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Gantenerumab: A Novel Human Anti-Aβ Antibody Demonstrates Sustained Cerebral Amyloid-β Binding and Elicits Cell-Mediated Removal of Human Amyloid-β
Open accessAbstract
The amyloid-β lowering capacity of anti-Aβ antibodies has been demonstrated in transgenic models of Alzheimer's disease (AD) and in AD patients. While the mechanism of immunotherapeutic amyloid-β removal is controversial, antibody-mediated sequestration of peripheral Aβ versus microglial phagocytic activity and disassembly of cerebral amyloid (or a combination thereof) has been proposed. For successful Aβ immunotherapy, we hypothesized that high affinity antibody binding to amyloid-β plaques and recruitment of brain effector cells is required for most efficient amyloid clearance. Here we report the generation of a novel fully human anti-Aβ antibody, gantenerumab, optimized in vitro for binding with sub-nanomolar affinity to a conformational epitope expressed on amyloid-β fibrils using HuCAL(®) phage display technologies. In peptide maps, both N-terminal and central portions of Aβ were recognized by gantenerumab. Remarkably, a novel orientation of N-terminal Aβ bound to the complementarity determining regions was identified by x-ray analysis of a gantenerumab Fab-Aβ(1-11) complex. In functional assays gantenerumab induced cellular phagocytosis of human amyloid-β deposits in AD brain slices when co-cultured with primary human macrophages and neutralized oligomeric Aβ42-mediated inhibitory effects on long-term potentiation in rat brain. In APP751(swedish)xPS2(N141I) transgenic mice, gantenerumab showed sustained binding to cerebral amyloid-β and, upon chronic treatment, significantly reduced small amyloid-β plaques by recruiting microglia and prevented new plaque formation. Unlike other Aβ antibodies, gantenerumab did not alter plasma Aβ suggesting undisturbed systemic clearance of soluble Aβ. These studies demonstrated that gantenerumab preferentially interacts with aggregated Aβ in the brain and lowers amyloid-β by eliciting effector cell-mediated clearance.
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“The decrease in amyloid (~5 CL) from baseline in the 1.0 mg/kg group was very modest and therapeutically irrelevant.”
From The amyloid hypothesis in Alzheimer disease: new insights from new therapeutics (2022) · cites this paper as [61]
In the citing paper
“For example, bapinezumab caused significant ARIA-E but removed very little amyloid 61 .”
From The amyloid hypothesis in Alzheimer disease: new insights from new therapeutics (2022) · cites this paper as [61]
In the citing paper
“| Bapineuzumab | 0.3 | ~7 a /12 | 0 | 71 | 0 | 9 | - |”
From The amyloid hypothesis in Alzheimer disease: new insights from new therapeutics (2022) · cites this paper as [61]
In the citing paper
“| Bapineuzumab | 0.3 | ~7 a /12 | 0 | 71 | 0 | 9 | - |”
From The amyloid hypothesis in Alzheimer disease: new insights from new therapeutics (2022) · cites this paper as [61]
In the citing paper
“| Bapineuzumab | 0.3 | ~7 a /12 | 0 | 71 | 0 | 9 | - |”
From The amyloid hypothesis in Alzheimer disease: new insights from new therapeutics (2022) · cites this paper as [61]
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Romero‐Molina, C., Navarro, V., Jiménez, S., Muñoz‐Castro, C., Sanchez-Mico, M. V., Gutiérrez, A., Vitórica, J., & Vizuete, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22189734 · Cited by 14
Emerging amyloid and tau targeting treatments for Alzheimer’s disease
Khan, A., Corbett, A., & Ballard, C. G. (2017) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2017.1326819 · Cited by 16
Passive Anti-amyloid Beta Monoclonal Antibodies: Lessons Learned over Past 20 Years
Wicker, A., Shriram, J., Decourt, B., & Sabbagh, M. N. (2024) · Neurology and Therapy · doi:10.1007/s40120-024-00664-z · Cited by 15
“Additionally, it was found to reduce new plaque formation without increasing soluble plasma A β levels in murine models [36].”
