The Ninth Biennial All-iowa Virology Symposium

نویسندگان

  • Helen C. Levitt
  • Prem S. Paul
  • Brad Blitvich
  • Promisree Choudhury
  • Cathy L. Miller
چکیده

1. Stress Granule Modulation by Mammalian Orthoreovirus Factories Promisree Choudhury and Cathy L. Miller Department of Veterinary Microbiology and Preventive Medicine, Iowa State University Phosphorylation of eIF2α induces formation of discrete cytoplasmic inclusions called stress granules (SG). SGs are comprised of translationaly silenced mRNAs, translation initiation factors, ribosomal proteins, and SG effector proteins such as TIA-1, TIAR, G3BP1 and G3BP2. Emerging evidence suggests that SGs are the site of activation of proteins critical in the innate immune response to virus infection, such as PKR and RIG-I. MRV entry into cells induces SG formation, however, as virus gene products are synthesized, SGs are disrupted even in the presence of phosphorylated eIF2α, suggesting MRV is able to disrupt virus-induced SGs in a manner dependent on new viral protein translation. In this work, we sought to determine the mechanism of MRV mediated SG modulation. Our results demonstrate that in many infected cells, SG effector proteins display localization peripheral to virus encoded structures termed viral factories (VFs) that are formed during MRV infection and facilitate viral transcription, translation, replication and assembly. In transfected cells, localization of SG proteins around VF-like structures (VFLs), formed solely by MRV μNS, was not detected. However, addition of non-structural protein σNS resulted in strong recruitment of G3BP1, G3BP2, Caprin1 and USP10 to VFLs. Moreover, σNS associated with G3BP1 in an immunoprecipitated protein complex either in the presence or absence of μNS. SG formation was not necessary for localization of SG proteins to VFLs, but VFLs containing σNS were able to inhibit SGs induced by the cellular stressor sodium arsenite, suggesting σNS dual association with G3BP1 and μNS may prevent SG formation during MRV infection. Localization of G3BP1 to VFLs was dependent on RNA binding domains of both σNS and G3BP1, as well as eIF2α phosphorylation and PKR activation. Moreover, replication of MRV was enhanced in cells lacking G3BP1, G3BP2 or both G3BP1/2. Taken together, our results implicate a key role of MRV VFs in SG modulation, mediated via the viral proteins μNS and σNS. These data suggest MRV factories may play an active role in disruption of the innate immune response to infection. 2. PARP-dependent ADP-ribosylation independently enhances the IFN response and represses coronavirus replication Anthony R. Fehr1, Gytis Jankevicius2, Craig Fett1, Ivan Ahel2 and Stanley Perlman1* 1Department of Microbiology, University of Iowa, Iowa City, IA 52242; 2Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1

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تاریخ انتشار 2017