Hauptseite > Publikationsdatenbank > Liposomal vaccines with conformation-specific amyloid peptide antigens define immune response and efficacy in APP transgenic mice > print

001     60181
005     20200402210440.0
024 7 _ |2 pmid
|a pmid:17517595
024 7 _ |2 pmc
|a pmc:PMC1887581
024 7 _ |2 DOI
|a 10.1073/pnas.0703137104
024 7 _ |2 WOS
|a WOS:000247114100049
024 7 _ |a altmetric:4971682
|2 altmetric
037 _ _ |a PreJuSER-60181
041 _ _ |a eng
082 _ _ |a 000
084 _ _ |2 WoS
|a Multidisciplinary Sciences
100 1 _ |a Muhs, A.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Liposomal vaccines with conformation-specific amyloid peptide antigens define immune response and efficacy in APP transgenic mice
260 _ _ |a Washington, DC
|b Academy
|c 2007
300 _ _ |a 9810 - 9815
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Proceedings of the National Academy of Sciences of the United States of America
|x 0027-8424
|0 5100
|y 23
|v 104
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a 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.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK409
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Alzheimer Disease: prevention & control
650 _ 2 |2 MeSH
|a Alzheimer Vaccines: immunology
650 _ 2 |2 MeSH
|a Alzheimer Vaccines: pharmacology
650 _ 2 |2 MeSH
|a Amyloid beta-Peptides: immunology
650 _ 2 |2 MeSH
|a Amyloid beta-Peptides: metabolism
650 _ 2 |2 MeSH
|a Amyloid beta-Protein Precursor: genetics
650 _ 2 |2 MeSH
|a Analysis of Variance
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Antigens: immunology
650 _ 2 |2 MeSH
|a Brain: immunology
650 _ 2 |2 MeSH
|a Brain: metabolism
650 _ 2 |2 MeSH
|a Cytokines: metabolism
650 _ 2 |2 MeSH
|a Enzyme-Linked Immunosorbent Assay
650 _ 2 |2 MeSH
|a Epitope Mapping
650 _ 2 |2 MeSH
|a Liposomes: immunology
650 _ 2 |2 MeSH
|a Mice
650 _ 2 |2 MeSH
|a Mice, Transgenic
650 _ 2 |2 MeSH
|a Nuclear Magnetic Resonance, Biomolecular
650 _ 2 |2 MeSH
|a Oligopeptides: genetics
650 _ 2 |2 MeSH
|a Peptide Fragments: immunology
650 _ 2 |2 MeSH
|a Recognition (Psychology): drug effects
650 _ 7 |0 0
|2 NLM Chemicals
|a Alzheimer Vaccines
650 _ 7 |0 0
|2 NLM Chemicals
|a Amyloid beta-Peptides
650 _ 7 |0 0
|2 NLM Chemicals
|a Amyloid beta-Protein Precursor
650 _ 7 |0 0
|2 NLM Chemicals
|a Antigens
650 _ 7 |0 0
|2 NLM Chemicals
|a Cytokines
650 _ 7 |0 0
|2 NLM Chemicals
|a Liposomes
650 _ 7 |0 0
|2 NLM Chemicals
|a Oligopeptides
650 _ 7 |0 0
|2 NLM Chemicals
|a PS1 antigen
650 _ 7 |0 0
|2 NLM Chemicals
|a Peptide Fragments
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a Alzheimer's disease
653 2 0 |2 Author
|a beta-amyloid
653 2 0 |2 Author
|a vaccine
700 1 _ |a Hickmann, D.T.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Pihlgren, M.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Chuard, N.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Giriens, V.
|b 4
|0 P:(DE-HGF)0
700 1 _ |a Meerschman, C.
|b 5
|0 P:(DE-HGF)0
700 1 _ |a van der Auwera, I.
|b 6
|0 P:(DE-HGF)0
700 1 _ |a van Leuven, F.
|b 7
|0 P:(DE-HGF)0
700 1 _ |a Sugawara, M.
|b 8
|0 P:(DE-HGF)0
700 1 _ |a Weingertner, M.C.
|b 9
|0 P:(DE-HGF)0
700 1 _ |a Bechinger, B.
|b 10
|0 P:(DE-HGF)0
700 1 _ |a Greferath, R.
|b 11
|0 P:(DE-HGF)0
700 1 _ |a Kolonko, N.
|b 12
|0 P:(DE-HGF)0
700 1 _ |a Nagel-Steger, L.
|b 13
|u FZJ
|0 P:(DE-Juel1)VDB72731
700 1 _ |a Riesner, D.
|b 14
|0 P:(DE-HGF)0
700 1 _ |a Brady, R.O.
|b 15
|0 P:(DE-HGF)0
700 1 _ |a Pfeifer, A.
|b 16
|0 P:(DE-HGF)0
700 1 _ |a Nicolau, C.
|b 17
|0 P:(DE-HGF)0
773 _ _ |a 10.1073/pnas.0703137104
|g Vol. 104, p. 9810 - 9815
|p 9810 - 9815
|q 104<9810 - 9815
|0 PERI:(DE-600)1461794-8
|t Proceedings of the National Academy of Sciences of the United States of America
|v 104
|y 2007
|x 0027-8424
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1887581
909 C O |o oai:juser.fz-juelich.de:60181
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914 1 _ |y 2007
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k INB-2
|l Molekulare Biophysik
|d 31.12.2008
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981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ISB-2-20090406
981 _ _ |a I:(DE-Juel1)ICS-6-20110106

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