Skip to Main content Skip to Navigation
Journal articles

Single-domain antibodies recognize selectively small oligomeric forms of amyloid beta, prevent Abeta-induced neurotoxicity and inhibit fibril formation.

Abstract : Neurotoxic oligomers of amyloid beta (Abeta) peptide have been incriminated in the pathogenesis of Alzheimer's disease. Further exploration of this issue has been hampered to this date by the fact that all previously described anti-Abeta antibodies are unable to discriminate between the different conformations of the peptide (oligomers, protofibrils and fibrils). Here, we describe the generation of novel camelid single-chain binding domains (VHHs) that recognizes specifically low molecular-weight (MW) oligomers. Three VHH specific for Abeta were obtained from an immunized alpaca phage display library. Two were able to recognize selectively intraneuronal Abeta oligomers; furthermore, one of them, V31-1, prevented Abeta-induced neurotoxicity and inhibited fibril formation. This study confirms that VHHs may recognize non-conventional epitopes and illustrates their potential for the immunodiagnostic of diseases due to protein accumulation.
Document type :
Journal articles
Complete list of metadatas

Cited literature [42 references]  Display  Hide  Download

https://hal-pasteur.archives-ouvertes.fr/pasteur-00429629
Contributor : Pierre Lafaye <>
Submitted on : Tuesday, November 3, 2009 - 4:55:29 PM
Last modification on : Wednesday, June 17, 2020 - 6:18:02 PM
Long-term archiving on: : Saturday, November 26, 2016 - 1:29:47 PM

File

 Restricted access
To satisfy the distribution rights of the publisher, the document is embargoed until : jamais

Please log in to resquest access to the document

Identifiers

Collections

Citation

Pierre Lafaye, Ikbel Achour, Patrick England, Charles Duyckaerts, François Rougeon. Single-domain antibodies recognize selectively small oligomeric forms of amyloid beta, prevent Abeta-induced neurotoxicity and inhibit fibril formation.. Molecular Immunology, Elsevier, 2009, 46 (4), pp.695-704. ⟨10.1016/j.molimm.2008.09.008⟩. ⟨pasteur-00429629⟩

Share

Metrics

Record views

169