Recombinant Human Mitochondrial antiviral-signaling protein (MAVS), partial, Biotinylated

Function

Adapter required for innate immune defense against viruses (PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806, PubMed:19631370, PubMed:20127681, PubMed:20451243, PubMed:21170385, PubMed:23087404, PubMed:27992402, PubMed:33139700, PubMed:37582970, PubMed:39589880, PubMed:38995016). Acts downstream of DHX33, RIGI and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFNB and RANTES (CCL5) (PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806, PubMed:19631370, PubMed:20127681, PubMed:20451243, PubMed:20628368, PubMed:21170385, PubMed:23087404, PubMed:25636800, PubMed:27736772, PubMed:33110251, PubMed:40042308). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state (PubMed:20451243). Upon viral infection, peroxisomal MAVS induces the rapid interferon-independent expression of defense factors that provide short-term protection, whereas mitochondrial MAVS activates an interferon-dependent signaling pathway with delayed kinetics, which amplifies and stabilizes the antiviral response (PubMed:20451243). May activate the same pathways following detection of extracellular dsRNA by TLR3 (PubMed:16153868). May protect cells from apoptosis (PubMed:16125763). Involved in NLRP3 inflammasome activation by mediating NLRP3 recruitment to mitochondria (PubMed:23582325)

Subcellular Location

Mitochondrion outer membrane (Single-pass membrane protein); Mitochondrion; Peroxisome

Tissue Specificity

Present in T-cells, monocytes, epithelial cells and hepatocytes (at protein level). Ubiquitously expressed, with highest levels in heart, skeletal muscle, liver, placenta and peripheral blood leukocytes

Subunit

(Microbial infection) Interacts with human enterovirus D68 protein VP3; this interaction inhibits MAVS leading to suppression of host innate immunity

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• Xu L.-G. et al. VISA is an adapter protein required for virus-triggered IFN-beta Signaling. — Mol. Cell (2005)
• Meylan E. et al. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. — Nature (2005)
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• Lad S.P. et al. Identification of MAVS splicing variants that interfere with RIGI/MAVS pathway signaling. — Mol. Immunol. (2008)
• Patel M.R. et al. Convergent evolution of escape from hepaciviral antagonism in primates. — PLoS Biol. (2012)
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• Matsuda A. et al. Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. — Oncogene (2003)