Inhibition of PKR phosphorylation by Vaccinia Virus' E3 Protein PKR interaction mapped to a region within the dsRNA-binding domain of E3 and overlapped with sequences in the C-terminus of this domain that are necessary for binding to dsRNA. Point mutants of E3 were generated and screened for PKR inhibition and direct interaction. Analysis of these mutants demonstrates that dsRNA-binding but not PKR interaction plays a critical role in the broad host range of VACV. Nonetheless, full inhibition of PKR in cells in culture requires both dsRNA-binding and PKR interaction. Because E3 is highly conserved among orthopoxviruses, understanding the mechanisms that E3 uses to inhibit PKR can give insight into host range pathogenesis of dsRNA producing viruses.]]>cauFoster, ClaytoncauAlattar, HamedthsJacobs, BertramdgcBlattman, JosephdgcMcFadden, GrantctbSchool of Life SciencesctbW. P. Carey School of BusinessctbDepartment of PsychologyctbBarrett, The Honors Collegeenghttps://hdl.handle.net/2286/R.I.4344127 pages115093930581628716197134414halattarIn Copyright2017-05TextMicrobiologyVirologyImmunology