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@ARTICLE{Braczynski:906834,
      author       = {Braczynski, Anne K. and Sevenich, Marc and Gering, Ian and
                      Kupreichyk, Tatsiana and Agerschou, Emil D. and Kronimus,
                      Yannick and Habib, Pardes and Stoldt, Matthias and Willbold,
                      Dieter and Schulz, Jörg B. and Bach, Jan-Philipp and
                      Falkenburger, Björn H. and Hoyer, Wolfgang},
      title        = {{A}lpha-{S}ynuclein-{S}pecific {N}aturally {O}ccurring
                      {A}ntibodies {I}nhibit {A}ggregation {I}n {V}itro and {I}n
                      {V}ivo},
      journal      = {Biomolecules},
      volume       = {12},
      number       = {3},
      issn         = {2218-273X},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2022-01728},
      pages        = {469 -},
      year         = {2022},
      abstract     = {Parkinson’s disease (PD) is associated with motor and
                      non-motor symptoms and characterized by aggregates of
                      alpha-synuclein (αSyn). Naturally occurring antibodies
                      (nAbs) are part of the innate immune system, produced
                      without prior contact to their specific antigen, and
                      polyreactive. The abundance of nAbs against αSyn is altered
                      in patients with PD. In this work, we biophysically
                      characterized nAbs against αSyn (nAbs-αSyn) and determined
                      their biological effects. nAbs-αSyn were isolated from
                      commercial intravenous immunoglobulins using column affinity
                      purification. Biophysical properties were characterized
                      using a battery of established in vitro assays. Biological
                      effects were characterized in HEK293T cells transiently
                      transfected with fluorescently tagged αSyn. Specific
                      binding of nAbs-αSyn to monomeric αSyn was demonstrated by
                      Dot blot, ELISA, and Surface Plasmon Resonance. nAbs-αSyn
                      did not affect viability of HEK293T cells as reported by
                      Cell Titer Blue and LDH Assays. nAbs-αSyn inhibited
                      fibrillation of αSyn reported by the Thioflavin T
                      aggregation assay. Altered fibril formation was confirmed
                      with atomic force microscopy. In cells transfected with
                      EGFP-tagged αSyn we observed reduced formation of
                      aggresomes, perinuclear accumulations of αSyn aggregates.
                      The results demonstrate that serum of healthy individuals
                      contains nAbs that specifically bind αSyn and inhibit
                      aggregation of αSyn in vitro. The addition of nAbs-αSyn to
                      cultured cells affects intracellular αSyn aggregates. These
                      findings help understanding the role of the innate immune
                      systems for the pathogenesis of PD and suggest that systemic
                      αSyn binding agents could potentially affect neuronal αSyn
                      pathology.},
      cin          = {IBI-7 / INM-11},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-7-20200312 / I:(DE-Juel1)INM-11-20170113},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:35327661},
      UT           = {WOS:000775905700001},
      doi          = {10.3390/biom12030469},
      url          = {https://juser.fz-juelich.de/record/906834},
}