Do anti-amyloid beta protein antibody cross reactivities confound Alzheimer disease research? View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-12

AUTHORS

Sally Hunter, Carol Brayne

ABSTRACT

BACKGROUND: Alzheimer disease (AD) research has focussed mainly on the amyloid beta protein (Aβ). However, many Aβ-and P3-type peptides derived from the amyloid precursor protein (APP) and peptides thought to derive from Aβ catabolism share sequence homology. Additionally, conformations can change dependent on aggregation state and solubility leading to significant uncertainty relating to interpretations of immunoreactivity with antibodies raised against Aβ. We review evidence relating to the reactivities of commonly used antibodies including 6F3D, 6E10 and 4G8 and evaluate their reactivity profiles with respect to AD diagnosis and research. RESULTS: Antibody cross-reactivities between Aβ-type, P3-type and Aβ-catabolic peptides confound interpretations of immunoreactivity. More than one antibody is required to adequately characterise Aβ. The relationships between anti-Aβ immunoreactivity, neuropathology and proposed APP cleavages are unclear. CONCLUSIONS: We find that the concept of Aβ lacks clarity as a specific entity. Anti-Aβ antibody cross-reactivities lead to significant uncertainty in our understanding of the APP proteolytic system and its role in AD with profound implications for current research and therapeutic strategies. More... »

PAGES

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References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1186/s12952-017-0066-3

    DOI

    http://dx.doi.org/10.1186/s12952-017-0066-3

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1074202944

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/28126004


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        "description": "BACKGROUND: Alzheimer disease (AD) research has focussed mainly on the amyloid beta protein (A\u03b2). However, many A\u03b2-and P3-type peptides derived from the amyloid precursor protein (APP) and peptides thought to derive from A\u03b2 catabolism share sequence homology. Additionally, conformations can change dependent on aggregation state and solubility leading to significant uncertainty relating to interpretations of immunoreactivity with antibodies raised against A\u03b2. We review evidence relating to the reactivities of commonly used antibodies including 6F3D, 6E10 and 4G8 and evaluate their reactivity profiles with respect to AD diagnosis and research.\nRESULTS: Antibody cross-reactivities between A\u03b2-type, P3-type and A\u03b2-catabolic peptides confound interpretations of immunoreactivity. More than one antibody is required to adequately characterise A\u03b2. The relationships between anti-A\u03b2 immunoreactivity, neuropathology and proposed APP cleavages are unclear.\nCONCLUSIONS: We find that the concept of A\u03b2 lacks clarity as a specific entity. Anti-A\u03b2 antibody cross-reactivities lead to significant uncertainty in our understanding of the APP proteolytic system and its role in AD with profound implications for current research and therapeutic strategies.", 
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