832
Views
1
CrossRef citations to date
0
Altmetric
Editorial

What is the oligoadenylate synthetases-like protein and does it have therapeutic potential for influenza?

&

References

  • Bowie AG, Unterholzner L. Viral evasion and subversion of pattern-recognition receptor signalling. Nat Rev Immunol 2008;8(12):911-22
  • Fernandez-Sesma A. The influenza virus NS1 protein: inhibitor of innate and adaptive immunity. Infect Disord Drug Targets 2007;7(4):336-43
  • Zhu J, Zhang Y, Ghosh A, et al. Antiviral activity of human OASL protein is mediated by enhancing signaling of the RIG-I RNA sensor. Immunity 2014;40(6):936-48
  • Rouse BT, Sehrawat S. Immunity and immunopathology to viruses: what decides the outcome? Nat Rev Immunol 2010;10(7):514-26
  • Sadler AJ, Williams BR. Interferon-inducible antiviral effectors. Nat Rev Immunol 2008;8(7):559-68
  • Schoggins JW, Macduff DA, Imanaka N, et al. Pan-viral specificity of IFN-induced genes reveals new roles for cGAS in innate immunity. Nature 2014;505(7485):691-5
  • Mibayashi M, Martinez-Sobrido L, Loo YM, et al. Inhibition of retinoic acid-inducible gene I-mediated induction of beta interferon by the NS1 protein of influenza A virus. J Virol 2007;81(2):514-24
  • Pichlmair A, Schulz O, Tan CP, et al. RIG-I-mediated antiviral responses to single-stranded RNA bearing 5’-phosphates. Science 2006;314(5801):997-1001
  • Gack MU, Albrecht RA, Urano T, et al. Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I. Cell Host Microbe 2009;5(5):439-49
  • Talon J, Horvath CM, Polley R, et al. Activation of interferon regulatory factor 3 is inhibited by the influenza A virus NS1 protein. J Virol 2000;74(17):7989-96
  • Hale BG, Jackson D, Chen YH, et al. Influenza A virus NS1 protein binds p85beta and activates phosphatidylinositol-3-kinase signaling. Proc Natl Acad Sci USA 2006;103(38):14194-9
  • Stasakova J, Ferko B, Kittel C, et al. Influenza A mutant viruses with altered NS1 protein function provoke caspase-1 activation in primary human macrophages, resulting in fast apoptosis and release of high levels of interleukins 1beta and 18. J Gen Virol 2005;86(Pt 1):185-95
  • Kristiansen H, Gad HH, Eskildsen-Larsen S, et al. The oligoadenylate synthetase family: an ancient protein family with multiple antiviral activities. J Interferon Cytokine Res 2011;31(1):41-7
  • Sun L, Wu J, Du F, et al. Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type I interferon pathway. Science 2013;339(6121):786-91
  • Schoggins JW, Wilson SJ, Panis M, et al. A diverse range of gene products are effectors of the type I interferon antiviral response. Nature 2011;472(7344):481-5
  • Lee MS, Kim B, Oh GT, et al. OASL1 inhibits translation of the type I interferon-regulating transcription factor IRF7. Nat Immunol 2013;14(4):346-55
  • O’Neill LA, Bowie AG. The powerstroke and camshaft of the RIG-I antiviral RNA detection machine. Cell 2011;147(2):259-61
  • Peisley A, Wu B, Yao H, et al. RIG-I forms signaling-competent filaments in an ATP-dependent, ubiquitin-independent manner. Mol Cell 2013;51(5):573-83
  • Gack MU, Shin YC, Joo CH, et al. TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity. Nature 2007;446(7138):916-20
  • Zeng W, Sun L, Jiang X, et al. Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity. Cell 2010;141(2):315-30

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.