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- W4313359612 abstract "Abstract Cathepsins belong to cysteine proteases and play essential roles in processing of internalized peptides during antigen presentation in the context of the major histocompatibility complex (MHC) class II molecules. Function of cathepsins is regulated by cystatins – endogenous protein inhibitors. Viruses, such as poxviruses, have evolved many mechanisms to escape immune responses after infection. Our studies are focused on ectromelia virus (ECTV, a poxvirus closely related to variola virus, VARV – a causative agent of smallpox), and its influence on cathepsins or cystatins. Our results show that ECTV down-regulates gene and protein expression of selected cathepsins and cystatins in infected murine JAWS II dendritic cells (DCs) and GM-CSF-derived bone marrow cells (GM-BM), composed of conventional DCs and macrophages. Moreover, the ability to endocytose and process a soluble antigen is reduced in JAWS II and GM-BM cells during ECTV infection. After knockdown of cathepsins and cystatins using siRNA in JAWS II DCs, the virus titer increases when compared with control cells. The inhibition of cathepsins and cystatins together with elevated virus titers during the absence of these proteases may be a viral strategy to escape immune responses and simultaneously enable the virus to replicate effectively in infected cells. Importantly, defining the poxvirus-host interactions, including lysosomal proteases, may lead to development of potential therapeutic targets or vaccination strategies." @default.
- W4313359612 created "2023-01-06" @default.
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- W4313359612 date "2018-05-01" @default.
- W4313359612 modified "2023-09-27" @default.
- W4313359612 title "Ectromelia virus suppresses cathepsins and cystatins expression at both mRNA and protein levels in dendritic cells" @default.
- W4313359612 doi "https://doi.org/10.4049/jimmunol.200.supp.126.21" @default.
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