RIG-IandMDA5are two distinctsensors of viral double-stranded RNA(dsRNA), a replication intermediate for RNA viruses [1-3]. Upon recognition of dsRNA, RIG-I and MDA5 are recruited by theMAVS adaptorto the outer membrane of the mitochondria leading to the activation of several transcription fac...
Specifically, RIG-I and MDA5 sense viral RNA in the cytosol and subsequently bind through their N-terminal caspase recruitment domains (CARDs) to the signaling adaptor MAVS (also called VISA, IPS-1, or CARDIF); this binding triggers antiviral innate immune responses, resulting in the production...
MAVS does not bind to free mitochondria but to mitochondrial associated membrane (MAM), which physically connects endoplasmic reticulum (ER) specialized domain to outer mitochondrial membrane. Upon recognition of viral RNA, RIG-I and MDA5 interact with MAVS through mutual caspase activation and ...
ERAL1 MAVS TRIM25 RIG-1/MDA5 Introduction The capacity to distinguish self from non-self is the basic function of the immune system. Innate immunity is the first line of defense against invading pathogens. Pathogen-associated molecular patterns (PAMPs) and danger-associated molecular patterns (DAMP...
(C/EBP), beta; CQ: chloroquine; DDX58/retinoic acid inducible gene 1/Rig-1: DExD/H box helicase 58; h: hours; IFIH1/MDA5: interferon induced with helicase C domain 1; IFNB/IFN-尾: interferon beta 1, fibroblast; KO: knockout; MAVS: mitochondrial antiviral signaling protein; NAFLD: ...
RNA组分,并通过自身的CARD与下游信号分子MAVS的CARD相互作用来传递信号,激活细胞转录因子IRF-3和NF-κB,使其进入细胞核内,诱导β干扰素的表达,从而启动固有免疫应答和调节随后的获得性免疫应答,增强机体抵抗病毒的能力.另外,近年来的研究还发现了两个与RIG-I在序列,功能上都有很大相似性的病毒RNA识别蛋白质:MDA5和...
Scattered evidence indicates that the RIG-I-MAVS-TRAF6 axis induces K63-linked polyubiquitination of Beclin-1, which has been implicated in triggering autophagy (Lee et al., 2018); p38 MAPK-mediated protein phosphorylation modulates host cell susceptibility to Salmonella infection by affecting ...
[14]. The CARD domain of MAVS interacts with the CARD domains of RIG-I and MDA5, while its PRR domain binds to TRAF2, 3, 5, and 6 members of the TRAF family, thereby facilitating subsequent signal transduction [15]. However, the function of TRAF1 within the RIG-I signaling pathway ...