Zinc binding agonist effect on the recognition of the β-amyloid (4–10) epitope by anti-β-amyloid antibodies
| Autor: | Séverine Zirah, Sergey A. Kozin, Roxana Cecal, Sylvie Rebuffat, Raluca Stefanescu, Xiaodan Tian, Marilena Manea, Pascale Debey, Michael Przybylski |
|---|---|
| Přispěvatelé: | Laboratoire de chimie et biochimie des substances naturelles, Centre National de la Recherche Scientifique (CNRS)-Muséum national d'Histoire naturelle (MNHN), University of Konstanz, Régulation et dynamique des génomes, Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Muséum national d'Histoire naturelle (MNHN)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2004 |
| Předmět: |
Conformational change
Amyloid medicine.drug_class Biophysics Enzyme-Linked Immunosorbent Assay Peptide Monoclonal antibody Biochemistry Antibodies Epitope Epitopes 03 medical and health sciences 0302 clinical medicine medicine Molecular Biology ComputingMilieux_MISCELLANEOUS 030304 developmental biology chemistry.chemical_classification 0303 health sciences Amyloid beta-Peptides Linear epitope biology P3 peptide Cell Biology Molecular biology 3. Good health [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM] Zinc chemistry Metals biology.protein Antibody 030217 neurology & neurosurgery [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology |
| Zdroj: | Biochemical and Biophysical Research Communications Biochemical and Biophysical Research Communications, Elsevier, 2004, 321 (2), pp.324-328. ⟨10.1016/j.bbrc.2004.06.150⟩ Biochemical and Biophysical Research Communications, Elsevier, 2004, 321, pp.324-328 |
| ISSN: | 0006-291X 1090-2104 |
| DOI: | 10.1016/j.bbrc.2004.06.150⟩ |
| Popis: | Amyloid plaques associated to Alzheimer's disease present a high content of zinc ions. We previously showed that the N-terminal region of the amyloid peptide Abeta constitutes an autonomous zinc-binding domain. This region encompasses the previously identified epitope Abeta(4-10) targeted by antibodies capable to reduce amyloid deposition, but the influence of Abeta/Zn binding on the epitope recognition remains unknown. We demonstrate here the effect of Zn2+ ions on the recognition of peptides sharing the sequence of the Abeta N-terminal domain, by two monoclonal antibodies recognizing the beta-amyloid(4-10) epitope. The presence of Zn2+, but not of other cations, increased the recognition of the (1-16) peptide, while it was without effect on the recognition of the (1-10) peptide. These findings show a zinc-induced conformational change of the (1-16)-N-terminal region of AP3, which results in a better accessibility of the Abeta(4-10) epitope to the anti-Abeta antibodies, and suggest a role of zinc in epitope-based vaccination approaches. |
| Databáze: | OpenAIRE |
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