MDA5 (melanoma differentiation-associated protein 5) is a RIG-I-like receptor dsRNA helicase enzyme that is encoded by the IFIH1 gene in humans. [5] MDA5 is part of the RIG-I-like receptor (RLR) family, which also includes RIG-I and LGP2, and functions as a pattern recognition receptor capable of detecting viruses.

We found that RIG-I or MDA5 mutants with low ATP hydrolysis activity exhibit constitutive activity but this was fully reverted when associated with mutations preventing RNA binding to the helicase domain. We propose that the turnover kinetics of the ATPase domain enables the discrimination of self/non-self RNA by both RIG-I and MDA5.

MDA5 recognizes long duplex RNAs that presumably exist in a complex higher-order configuration, engaging RNA through interactions with its helicase (HEL) and carboxy-terminal domain (CTD) and via the formation of cooperative filaments (Wu et al., 2013; Yu et al., 2018).

黑色素瘤分化相关基因5 （Melanoma differentiation-associated gene 5，简称MDA-5）也被称为 IFIH1基因 或 Helicard基因。 该基因位于染色体2q24.3上，是一个早期干扰素β反应性基因。 MDA-5在抗病毒免疫反应中起到关键作用，它可以识别小核糖核酸病毒RNA并介导免疫激活，促进病毒感染细胞的凋亡。 因此，MDA-5可以作为一种病毒感染的感应器或病原体识别受体。 MDA5（黑色素瘤分化相关蛋白5）是一种 RIG-I类受体 dsRNA螺旋酶，由IFIH1基因编码。 MDA5是RIG-I …

Melanoma differentiation-associated gene-5 (MDA5) detects viral double-stranded RNA in the cytoplasm. RNA binding induces MDA5 to activate the signalling adaptor MAVS through interactions between the caspase recruitment domains (CARDs) of the two ...

RIG-I (Retinoic acid-inducible gene I) and MDA5 (Melanoma Differentiation-Associated protein 5), collectively known as the RIG-I-like receptors (RLRs), are key protein sensors of the pathogen-associated molecular patterns (PAMPs) in the form of viral double-stranded RNA (dsRNA) motifs to induce expression of type 1 interferons (IFN1) (IFNα and I...

2018年12月18日 · RIG-I and MDA5 consist of two amino-terminal tandem caspase activation and recruitment domains (CARD1-2) that are important for signal transduction; a central DExH/C HELicase domain (HEL); and...

2013年1月17日 · MDA5, a viral double-stranded RNA (dsRNA) receptor, shares sequence similarity and signaling pathways with RIG-I yet plays essential functions in antiviral immunity through distinct specificity for viral RNA.

The C-terminal domain (CTD) of MDA5 is responsible for RNA recognition and binding, the helicase (Hel) domains 1/2i/2 are responsible for RNA modification through ATP hydrolysis and the...

2006年4月9日 · Here we use mice deficient in MDA5 (MDA5-/-) to show that MDA5 and RIG-I recognize different types of dsRNAs: MDA5 recognizes poly (I:C), and RIG-I detects in vitro transcribed dsRNAs. RNA...