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- W2893090986 abstract "The unfolded protein response (UPR) is an ancient cellular response to ER stress that is of broad importance to viruses. Certain consequences of the UPR, including mRNA degradation and translational shutoff, would presumably be disadvantageous to viruses, while other attributes of the UPR, such as ER expansion and upregulation of protein folding chaperones, might enhance viral replication. Although HCMV is estimated to express well over 150 different viral proteins, we show that the HCMV ER-resident glycoprotein UL148 contributes substantially to the UPR during infection and, moreover, is sufficient to activate the UPR in noninfected cells. Experimental activation of the UPR in mammalian cells is difficult to achieve without the use of toxins. Therefore, UL148 may provide a new tool to investigate fundamental aspects of the UPR. Furthermore, our findings may have implications for understanding the mechanisms underlying the effects of UL148 on HCMV cell tropism and evasion of cell-mediated immunity." @default.
- W2893090986 created "2018-10-05" @default.
- W2893090986 creator A5006646838 @default.
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- W2893090986 date "2018-10-15" @default.
- W2893090986 modified "2023-10-11" @default.
- W2893090986 title "The Human Cytomegalovirus Endoplasmic Reticulum-Resident Glycoprotein UL148 Activates the Unfolded Protein Response" @default.
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- W2893090986 doi "https://doi.org/10.1128/jvi.00896-18" @default.
- W2893090986 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6158444" @default.
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