Antiviral Mechanisms of the 2'-5' Oligoadenylate Synthetases: Novel and Classical Antiviral Activities

Publikation: Bog/antologi/afhandling/rapportPh.d.-afhandlingForskning

  • Helle Kristiansen, Danmark
The 2'-5' Oligoadenylate Synthetases (OAS) are a family of IFN-induced proteins, which possess antiviral activity against viruses such as EMCV, WNV and CHIKV. The classical antiviral mechanism of these proteins is mediated through RNase L. RNase L is a potent RNase, which is activated by the 2-5As synthesised by OAS. OAS synthesises 2-5As after recognition of dsRNA, which is typically found during a viral infection. 2-5As are oligoadenylates, which are linked by a phosphodiester bond between the 2' C and the 5' C of the ribose. This unique bond enables RNase L to distinguish these nucleotides from 3'-5' linked nucleotides (RNA and DNA). RNase L binds the 2-5As, which in turn activates this enzyme. Upon activation, RNase L degrades viral and cellular RNA, inhibiting further viral growth in the cell.
However, a number of the OAS proteins also possess an alternative mechanism of viral inhibition, which is independent of the 2-5A activity and of RNase L. In this thesis, I have investigated the novel antiviral activity of OAS1.
OriginalsprogEngelsk
ForlagAarhus University, Faculty of Science and Technology
Antal sider178
Rekvirerende organGraduate School of Science and Technology
StatusUdgivet - 30 nov. 2012

Note vedr. afhandling

Dato for forsvar 0803-2013

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