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

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

Erratum

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

An updated version of Table 1 is published in this erratum, with the inclusion of three new references [12,13,14].

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.

References

  1. 1.

    Hunter S, Brayne C. Do anti-amyloid beta protein antibody cross reactivities confound Alzheimer disease research? J Negat Results Biomed. 2017;16:1. doi:10.1186/s12952-017-0066-3.

  2. 2.

    Thal DR, Schultz C, Dehghani F, Yamaguchi H, Braak H, Braak E. Amyloid beta-protein (Abeta)-containing astrocytes are located preferentially near N-terminal-truncated Abeta deposits in the human entorhinal cortex. Acta Neuropathol. 2000;100:608–17.

  3. 3.

    Hatami A, Monjazeb S, Glabe C. The Anti-Amyloid-beta Monoclonal Antibody 4G8 Recognizes a Generic Sequence-Independent Epitope Associated with alpha-Synuclein and Islet Amyloid Polypeptide Amyloid Fibrils. J Alzheimers Dis. 2015;50:517–25.

  4. 4.

    Hatami A, Albay 3rd R, Monjazeb S, Milton S, Glabe C. Monoclonal antibodies against Abeta42 fibrils distinguish multiple aggregation state polymorphisms in vitro and in Alzheimer disease brain. J Biol Chem. 2014;289:32131–43.

  5. 5.

    Moore S, Evans LD, Andersson T, Portelius E, Smith J, Dias TB, et al. APP metabolism regulates tau proteostasis in human cerebral cortex neurons. Cell Rep. 2015;11:689–96.

  6. 6.

    Thal DR, Sassin I, Schultz C, Haass C, Braak E, Braak H. Fleecy amyloid deposits in the internal layers of the human entorhinal cortex are comprised of N-terminal truncated fragments of Abeta. J Neuropathol Exp Neurol. 1999;58:210–6.

  7. 7.

    Iwatsubo T, Odaka A, Suzuki N, Mizusawa H, Nukina N, Ihara Y. Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: evidence that an initially deposited species is A beta 42(43). Neuron. 1994;13:45–53.

  8. 8.

    Citron M, Diehl TS, Gordon G, Biere AL, Seubert P, Selkoe DJ. Evidence that the 42- and 40-amino acid forms of amyloid beta protein are generated from the beta-amyloid precursor protein by different protease activities. Proc Natl Acad Sci U S A. 1996;93:13170–5.

  9. 9.

    Iwatsubo T, Saido TC, Mann DM, Lee VM, Trojanowski JQ. Full-length amyloid-beta (1-42(43)) and amino-terminally modified and truncated amyloid-beta 42(43) deposit in diffuse plaques. Am J Pathol. 1996;149:1823–30.

  10. 10.

    Saido TC, Yamao-Harigaya W, Iwatsubo T, Kawashima S. Amino- and carboxyl-terminal heterogeneity of beta-amyloid peptides deposited in human brain. Neurosci Lett. 1996;215:173–6.

  11. 11.

    Bouter Y, Lopez Noguerola JS, Tucholla P, Crespi GA, Parker MW, Wiltfang J, et al. Abeta targets of the biosimilar antibodies of Bapineuzumab, Crenezumab, Solanezumab in comparison to an antibody against Ntruncated Abeta in sporadic Alzheimer disease cases and mouse models. Acta Neuropathol. 2015;130:713–29.

  12. 12.

    Miles LA, Crespi GA, Doughty L, Parker MW. Bapineuzumab captures the N-terminus of the Alzheimer's disease amyloid-beta peptide in a helical conformation. Sci Rep. 2013;3:1302.

  13. 13.

    Watt AD, Crespi GA, Down RA, Ascher DB, Gunn A, Perez KA, et al. Do current therapeutic anti-Abeta antibodies for Alzheimer's disease engage the target? Acta Neuropathol. 2014;127:803–10.

  14. 14.

    Crespi GA, Hermans SJ, Parker MW, Miles LA. Molecular basis for mid-region amyloid-beta capture by leading Alzheimer's disease immunotherapies. Sci Rep. 2015;5:9649.

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Author information

Correspondence to Sally Hunter.

Additional information

The online version of the original article can be found under doi:10.1186/s12952-017-0066-3.

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Hunter, S., Brayne, C. Erratum to: Do anti-amyloid beta protein antibody cross reactivities confound Alzheimer disease research?. J Negat Results BioMed 16, 8 (2017) doi:10.1186/s12952-017-0073-4

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