlands
ID NLM: 101240303
Informations de publication
Date de publication:
2019
2019
Historique:
received:
05
10
2018
revised:
23
10
2018
accepted:
12
12
2018
pubmed:
21
12
2018
medline:
23
7
2019
entrez:
21
12
2018
Statut:
ppublish
Résumé
Cells need high-sensitivity detection of non-self molecules in order to fight against pathogens. These cellular sensors are thus of significant importance to medicinal purposes, especially for treating novel emerging pathogens. RIG-I-like receptors (RLRs) are intracellular sensors for viral RNAs (vRNAs). Their active forms activate mitochondrial antiviral signaling protein (MAVS) and trigger downstream immune responses against viral infection. Functional and structural studies of the RLR-MAVS signaling pathway have revealed significant supramolecular variability in the past few years, which revealed different aspects of the functional signaling pathway. Here I will discuss the molecular events of RLR-MAVS pathway from the angle of detecting single copy or a very low copy number of vRNAs in the presence of non-specific competition from cytosolic RNAs, and review key structural variability in the RLR / vRNA complexes, the MAVS helical polymers, and the adapter-mediated interactions between the active RLR / vRNA complex and the inactive MAVS in triggering the initiation of the MAVS filaments. These structural variations may not be exclusive to each other, but instead may reflect the adaptation of the signaling pathways to different conditions or reach different levels of sensitivity in its response to exogenous vRNAs.
Identifiants
pubmed: 30569868
pii: MC-EPUB-95310
doi: 10.2174/1573406415666181219101613
pmc: PMC6858087
mid: NIHMS1004504
doi:
Substances chimiques
Adaptor Proteins, Signal Transducing
0
MAVS protein, human
0
RNA, Viral
0
RNA Helicases
EC 3.6.4.13
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
443-458Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM111367
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM093271
Pays : United States
Organisme : NCRR NIH HHS
ID : S10 RR027972
Pays : United States
Organisme : NIGMS NIH HHS
ID : U24 GM116788
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM088745
Pays : United States
Organisme : NIGMS NIH HHS
ID : R21 GM131231
Pays : United States
Informations de copyright
Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.
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