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@ARTICLE{Muhs:60181,
author = {Muhs, A. and Hickmann, D.T. and Pihlgren, M. and Chuard, N.
and Giriens, V. and Meerschman, C. and van der Auwera, I.
and van Leuven, F. and Sugawara, M. and Weingertner, M.C.
and Bechinger, B. and Greferath, R. and Kolonko, N. and
Nagel-Steger, L. and Riesner, D. and Brady, R.O. and
Pfeifer, A. and Nicolau, C.},
title = {{L}iposomal vaccines with conformation-specific amyloid
peptide antigens define immune response and efficacy in
{APP} transgenic mice},
journal = {Proceedings of the National Academy of Sciences of the
United States of America},
volume = {104},
issn = {0027-8424},
address = {Washington, DC},
publisher = {Academy},
reportid = {PreJuSER-60181},
pages = {9810 - 9815},
year = {2007},
note = {Record converted from VDB: 12.11.2012},
abstract = {We investigated the therapeutic effects of two different
versions of Abeta(1-15 (16)) liposome-based vaccines.
Inoculation of APP-V717IxPS-1 (APPxPS-1) double-transgenic
mice with tetra-palmitoylated amyloid 1-15 peptide
(palmAbeta(1-15)), or with amyloid 1-16 peptide
(PEG-Abeta(1-16)) linked to a polyethyleneglycol spacer at
each end, and embedded within a liposome membrane, elicited
fast immune responses with identical binding epitopes.
PalmAbeta(1-15) liposomal vaccine elicited an immune
response that restored the memory defect of the mice,
whereas that of PEG-Abeta(1-16) had no such effect.
Immunoglobulins that were generated were predominantly of
the IgG class with palmAbeta(1-15), whereas those elicited
by PEG-Abeta(1-16) were primarily of the IgM class. The IgG
subclasses of the antibodies generated by both vaccines were
mostly IgG2b indicating noninflammatory Th2 isotype. CD and
NMR revealed predominantly beta-sheet conformation of
palmAbeta(1-15) and random coil of PEG-Abeta(1-16). We
conclude that the association with liposomes induced a
variation of the immunogenic structures and thereby
different immunogenicities. This finding supports the
hypothesis that Alzheimer's disease is a "conformational"
disease, implying that antibodies against amyloid sequences
in the beta-sheet conformation are preferred as potential
therapeutic agents.},
keywords = {Alzheimer Disease: prevention $\&$ control / Alzheimer
Vaccines: immunology / Alzheimer Vaccines: pharmacology /
Amyloid beta-Peptides: immunology / Amyloid beta-Peptides:
metabolism / Amyloid beta-Protein Precursor: genetics /
Analysis of Variance / Animals / Antigens: immunology /
Brain: immunology / Brain: metabolism / Cytokines:
metabolism / Enzyme-Linked Immunosorbent Assay / Epitope
Mapping / Liposomes: immunology / Mice / Mice, Transgenic /
Nuclear Magnetic Resonance, Biomolecular / Oligopeptides:
genetics / Peptide Fragments: immunology / Recognition
(Psychology): drug effects / Alzheimer Vaccines (NLM
Chemicals) / Amyloid beta-Peptides (NLM Chemicals) / Amyloid
beta-Protein Precursor (NLM Chemicals) / Antigens (NLM
Chemicals) / Cytokines (NLM Chemicals) / Liposomes (NLM
Chemicals) / Oligopeptides (NLM Chemicals) / PS1 antigen
(NLM Chemicals) / Peptide Fragments (NLM Chemicals) / J
(WoSType)},
cin = {INB-2},
ddc = {000},
cid = {I:(DE-Juel1)VDB805},
pnm = {Funktion und Dysfunktion des Nervensystems},
pid = {G:(DE-Juel1)FUEK409},
shelfmark = {Multidisciplinary Sciences},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:17517595},
pmc = {pmc:PMC1887581},
UT = {WOS:000247114100049},
doi = {10.1073/pnas.0703137104},
url = {https://juser.fz-juelich.de/record/60181},
}