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@ARTICLE{Albus:904302,
      author       = {Albus, Alexandra and Kronimus, Yannick and Neumann, Sascha
                      and Vidovic, Natascha and Frenzel, André and Kuhn, Philipp
                      and Seifert, Marc and Ziehm, Tamar and van der Wurp, Hendrik
                      and Dodel, Richard},
      title        = {{E}ffects of a {M}ultimerized {R}ecombinant {A}utoantibody
                      {A}gainst {A}myloid-β},
      journal      = {Neuroscience},
      volume       = {463},
      issn         = {0306-4522},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {FZJ-2021-05872},
      pages        = {355 - 369},
      year         = {2021},
      abstract     = {Alzheimer's disease (AD) is the most common
                      neurodegenerative disease; thus, the search for a cure or
                      causal therapy has become necessary. Despite intense
                      research on this topic in recent decades, there is no
                      curative therapy up today, and also no disease-modifying
                      treatment has been approved. As promising approach passive
                      immunization strategies have thereby come forth. In this
                      study, we focused on naturally occurring autoantibodies
                      against the AD-associated peptide amyloid-β. These
                      antibodies have already reported to show beneficial
                      functions in vitro and in mouse models of AD. However, their
                      availability is limited due to their low abundance in
                      peripheral blood. In a recent study, we were able to
                      generate four recombinant antibodies against amyloid-β. In
                      the present study, we tested these antibodies in ELISA and
                      SPR assays for their binding behavior and by aggregation-
                      and phagocytosis assays as functional evidences to
                      characterize their amyloid-β-related neutralizing and
                      clearance abilities. Further ex vivo assay on organotypic
                      hippocampal slice cultures gave first evidence of microglial
                      activation and inflammatory features. The tested recombinant
                      antibodies in IgG format showed, in comparison to naturally
                      occurring autoantibodies against amyloid-β, insufficient
                      binding capacities and -affinities. However, after
                      conversion of one antibody into a single chain format
                      multimerization of the scFv-Fc construct, the investigated
                      binding capacity and -affinity showed improvements. Further
                      functional assays predict a protective effect of this
                      antibody. Although, all four recombinant antibodies showed
                      binding to amyloid-β, promising features were only
                      detectable after conversion into a multimeric format. The
                      multimeric scFv-Fc antibody exhibited thereby strong impact
                      on amyloid-β clearance and inhibition of oligomerization.},
      cin          = {IBI-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {33958140},
      UT           = {WOS:000647661600010},
      doi          = {10.1016/j.neuroscience.2021.03.006},
      url          = {https://juser.fz-juelich.de/record/904302},
}