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Interferon‐Induced Mx Proteins: Dynamin‐Like GTPases with Antiviral Activity
Abstract
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.
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“Increased expression of MUC5AC mRNA in bronchial epithelial cells has been reported for mice after RSV infection (97)”
From The airway epithelium: soldier in the fight against respiratory viruses (2011) · cites this paper as [97]
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Pletneva, L. M., Haller, O., Porter, D. D., Prince, G. A., & Blanco, J. C. G. (2006) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2006.26.914 · Cited by 41
Self-citationWenzel, J., Gütgemann, I., Distelmaier, M., Uerlich, M., Mikus, S., Bieber, T. R. M., & Tüting, T. (2005) · Journal of the American Academy of Dermatology · doi:10.1016/j.jaad.2005.05.042 · Cited by 41
Peltekian, C., Gordien, E., Garreau, F., Meas‐Yedid, V., Soussan, P., Willams, V., Chaix, M., Olivo‐Marín, J., Bréchot, C., & Kremsdorf, D. (2005) · Journal of Hepatology · doi:10.1016/j.jhep.2005.06.019 · Cited by 40
Antiviral Activities of Interleukin-27: A Partner for Interferons?
Amsden, H., Kourko, O., Roth, M., & Gee, K. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.902853 · Cited by 39
Metadata
- Authors
- Haller, O., & Kochs, G.
- Affiliations
- University of Freiburg (DE)
- Corresponding author
- Haller, Otto
- Venue
- Traffic
- Publisher
- Wiley
- Published
- 2002-09-16
- Volume
- 3
- Issue
- 10
- Pages
- 710-717
- ISSN
- 1398-9219 (ISSN-L)
- 1600-0854
- OpenAlex
- W2090023448
- Cited by
- 460
- References
- 53
- Citations by year
- 2026: 2 · 2025: 10 · 2024: 13 · 2023: 12 · 2022: 9 · 2021: 9 · 2020: 15 · 2019: 8 · 2018: 11 · 2017: 14 · 2016: 8 · 2015: 14 · 2014: 12 · 2013: 17 · 2012: 23
- FWCI
- 2.41
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Traffic (publishedVersion)
- PubMed (publishedVersion)
- FreiDok plus (Universitätsbibliothek Freiburg) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- Mx protein, MxA, dynamin superfamily, antiviral activity, Bunyaviridae, orthomyxoviruses, Thogoto virus, Golgi apparatus, endoplasmic reticulum, GTP hydrolysis, viral assembly, RNA viruses, host-virus interaction
- MeSH terms
- Antiviral Agents, Interferons, Molecular Weight, Subcellular Fractions, GTP-Binding Proteins, GTP Phosphohydrolases, Dynamins, Myxovirus Resistance Proteins
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