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| Hauptseite > Publikationsdatenbank > Rational design of structure‐based vaccines targeting misfolded alpha‐synuclein conformers of Parkinson's disease and related disorders > print |
| Hauptseite > Publikationsdatenbank > Rational design of structure‐based vaccines targeting misfolded alpha‐synuclein conformers of Parkinson's disease and related disorders > print |
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| 100 | 1 | _ | |a Flores-Fernandez, Jose Miguel |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Rational design of structure‐based vaccines targeting misfolded alpha‐synuclein conformers of Parkinson's disease and related disorders |
| 260 | _ | _ | |a Hoboken, NJ |c 2024 |b Wiley |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a Synucleinopathies, including Parkinson's disease (PD), multiple system atrophy (MSA), and dementia with Lewy bodies (DLB), are neurodegenerative disorders caused by the accumulation of misfolded alpha-synuclein protein. Developing effective vaccines against synucleinopathies is challenging due to the difficulty of stimulating an immune-specific response against alpha-synuclein without causing harmful autoimmune reactions, selectively targeting only pathological forms of alpha-synuclein. Previous attempts using linear peptides and epitopes without control of the antigen structure failed in clinical trials. The immune system was unable to distinguish between native alpha-synuclein and its amyloid form. The prion domain of the fungal HET-s protein was selected as a scaffold to introduce select epitopes from the surface of alpha-synuclein fibrils. Four vaccine candidates were generated by introducing specific amino acid substitutions onto the surface of the scaffold protein. The approach successfully mimicked the stacking of the parallel in-register beta-sheet structure seen in alpha-synuclein fibrils. All vaccine candidates induced substantial levels of IgG antibodies that recognized pathological alpha-synuclein fibrils derived from a synucleinopathy mouse model. Furthermore, the antisera recognized pathological alpha-synuclein aggregates in brain lysates from patients who died from DLB, MSA, or PD, but did not recognize linear alpha-synuclein peptides. Our approach, based on the rational design of vaccines using the structure of alpha-synuclein amyloid fibrils and strict control over the exposed antigen structure used for immunization, as well as the ability to mimic aggregated alpha-synuclein, provides a promising avenue toward developing effective vaccines against alpha-synuclein fibrils. |
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| 700 | 1 | _ | |a Tamgüney, Gültekin |0 P:(DE-Juel1)177986 |b 12 |e Corresponding author |
| 700 | 1 | _ | |a Wille, Holger |0 P:(DE-HGF)0 |b 13 |
| 773 | _ | _ | |a 10.1002/btm2.10665 |g Vol. 9, no. 4, p. e10665 |0 PERI:(DE-600)2865162-5 |n 4 |p e10665 |t Bioengineering & translational medicine |v 9 |y 2024 |x 2380-6761 |
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