{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMX1 is a type I/III interferon–induced dynamin‐like GTPase that serves as a key effector of the innate antiviral response. Its structure comprises an N‐terminal GTPase domain, a middle domain that mediates self‐assembly, and a C‐terminal GTPase effector domain. Structural and biochemical studies revealed that MX1 can oligomerize into ring‐like and filamentous assemblies, and its ability to bind and hydrolyze GTP promotes dramatic conformational changes that are critical for targeting viral substrates. These elegant self‐assembly properties and membrane‐associating features underpin the mechanochemical functions of MX1 against a broad spectrum of viral pathogens."}, {"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": "\nMechanistically, MX1 exerts its antiviral effects primarily by directly interacting with viral components. In influenza virus infection, for example, MX1 disrupts key protein–protein interactions (such as those between viral PB2 and nucleoprotein) and inhibits the proper assembly of viral ribonucleoprotein complexes, thereby impairing viral transcription and replication. Similar inhibitory actions extend to diverse viruses—including hantaviruses, flaviviruses, West Nile virus, and Crimean–Congo hemorrhagic fever virus—where MX1 binding to virus‐encoded nucleocapsid proteins appears to interfere with viral genome transport and assembly."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its direct antiviral action, MX1 expression is tightly regulated by interferon signaling and serves as a robust surrogate marker of the IFN‐induced antiviral state. Genetic polymorphisms within its promoter region influence MX1 expression levels and have been associated with differences in outcomes for patients suffering from hepatitis C, SARS, and other infectious diseases. The sensitivity of MX1 induction also makes it a valuable biomarker in clinical research for assessing IFN bioactivity and monitoring innate immune responses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its canonical antiviral roles, MX1 has been implicated in broader immunomodulatory and clinical contexts. Alterations in MX1 expression or function—whether through alternative splicing, regulatory polymorphisms, or modulation by viral proteins—can influence cellular processes such as membrane remodeling, intracellular trafficking, and even intercellular communication via exosomes. Such multifaceted roles have been observed in diverse disease settings, including inflammatory skin conditions like vitiligo, certain malignancies such as head and neck or prostate cancers, and even in the regulatory dynamics of calcium channel signaling. These findings underscore the versatility of MX1 not only as a direct viral inhibitor but also as a mediator of host immune homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "35"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Georg Kochs, Markus Haener, Ueli Aebi, et al. 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