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Mol Immunol. 2009 Jul;46(11-12):2267-73. doi: 10.1016/j.molimm.2009.04.007. Epub 2009 May 17.

Specific recognition of the C-terminal end of A beta 42 by a high affinity monoclonal antibody.

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  • 1Clinical Institute, The Faculty of Health Science, Aarhus University, Brendstrupg√•rdsvej 100, 8200 Arhus N, Denmark. trine@loke.dk

Abstract

The neurotoxic peptide A beta(42) is derived from the amyloid precursor protein by proteolytic cleavage and is deposited in the brain of patients suffering from Alzheimer's disease (AD). In this study we generate a high affinity monoclonal antibody that targets the C-terminal end of A beta(42) with high specificity. By this is meant that the paratope of the antibody must enclose the C-terminal end of A beta(42) including the carboxy-group of amino acid 42, and not just recognize a linear epitope in the C-terminal part of A beta. This has been accomplished by using a unique antigen construct made by the Ligand Presenting Assembly technology (LPA technology). This strategy results in dimeric presentation of the free C-terminal end of A beta(42). The generated Mab A beta1.1 is indeed specific for the C-terminal end of A beta(42) to which it binds with high affinity. Mab A beta1.1 recognizes the epitope in human AD tissue and stains plaques with high specificity. Therefore the monoclonal antibody can thus be useful in the histological investigations of the AD pathology.

PMID:
19447496
[PubMed - indexed for MEDLINE]
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