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Interferon‐Induced Mx Proteins: Dynamin‐Like GTPases with Antiviral Activity
Author(s) -
Haller Otto,
Kochs Georg
Publication year - 2002
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1034/j.1600-0854.2002.31003.x
Subject(s) - gtpase , biology , dynamin , microbiology and biotechnology , vesicular stomatitis virus , golgi apparatus , interferon , gtp' , cytoplasm , virology , viral replication , endoplasmic reticulum , rab , virus , biochemistry , cell , endocytosis , enzyme
Mx proteins are interferon‐induced GTPases that belong to the dynamin superfamily of large GTPases. Similarities include a high molecular weight, a propensity to self‐assemble, a relatively low affinity for GTP, and a high intrinsic rate of GTP hydrolysis. A unique property of Mx GTPases is their antiviral activity against a wide range of RNA viruses, including bunya‐ and orthomyxoviruses. The human MxA GTPase accumulates in the cytoplasm of interferon‐treated cells, partly associating with the endoplasmic reticulum. In the case of bunyaviruses, MxA interferes with transport of the viral nucleocapsid protein (N) to the Golgi compartment, the site of virus assembly. In the case of Thogoto virus (an orthomyxovirus), MxA prevents the incoming viral nucleocapsids from being transported into the nucleus, the site of viral transcription and replication. In both cases, the GTP‐binding and carboxy‐terminal effector functions of MxA are required for target recognition. In general, Mx GTPases appear to detect viral infection by sensing nucleocapsid‐like structures. As a consequence, these viral components are trapped and sorted to locations where they become unavailable for the generation of new virus particles.