Mitochondrial antiviral signaling protein: a potential therapeutic target in renal disease

Abstract

Mitochondrial antiviral signaling protein (MAVS) is a key innate immune adaptor on the outer mitochondrial membrane that acts as a switch in the immune signal transduction response to viral infections. Some studies have reported that MAVS mediates NF-κB and type I interferon signaling during viral infection and is also required for optimal NLRP3 inflammasome activity. Recent studies have reported that MAVS is involved in various cancers, systemic lupus erythematosus, kidney diseases, and cardiovascular diseases. Herein, we summarize the structure, activation, pathophysiological roles, and MAVS-based therapies for renal diseases. This review provides novel insights into MAVS’s role and therapeutic potential in the pathogenesis of renal diseases.

Understanding the impact of in vitro transcription byproducts and contaminants

“…RIG-I and MDA5 both activate the MAVS pathway upon filamentation and the subsequent ubiquitination and oligomerization of their two N-terminal CARD domains ( Peisley et al, 2012 ; Peisley et al, 2013 ). MAVS recruits TRAF3/6 which subsequently activates the kinase complexes TBK1 and IKK, which in turn leads to activation of IRF3/7 and NF-κB, respectively ( Wu et al, 2023 ). While the downstream signaling cascades of the two receptors are very similar, the dsRNA species that they each recognize are distinct.…”

Mitochondrial oxidative stress, mitochondrial ROS storms in long COVID pathogenesis

“…This causes the activation and recruitment of NLR family pyrin domain containing 3 (NLRP3). Wu et al have reported that MAVS mediates NF-kB and type I interferon signaling during viral infection and is also required to activate the NLR family pyrin domain containing 3 (NLRP3) that triggers an immune response (55).. Apoptosisassociated speck-like protein containing a caspase recruitment domain (ASC) protein (56), and Caspase-1, which assemble to create the NLRP3 inflammasome (57). The activated NLRP3 inflammasome cleaves the cytokines Pro-IL-1B and Pro-IL-18 into their mature and biologically active forms (IL-1B and IL-18), thus exacerbating the inflammation state (58).…”