The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.
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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Trends in Research on Gantenerumab for Alzheimer’s Disease: A Bibliometric and Thematic Analysis
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Laversenne, V., Nazeeruddin, S., Källstig, E., Colin, P., Voize, C., & Schneider, B. L. (2020) · Figshare · doi:10.6084/m9.figshare.13278567
Sandberg, A., Berenjeno-Correa, E., Rodriguez, R. C., Axenhus, M., Weiss, S. S., Batenburg, K. L., Hoozemans, J. J. M., Tjernberg, L. O., & Scheper, W. (2023) · Figshare · doi:10.6084/m9.figshare.22612324
Laversenne, V., Nazeeruddin, S., Källstig, E., Colin, P., Voize, C., & Schneider, B. L. (2020) · Figshare · doi:10.6084/m9.figshare.13278561
Sandberg, A., Berenjeno-Correa, E., Rodriguez, R. C., Axenhus, M., Weiss, S. S., Batenburg, K. L., Hoozemans, J. J. M., Tjernberg, L. O., & Scheper, W. (2023) · Figshare · doi:10.6084/m9.figshare.22612348
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Sandberg, A., Berenjeno-Correa, E., Rodriguez, R. C., Axenhus, M., Weiss, S. S., Batenburg, K. L., Hoozemans, J. J. M., Tjernberg, L. O., & Scheper, W. (2023) · Figshare · doi:10.6084/m9.figshare.22612342
Laversenne, V., Nazeeruddin, S., Källstig, E., Colin, P., Voize, C., & Schneider, B. L. (2020) · Figshare · doi:10.6084/m9.figshare.13278573
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Laversenne, V., Nazeeruddin, S., Källstig, E., Colin, P., Voize, C., & Schneider, B. L. (2020) · Figshare · doi:10.6084/m9.figshare.13278555
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“…cleavage, 28 molecular chaperones (heat shock proteins), which drive disassembly through ATP-dependent mechanisms, 29 proteolytic fragmentation, 30 or isomerase-mediated remodeling, 31 and humanized antibodies such as Crenezumab 32 and Gantenerumab, 33 which selectively clear aggregated species.”
Sharma, S., Sharma, U., Sethiya, N. K., & Singh, L. (2026) · Current Aging Science · doi:10.2174/0118746098373086251201095903
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Various Immunotherapy and Targeted Therapeutics for Managing Alzheimer’s Disease
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“Gantenerumab is a human monoclonal antibody designed to target A β fibrils by iden‑ tifying a structural epitope on A β aggregates [117].”
Antibody-Based Medicines Versus Conventional Treatments for Alzheimer’s Disease
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“This is consistent with the increased expression of lysosomal and protein degradation genes in lecanemab-treated human tissue [23], lecanemab-treated animal models [25], and with ex vivo studies showing that gantenerumab induced colocalization of A β and LAMP-2 [16].”
A Narrative Review of Amyloid-β Monoclonal Antibodies for Alzheimer Disease
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THERAPY FOR ALZHEIMER’S DISEASE - FOCUS ON LECANEMAB
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Liquormarker Aß 1-42, T-Tau und P-Tau in der Differenzialdiagnostik der Demenzen
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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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