BackgroundWang, Z., Jin, M., Hong, W., Liu, W., Reczek, D., Lagomarsino, V. N., Hu, Y., Weeden, T., Frosch, M. P., Young‐Pearse, T. L., et al. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01511-2 · Cited by 13
Immunotherapy in Alzheimer’s Disease: Current Status and Future Directions
Vashisth, K., Sharma, S., Ghosh, S., Babu, M. A., Ghosh, S., Iqbal, D., Kamal, M., Almutary, A. G., Jha, S. K., Ojha, S. K., et al. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-230603 · Cited by 13
Amyloid solutions: lecanemab, gantenerumab, and donanemab in the treatment of Alzheimer's disease
Ameen, T. B., Ali, U., Salma, O., Samee, M. A., Abbas, S. M. I., Kashif, S. N., Arifi, M. A., Ali, M., Khowaja, M., Ali, S. M. S., et al. (2025) · The Egyptian Journal of Neurology Psychiatry and Neurosurgery · doi:10.1186/s41983-025-00968-3 · Cited by 20
“Studies utilizing electron microscopy have confirmed that gantenerumab binds to Aβ fibrils within plaques in ex vivo samples, while immunofluorescence analysis has demonstrated its binding to Aβ in the brains of individuals with Alzheimer’s disease (AD) [217, 219].”
InfluentialValidation of an MRI Rating Scale for Amyloid‐Related Imaging Abnormalities
Bechten, A., Wattjes, M. P., Purcell, D. D., Aliaga, E. S., Daams, M., Brashear, H. R., Arrighi, H. M., & Barkhof, F. (2017) · Journal of Neuroimaging · doi:10.1111/jon.12422 · Cited by 13
Membrane-Modulating Drugs can Affect the Size of Amyloid-β25–35 Aggregates in Anionic Membranes
Khondker, A., Alsop, R. J., Himbert, S., Tang, J., Shi, A., Hitchcock, A. P., & Rheinstadter, M. C. (2018) · Scientific Reports · doi:10.1038/s41598-018-30431-8 · Cited by 13
França, V. L. B., BEZERRA, E. M., da COSTA, R. F., Carvalho, H. F., Freire, V. N., & Matos, G. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00453 · Cited by 13
Recent advances in immunotherapy targeting amyloid-beta and tauopathies in Alzheimer’s disease
Sha, S., Ren, L., Xing, X., Guo, W., Wang, Y., Li, Y., Cao, Y., & Qu, L. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-00846 · Cited by 16
“Semorinemab (RO7105705) is a humanized IgG4 monoclonal antibody that recognizes 6–23 amino acids of tau protein and simultaneously binds to different tau forms, including monomers and oligomers.”
Clinical Pharmacology of Novel Anti-Alzheimer Disease Modifying Medications
Caraci, F., Bosco, P., Leggio, G. M., Malaguarnera, M., Drago, F., Bucolo, C., & Salomone, S. (2013) · Current Topics in Medicinal Chemistry · doi:10.2174/15680266113139990141 · Cited by 12
Pre-amyloid oligomers budding:a metastatic mechanism of proteotoxicity
Bernini, F., Malferrari, D., Pignataro, M., Bortolotti, C. A., Rocco, G. D., Lancellotti, L., Brigatti, M. F., Kayed, R., Borsari, M., del Monte, F., et al. (2016) · Scientific Reports · doi:10.1038/srep35865 · Cited by 12
Leite, J. P., & Gales, L. (2018) · FEBS Letters · doi:10.1002/1873-3468.13285 · Cited by 12
Mazer, N. A., Hofmann, C., Lott, D., Gieschke, R., Klein, G., Boess, F., Grimm, H. P., Kerchner, G. A., Baudler, M., Smith, J., et al. (2022) · Alzheimer s & Dementia · doi:10.1002/alz.12877 · Cited by 13
“44 Linkage 2 is the most complex in the model.”
Lannfelt, L. (2023) · Upsala Journal of Medical Sciences · doi:10.48101/ujms.v128.10316 · Cited by 12
“Gantenerumab (Roche) is a fully human mAb that targets N-terminal and mid-regions of Aβ and preferentially binds to aggregated fibrillar Aβ (49).”
