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Myxovirus resistance protein 1 (MxA) is a large dynamin-like GTPase induced mainly by type I and III interferons and is essential for the cell-autonomous antiviral defense in humans[2][4]. MxA is composed of a GTPase domain, a central bundle signaling element, and a stalk domain responsible for oligomerization[1][4]. Upon induction, MxA oligomerizes and forms ring-like structures that physically interact with and inhibit the transcriptional and replicative machinery of sensitive viruses, such as influenza virus and SARS-CoV[1][2][3][4]. Genetic polymorphisms in the MX1 promoter influence both basal and induced expression levels and are associated with differential susceptibility to certain viral infections and treatment outcomes with interferons[3]. MxA is a valuable readout for innate immune activation and is being investigated as a biomarker for both infectious diseases and interferon treatment efficacy[3][4].
Drugs induce MxA expression via stimulation of interferon receptor signaling. MxA acts by binding and hydrolyzing GTP, oligomerizing, and targeting viral nucleoproteins, thus inhibiting viral replication and transcription[1][2][4]
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