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- W2083592045 abstract "Transfusion of blood and blood products contaminated with the pathogenic form of prion protein Prpsc, thought to be the causative agent of variant a Creutzfeldt–Jakob disease (vCJD), may result in serious consequences in recipients with a compromised immune system, for example, as seen in HIV-1 infection. In the present study, we demonstrate that treatment of peripheral blood monocyte-derived macrophages (MDM) with PrP106–126, a synthetic domain of PrPsc that has intrinsic functional activities related to the full-length protein, markedly increased their susceptibility to HIV-1 infection, induced cytokine secretion, and enhanced their migratory behavior in response to N-formyl-l-methionyl-l-leucyl-l-phenylalanine (fMLP). Live-cell imaging of MDM cultured in the presence of PrP106–126 showed large cell clusters indicative of cellular activation. Tyrosine kinase inhibitor STI-571, protein kinase C inhibitor K252B, and cyclin-dependent kinase inhibitor olomoucine attenuated PrP106–126-induced altered MDM functions. These findings delineate a previously undefined functional role of PrP106–126-mediated host cell response in promoting HIV-1 pathogenesis." @default.
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- W2083592045 date "2015-02-01" @default.
- W2083592045 modified "2023-09-27" @default.
- W2083592045 title "Pathogenic prion protein fragment (PrP106–126) promotes human immunodeficiency virus type-1 infection in peripheral blood monocyte-derived macrophages" @default.
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- W2083592045 doi "https://doi.org/10.1016/j.virol.2014.11.032" @default.
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