BackgroundDevelopment of amyloid beta-directed antibodies against Alzheimer's disease: Twists and turns
Lu, D., Dou, F., & Gao, J. (2023) · Drug Discoveries & Therapeutics · doi:10.5582/ddt.2023.01215 · Cited by 16
Anti-Amyloid-β Immunotherapy for Alzheimer’s Disease
Crehan, H., & Lemere, C. A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00007-1 · Cited by 14
Perspectives on drug discovery strategies based on IDPs
Fuertes, G., Nevola, L., & Esteban-Martín, S. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816348-1.00009-0 · Cited by 11
Enhanced self-assembly of the 7–12 sequence of amyloid-β peptide by tyrosine bromination
Maiolo, D., Pizzi, A., Gori, A., Bergamaschi, G., Pigliacelli, C., Gazzera, L., Consonni, A., Baggi, F., Moda, F., Bombelli, F. B., et al. (2020) · Supramolecular chemistry · doi:10.1080/10610278.2020.1734203 · Cited by 11
Immune modulations and immunotherapies for Alzheimer’s disease: a comprehensive review
Mahdiabadi, S., Momtazmanesh, S., Perry, G. L., & Rezaei, N. (2021) · Reviews in the Neurosciences · doi:10.1515/revneuro-2021-0092 · Cited by 13
Kinetic fingerprints differentiate anti-Aβ therapiesPreprint
Linse, S. S., Scheidt, T., Bernfur, K., Vendruscolo, M., Dobson, C. M., Cohen, S. I. A., Šileikis, E., Lundquist, M., Qian, F., O’Malley, T. T., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/815308 · Cited by 11
Rizoska, B., Zachrisson, O., Appelkvist, P., Boström, E., Björklund, M., Rachalski, A., Gkanatsiou, E., Kylefjord, H., Söderberg, L., Nygren, P., et al. (2024) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2024.103950 · Cited by 10
“…treatment could prevent, but not completely reverse, amyloid deposition, was consistent with previous passive immunization studies in transgenic APP mouse models using anti-A β antibodies (Levites et al., 2006; Tucker et al., 2008; Wang et al., 2011; Bohrmann et al., 2012; Cadiz et al., 2024).”
ResultMiles, L. A., & Masters, C. L. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251361049 · Cited by 11
Novel disease-modifying therapeutics for the treatment of Alzheimer’s disease
Léger, G. C., & Massoud, F. (2013) · Expert Review of Clinical Pharmacology · doi:10.1586/17512433.2013.811237 · Cited by 10
Computational Analysis for the Rational Design of Anti-Amyloid Beta (Aβ) Antibodies
Greene, D., Po, T., Pan, J., Tabibian, T., & Luo, R. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b01837 · Cited by 10
Molecular Recognition between Aβ-Specific Single-Domain Antibody and Aβ Misfolded Aggregates
Zhang, M., Zheng, J., Nussinov, R., & Ma, B. (2018) · Antibodies · doi:10.3390/antib7030025 · Cited by 10
Anti-Aβ antibodies bound to neuritic plaques enhance microglia activity and mitigate tau pathology
Laversenne, V., Nazeeruddin, S., Källstig, E., Colin, P., Voize, C., & Schneider, B. L. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01069-3 · Cited by 11
Maiolo, D., Pizzi, A., Gori, A., Gazzera, L., Demitri, N., Genoni, A., Baggi, F., Moda, F., Terraneo, G., Bombelli, F. B., et al. (2020) · ChemistryOpen · doi:10.1002/open.201900350 · Cited by 9
Metadata
- Authors
- Bohrmann, B., Baumann, K., Benz, J., Gerber, F., Huber, W., Knoflach, F., Messer, J., Oroszlan, K., Rauchenberger, R., Richter, W. F., Rothe, C., Urban, M., Bardroff, M., Winter, M., Nordstedt, C., & Loetscher, H.
- Affiliations
- F. Hoffmann-La Roche AG (CH)
- F. Hoffmann-La Roche Ltd., pRED, Basel, Switzerland
- MorphoSys (Germany) (DE)
- Corresponding author
- Bohrmann, Bernd
- Venue
- Journal of Alzheimer's Disease
- Publisher
- SAGE Publications
- Published
- 2012-01-12
- Volume
- 28
- Issue
- 1
- Pages
- 49-69
- ISSN
- 1387-2877 (ISSN-L)
- 1875-8908
- OpenAlex
- W1927066019
- Cited by
- 448
- References
- 61
- Citations by year
- 2026: 21 · 2025: 32 · 2024: 49 · 2023: 43 · 2022: 43 · 2021: 26 · 2020: 45 · 2019: 29 · 2018: 29 · 2017: 23 · 2016: 31 · 2015: 21 · 2014: 31 · 2013: 19 · 2012: 5
- FWCI
- 16.30
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Alzheimer s Disease (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- DORA PSI (Paul Scherrer Institute) (submittedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- gantenerumab, anti-amyloid beta antibodies
- MeSH terms
- Amino Acid Sequence, Animals, Antibodies, Monoclonal, Cerebral Cortex, Cricetulus, Female, Cricetinae, Humans, Male, Mice, Inbred C57BL, Mice, Transgenic, Molecular Sequence Data, Phagocytosis, Protein Binding, Amyloid beta-Peptides, CHO Cells, Rats, Sprague-Dawley, Protein Structure, Tertiary, Crystallography, X-Ray, Excitatory Postsynaptic Potentials, Mice, Rats, Antibodies, Monoclonal, Humanized
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