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2014 | 70 | 07 |
Tytuł artykułu

Granule stresu i ciałka degradujące - ważne mechanizmy obronne w zakażenich wirusowych

Treść / Zawartość
Warianty tytułu
EN
Stress granules and processing bodies: Important mechanisms in viral infections
Języki publikacji
PL
Abstrakty
EN
It has been shown that, in addition to the mechanisms of the immune system, other systems as well are involved in the suppression of viral infections in macroorganisms. These systems include cell structures, such as RNA granules, i.e. stress granules (SG) and processing bodies (PB), which fight infections by protecting cellular mRNA. Their action consists in creating conditions favourable for the genetic material of the cell by placing it inside the RNA granule and stopping the biosynthesis of proteins.
Wydawca
-
Rocznik
Tom
70
Numer
07
Opis fizyczny
s.400-403,bibliogr.
Twórcy
  • Katedra Immunologii, Wydział Biologii, Uniwersytet Szczeciński, ul.Felczaka 3c, 71-412 Szczecin
  • Katedra Immunologii, Wydział Biologii, Uniwersytet Szczeciński, ul.Felczaka 3c, 71-412 Szczecin
autor
  • Katedra Mikrobiologii, Wydział Biologii, Uniwersytet Szczeciński, ul.Felczaka 3c, 71-412 Szczecin
Bibliografia
  • 1. Abrahamyan L. G., Chatel-Chaix L., Ajamian L., Milev M. P., Monette A., Clément J.-F., Song R., Lehmann M., DesGroseillers L., Laughrea M., Boccaccio G., Mouland A. J.: Novel Staufen1 ribonucleoproteins prevent formatting of stress granules but favour encapsidation of HIV-1 genomic RNA. J. Cell. Sci. 2010, 123, 369-383.
  • 2. Anderson P., Kedersha N.: Stress granules: the Tao of RNA triage. Trends Biochem. Sci. 2007, 33, 141-150.
  • 3. Ariumi Y., Kuroki M., Kushima Y., Osugi K., Hijikata M., Maki M., Kieda M., Kato N.: Hepatitis C virus hijacks P-body and stress granule components around lipid droplets. J. Virol. 2011, 85, 6882-6892.
  • 4. Balagopal V., Parker R.: Polysomes, P bodies and stress granules: states and fates of eukaryotic mRNAs. Curr. Opin. Cell Biol. 2009, 21, 403-408.
  • 5. Beckham C. J., Parker R.: P bodies, stress granules, and viral cycles. Cell Host Microbe 2008, 3, 206-212.
  • 6. Creistea I. M., Rozjabek H., Molloy K. R., Karki S., White L. L., Rice C. M., Rout M. P., Chait B. T., MacDonald M. R.: Host factors associated with Sindbis virus RNA-dependent RNA polymerase: role for G3BP1 and G3PB2 in virus replication. J. Virol. 2010, 84, 6720-6732.
  • 7. Dougherty J. D., White J. P., Lloyd R. E.: Poliovirus-mediated disruption of cytoplasmic processing bodies. J. Virol. 2011, 85, 64-75.
  • 8. Garber K., Smith K. T., Reines D., Warren S. T.: Transcription, translation and fragile X syndrome. Curr. Opin. Genet. Dev. 2006, 16, 270-275.
  • 9. Greer A. E., Hearing P., Ketner G.: The adenovirus E4 11K protein binds and relocalizes the cytoplasmic P-body component Ddx6 to aggresomes. Virology 2011, 417, 161-168.
  • 10. Kayali F., Montie H. L., Rafols J. A., DeGracia D. J.: Prolonged translation arrest in reperfused hippocampal cornu Ammonis 1 is mediated by stress granules. Neuroscience 2005, 134, 1223-1245.
  • 11. Khaperskyy D. A., Hatchette T. F., McCormick C.: Influenza a virus inhibits cytoplasmic stress granule formation. FASEB J. 2011, 26, 1629-1639.
  • 12. Legros S., Boxus M., Gatot J. S., Van Lint C., Kruys V., Kettmann R., Twizere J. C., Dequiedt F.: The HTLV-1 Tax protein inhibits formation of stress granules by interacting with histone deacetylase 6. Oncogene 2011, 30, 4050-4062.
  • 13. Li W., Li Y., Kedersha N., Anderson P., Emara M., Swiderek K. M., Moreno G. T., Brinton M. A.: Cell proteins TIA-1 and TIAR interact with the 3º stemloop of the West Nile virus complementary minus-strand RNA and facilitate virus replication. J. Virol. 2002, 76, 11989-12000.
  • 14. Moeller B. J., Cao Y., Li C. Y., Dewhirst M. W.: Radiation activates HIF-1 to regulate vascular radiosensivity in tumors: role of reoxygenation, free radicals, and stress granules. Cancer Cell 2004, 5, 429-441.
  • 15. Mok B., Song W.-Y., Wang P., Tai H., Chen Y., Zheng M., Wen X., Lau S.-Y., Wu W. L., Matsumoto K., Yuen K.-Y., Chen H.: The NS1 protein of influenza virus interacts with cellular processing bodies (P-bodies) and stress granules through RNA-associated protein 55 (RAP55) during virus infection. J. Virol. 2012, 86, 12695-12707.
  • 16. Monani U. R.: Spinal muscular atrophy: a deficiency in a ubiquitous protein; a motor neuron-specific disease. Neuron 2005, 48, 885-896.
  • 17. Montero H., Rojas M., Arias C. F., López S.: Rotavirus infection induces the phosporylation of eIF2alpha but prevents the formation of stress granules. J. Virol. 2008, 82, 1496-1504.
  • 18. Reineke L. C., Lloyd R. E.: Diversion of stress granules and P-bodies during viral infection. Virology 2013, 436, 255-267.
  • 19. Smith J. A., Schmechel S. C., Raghavan A., Abelson M., Reilly C., Katze M. G., Kaufman R. J., Bohjanen P. R., Schiff L. A.: Reovirus induces and benefits from an integrated cellular stress response. J. Virol. 2006, 80, 2019-2033.
  • 20. Takahara T., Maeda T.: Transient sequestration of TORC1 into stress granules during heat stress. Mol. Cell. 2012, 47, 242-252.
  • 21. Valiente-Echeverría F., Melnychuk L., Mouland A. J.: Viral modulation of stress granules. Vir. Res. 2012, 169, 430-437.
  • 22. White J. P., Cardenas A. M., Marissen W. E., Lloyd R. E.: Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase. Cell Host Microbe 2007, 2, 295-305.
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
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