The DOI matches its Crossref record; 63 of the 63 references it cites were found in a registry or an index.
Interferon-Induced Ifit Proteins: Their Role in Viral Pathogenesis
Open accessAbstract
A major component of the protective antiviral host defense is contributed by the intracellular actions of the proteins encoded by interferon-stimulated genes (ISGs); among these are the i nter f eron- i nduced proteins with t etratricopeptide repeats (IFITs), consisting of four members in human and three in mouse. IFIT proteins do not have any known enzyme activity. Instead, they inhibit virus replication by binding and regulating the functions of cellular and viral proteins and RNAs. Although all IFITs are comprised of multiple copies of the degenerate tetratricopeptide repeats, their distinct tertiary structures enable them to bind different partners and affect host-virus interactions differently. The recent use of Ifit knockout mouse models has revealed novel antiviral functions of these proteins and new insights into the specificities of ISG actions. This article focuses on human and murine IFIT1 and IFIT2 by reviewing their mechanisms of action, their critical roles in protecting mice from viral pathogenesis, and viral strategies to evade IFIT action.
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Cites
Functional Role of Type I and Type II Interferons in Antiviral Defense
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2′-O methylation of the viral mRNA cap evades host restriction by IFIT family members
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Self-citationThe broad-spectrum antiviral functions of IFIT and IFITM proteins
Diamond, M. S., & Farzan, M. (2013) · Nature Reviews Immunology · doi:10.1038/nri3344 · Cited by 849
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Self-citationIFIT1 is an antiviral protein that recognizes 5′-triphosphate RNA
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Cited by
RIG-I and Other RNA Sensors in Antiviral Immunity
Chow, K. T., Gale, M., & Loo, Y.-M. (2018) · Annual Review of Immunology · doi:10.1146/annurev-immunol-042617-053309 · Cited by 429
Berger, G., Knelson, E. H., Jimenez-Macias, J. L., Nowicki, M. O., Han, S., Panagioti, E., Lizotte, P. H., Adu-Berchie, K., Stafford, A., Dimitrakakis, N., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2111003119 · Cited by 179
Sikorski, P. J., Warminski, M., Kubacka, D., Ratajczak, T., Nowis, D., Kowalska, J., & Jemielity, J. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa032 · Cited by 142
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Advancing mRNA technologies for therapies and vaccines: An African context
Kairuz, D., Samudh, N., Ely, A., Arbuthnot, P., & Bloom, K. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1018961 · Cited by 25
“IFITs bind to eIF3 to prevent formation of the pre-initiation complex that is required for translation, and binds to mRNAs that lack a cap 1 moiety to prevent its translation (reviewed in (31)).”
Background
Metadata
- Authors
- Fensterl, V., & Sen, G. C.
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2015-03
- Volume
- 89
- Issue
- 5
- Pages
- 2462-2468
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- OpenAlex
- W2141659272
- Cited by
- 339
- References
- 63
- FWCI
- 6.35
- Type
- journal article
- Language
- en
- Open access
- green
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