Our findings thus demonstrate that IL-6 plays a major role in EV71-induced immunopathogenesis. As there is still neither vaccine nor treatment available against EV71, anti-IL-6 antibody treatment represents a potential therapeutic approach to providing protection from the most severe complications of the disease.”
“Recent studies have shown that
audiovisual synchrony is recalibrated after exposure to asynchronous auditory and visual signals. This temporal recalibration Pexidartinib has been shown only under a dual-task situation for speech signals. Here we examined whether the temporal recalibration occurs for audiovisual speech in a single-task situation using an offline adaptation method. In the experiment, participants were exposed to synchronous or asynchronous audiovisual syllables (either congruent or incongruent) for 3 min. The adaptation phase was followed by test trials, in which participants judged whether the auditory or visual
stimulus was presented first. Results showed shifts in the point of subjective simultaneity and the sensitivity. Our results suggest that attention to adaptation stimuli is necessary to induce temporal recalibration for speech. NeuroReport 22:684-688 (C) 2011 Wolters Kluwer Health | Lippincott Williams & Wilkins.”
“Infection by prions involves conversion of a host-encoded cell surface protein (PrPC) to a disease-related isoform (PrPSc). PrPC carries two glycosylation sites variably occupied Tideglusib this website by complex N-glycans, which have been suggested by previous studies to influence the susceptibility to these diseases and to determine characteristics of prion strains. We used the Rov cell system, which is susceptible to sheep prions, to generate a series of PrPC glycosylation mutants with mutations at one or both attachment sites. We examined their subcellular trafficking and ability to convert into PrPSc and to sustain stable prion propagation in the absence of wild-type PrP. The susceptibility to infection of mutants monoglycosylated at either site differed dramatically
depending on the amino acid substitution. Aglycosylated double mutants showed overaccumulation in the Golgi compartment and failed to be infected. Introduction of an ectopic glycosylation site near the N terminus fully restored cell surface expression of PrP but not convertibility into PrPSc, while PrPC with three glycosylation sites conferred cell permissiveness to infection similarly to the wild type. In contrast, predominantly aglycosylated molecules with nonmutated N-glycosylation sequons, produced in cells expressing glycosylphosphatidylinositol-anchorless PrPC, were able to form infectious PrPSc. Together our findings suggest that glycosylation is important for efficient trafficking of anchored PrP to the cell surface and sustained prion propagation.