{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMitochondrial antiviral‐signaling protein (MAVS) is a pivotal adaptor that, when engaged by cytosolic RNA sensors such as RIG‐I, MDA5, and even Nod2, orchestrates the innate immune response to viral infection. Located on the outer mitochondrial membrane, MAVS facilitates the recruitment of downstream kinases and adaptor molecules that activate transcription factors—including NF‐κB, IRF3, and IRF7—to induce type I interferon and proinflammatory cytokine expression. In addition, MAVS undergoes a prion‐like conformational switch and assembles filamentous structures that amplify the antiviral signal, thereby integrating multiple upstream viral RNA recognition events into a robust immune response."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSeveral viruses have evolved sophisticated strategies to subvert MAVS‐mediated signaling and thereby evade host immunity. The hepatitis C virus, for example, exploits its NS3/4A protease to cleave MAVS from the mitochondrial membrane, effectively silencing interferon induction. Likewise, hepatitis B virus employs its HBX protein to promote MAVS degradation, while enteroviruses and influenza viruses use their proteases and accessory proteins (including components such as PB2, PB1‐F2, and even the dengue virus–related mechanisms) to impair MAVS function or interrupt its downstream signaling. Other pathogens—notably, poliovirus, HIV‐1, and SARS‐CoV‑2—target MAVS through direct interaction or proteolytic cleavage to block interferon responses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMAVS activity is also finely modulated by an array of host regulatory factors that ensure balanced antiviral responses and prevent immunopathology. Negative regulators such as PCBP2 promote ubiquitination and proteasomal degradation of MAVS, while mitochondrial fusion proteins like Mfn2 and MFN1—and even apoptotic caspases—adjust MAVS aggregation and signal duration. In parallel, MAVS has been implicated in inflammasome activation by facilitating NLRP3 oligomerization, as described in studies linking MAVS to inflammasome components. Positive modulators including IFIT3, which bridges TBK1 to MAVS, and RNA helicases like DHX9 further enhance the antiviral cascade. Additional layers of regulation are provided by pathways that target MAVS for selective autophagic degradation (for example, via tetherin‐MARCH8 or Ndfip1‐recruited E3 ligases), and by the linear ubiquitination of key signaling partners. Moreover, MAVS‐dependent pathways contribute to defenses in diverse cellular settings—from epithelial cells responding to Legionella infection to mitigating responses against chikungunya virus and modulating HIV‐1 replication—and may even influence gut microbial homeostasis"}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "35"}, {"type": "fg_f", "ref": "15"}, {"type": "fg_f", "ref": "25"}]}, {"type": "t", "text": "[reinforced]"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "36"}, {"type": "fg_f", "ref": "17"}]}, {"type": "t", "text": "[for viral interference], and"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}]}, {"type": "t", "text": "have all contributed to our growing understanding of the diverse mechanisms that modulate MAVS function in both promoting and attenuating antiviral immunity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "30"}, {"type": "fg_f", "ref": "14"}, {"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Rashu B Seth, Lijun Sun, Chee-Kwee Ea, et al. 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