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- W2089898616 abstract "Misfolding of the naturally unfolded protein Tau causes its aggregation into fibrils of as yet unknown structure. The aggregates form neurofibrillary tangles in neuronal somata and neuropil threads in neuronal processes, constituting the typical post-mortem pathological signature in primary tauopathies. In Alzheimer's disease (AD), tau pathology is presumed secondary to amyloid pathology, but their respective roles and relative contributions to AD remain open for analysis and debate. Therapeutic approaches have yet to prove their specificity and efficacy, emphasizing the need for additional treatment options, including immunotherapy. Experimental studies of tau-based immunotherapy must demonstrate that this strategy can alleviate the pathological impact of Tau. Moreover, such studies will contribute to unravel the function and role of Tau in normal and in pathological physiology. We designed, generated and explored experimentally in vivo, different liposome-based vaccines (Muhs et al., 2007) carrying phospho-peptides that cover important “patho-topes” of Tau. TauP301L mice were immunized and the specificity of their polyclonal antisera responses analyzed biochemically and immunohistochemically (TAUPIR). Vaccine efficacy was defined by clinical and pathological read-outs. Liposome-based vaccines, displaying synthetic phospho-Tau peptides, elicited robust anti-phospho-Tau antibody responses (IgG/IgM) in wild-type and in Tau.P301L transgenic mice already after 2 immunizations. The polyclonal antisera specifically detected pathological tauopathy in brain of Tau.P301LxGSK3ß mice (biGT) with proven tauopathy (Terwel et al., 2008). Abundant labeling of neurofibrillary tangles and neuropil threads in hippocampus and cortex was corroborated biochemically by western blotting of mouse brain extracts and isolated hP-Tau preparations (Vandebroek et al., 2005). Specific ELISA with synthetic tau-derived peptides, with and without phosphorylation of specified S/T residues, demonstrated high affinity and specificity of the antisera for phospho-epitopes. After 3 months, immunized Tau.P301L mice presented with improved survival, delayed motor-impairment, reduced loss in body-weight and decreases in specified phospho-Tau species (human and mouse Tau). We demonstrate that synthetic phospho-Tau peptide liposomal vaccines elicited rapidly and robustly, phospho-tau specific antiserum responses. Under long-term regimes of vaccination the novel vaccines reduced protein tau-related pathological parameters and improved clinical condition and survival of Tau.P301L mice, without obvious side-effects." @default.
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- W2089898616 date "2011-07-01" @default.
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- W2089898616 title "O4-03-04: Novel phospho-tau-specific liposome-based vaccines to treat tau pathology" @default.
- W2089898616 doi "https://doi.org/10.1016/j.jalz.2011.05.1983" @default.
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