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  • Erratum
  • Open Access

Erratum to: Do anti-amyloid beta protein antibody cross reactivities confound Alzheimer disease research?

Journal of Negative Results in BioMedicine201716:8

  • Published:

The original article was published in Journal of Negative Results in BioMedicine 2017 16:1


After publication of the original article [1], it came to the authors’ attention that evidence relating to the epitopes recognised and cross reactivities of the antibodies that form the parents of Bapineuzumab and Solanezumab was omitted from Table 1.
Table 1

Epitopes and cross reactivities of selected antibodies raised against Aβ



Cross Reactivity



Raised against synthetic peptide Aβ17-24; epitope lies within aa 18–23; recognises multiple forms of Aβ

Cross reacts with APP770 and P3; reacts with conformational epitope of aggregated fibrils including α-synuclein



Raised against Aβ1-17; epitope lies within aa 4–9; recognises Aβ with intact N-terminal epitope

Cross reacts with APP and Aβ(1–16); No reaction predicted with P3

[2, 5]


Raised against synthetic peptide Aβ8-17; epitope lies within aa 10–15; recognises Aβ with intact N-terminal epitope

Predicted to react with Aβ(1–16); Does not react with P3

[2, 6]



Recognises C-terminal Aβ peptides ending at aa40; epitope not well described

Cross reacts with N-terminal truncated peptides including P3




Recognises C-terminal Aβ peptides ending at aa42; epitope not well described

Cross reacts with N-terminal truncated peptides including P3



Raised against Aβ(25–35); recognises Aβ38, Aβ39, Aβ40, Aβ42 and Aβ43; epitope not well described

Cross reacts with N-terminal truncated peptides including P3



Raised against Aβ(35–43); recognises Aβ42 and Aβ43; epitope not well described

Cross reacts with N-terminal truncated peptides including P3; does not recognise Aβ40; used in commercial ELISA kits for the detection of Aβ42

[7, 8]


Raised against Aβ(1–40) Recognises Aβ40; 100-1000x more reactive with Aβ40 than Aβ42 and Aβ43; epitope not well described

Cross reacts with N-terminal truncated peptides including P3; used in commercial ELISA kits for the detection of Aβ40




Raised against P3(40); recognises P3(40) and synthetic P3(42) peptide; epitope not well described

Reactivity with insoluble, aggregated P3(42) not confirmed

[7, 9, 10]


Raised against Aβ with N-terminal aspartic acid; epitope lies within aa 1–5; recognises multiple C-terminal variations

Does not cross react with sAPPs or full length APP; No reactivity with N-terminally altered Aβ; No reaction predicted with P3; parent of Bapineuzumab



Raised against synthetic Aβ; epitope lies within aa 13–28; recognises soluble monomer and multiple C-terminal variations

Cross reacts with various plasma proteins containing the core sequence KLVFF; does not cross react with P3; parent of Solanezumab


An updated version of Table 1 is published in this erratum, with the inclusion of three new references [1214].

This evidence do not in any way undermine the argument that the cross-reactivities of anti-amyloid antibodies may confound research, and in fact can be interpreted as strengthening the argument.

The cross-reactivity of both Bapineuzumab and Solanezumab with various Aβ C-terminals and the cross reactivity of Solanezumab with various plasma proteins does not clarify the understanding of the APP proteolytic system and its role in disease, or identify with any certainty which peptides are of interest and are being targeted.



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Authors’ Affiliations

Department of Public Health and Primary Care, Institute of Public Health Forvie Site, University of Cambridge School of Clinical Medicine, Box 113 Cambridge Biomedical Campus, Cambridge, CB2 0SP, UK


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© The Author(s). 2017