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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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Citations
Cites
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · cited 1×
“Cryosections of mouse brains and postmortem human frontal cortices from AD cases at Braak stage VI [29] were prepared at 10 and 20 m nominal thickness, treated with ice-cold acetone and washed in PBS.”
MethodThe Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160
Bard, F., Cannon, C., Barbour, R., Burke, R.-L., Games, D., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., et al. (2000) · Nature Medicine · doi:10.1038/78682 · Cited by 2,012
3D structure of Alzheimer's amyloid-β(1–42) fibrils
Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D. A., & Riek, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506723102 · Cited by 2,001
Self-citationAβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
Janus, C., Pearson, J., McLaurin, J., Mathews, P. M., Jiang, Y., Schmidt, S. D., Chishti, M. A., Horne, P., Heslin, D., French, J., et al. (2000) · Nature · doi:10.1038/35050110 · Cited by 1,431
Holmes, C., Boche, D., Wilkinson, D., Yadegarfar, G., Hopkins, V., Bayer, A., Jones, R. W., Bullock, R., Love, S., Neal, J. W., et al. (2008) · The Lancet · doi:10.1016/s0140-6736(08)61075-2 · Cited by 1,416
Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: a case report
Nicoll, J. A. R., Wilkinson, D., Holmes, C., Steart, P., Markham, H., & Weller, R. O. (2003) · Nature Medicine · doi:10.1038/nm840 · Cited by 1,397
Cited by
Sorted by citations
Items 101–200 of 448
Treating Alzheimer’s disease with monoclonal antibodies: current status and outlook for the future
Prins, N. D., & Scheltens, P. (2013) · Alzheimer s Research & Therapy · doi:10.1186/alzrt220 · Cited by 79
Anti-amyloid-β protein agents for the treatment of Alzheimer’s disease: an update on emerging drugs
Lozupone, M., Solfrizzi, V., D’Urso, F., Di Gioia, I., Sardone, R., Dibello, V., Stallone, R., Liguori, A., Ciritella, C., Daniele, A., et al. (2020) · Expert Opinion on Emerging Drugs · doi:10.1080/14728214.2020.1808621 · Cited by 77
Panza, F., Solfrizzi, V., Imbimbo, B. P., & Logroscino, G. (2014) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2014.935332 · Cited by 80
Immunotherapy for Alzheimer’s disease: past, present and future
Spencer, B. J., & Masliah, E. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00114 · Cited by 73
Therapy for Alzheimer’s disease: Missing targets and functional markers?
Stoiljković, M., Horváth, T. L., & Hajós, M. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101318 · Cited by 74
Mechanisms of recognition of amyloid-β (Aβ) monomer, oligomer, and fibril by homologous antibodies
Zhao, J., Nussinov, R., & Ma, B. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.801514 · Cited by 71
Snow, A. D., Castillo, G. M., Nguyen, B. P., Choi, P. Y., Cummings, J. A., Cam, J. A., Hu, Q., Lake, T. P., Pan, W., Kastin, A. J., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-38645-0 · Cited by 73
Engineering antibody and protein therapeutics to cross the blood–brain barrier
Zhao, P., Zhang, N., & An, Z. (2022) · Antibody Therapeutics · doi:10.1093/abt/tbac028 · Cited by 75
“Gantenerumab, a fully human IgG1 mAb that binds to AA3–12 and AA18–27 of Aβ, is a conformational epitope in Aβ fibrils [31].”
An in vitro paradigm to assess potential anti-Aβ antibodies for Alzheimer’s disease
Jin, M., O’Nuallain, B., Hong, W., Boyd, J. D., Lagomarsino, V. N., O’Malley, T. T., Liu, W., Vanderburg, C. R., Frosch, M. P., Young‐Pearse, T. L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05068-w · Cited by 70
(2013) · PubMed · Cited by 66
Weidle, U. H., Niewöhner, J., & Tiefenthaler, G. (2015) · PubMed · Cited by 68
Antibody-Based Drugs and Approaches Against Amyloid-β Species for Alzheimer’s Disease Immunotherapy
Liu, J., Yang, B., Ke, J., Li, W., & Suen, W.-C. (2016) · Drugs & Aging · doi:10.1007/s40266-016-0406-x · Cited by 67
“Gantenerumab (phase III, Roche), a human IgG1 mAb that was screened and optimized by phage display technology [73], possesses two epitopes, Ab1–10 and Ab19–26 (shown in Fig.”
BackgroundSumbria, R. K., Hui, E. K., Lu, J. Z., Boado, R. J., & Pardridge, W. M. (2013) · Molecular Pharmaceutics · doi:10.1021/mp400348n · Cited by 65
An anti-pyroglutamate-3 Aβ vaccine reduces plaques and improves cognition in APPswe/PS1ΔE9 mice
Frost, J. L., Liu, B., Rahfeld, J., Kleinschmidt, M., O’Nuallain, B., Le, K. X., Lues, I., Caldarone, B. J., Schilling, S., Demuth, H., et al. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.08.021 · Cited by 64
“Differing clearance of plaques has been observed previously also with gantenerumab (Bohrmann et al., 2012), and similar effects might account for the apparent discrepancy between quantitative image analysis of plaque size and the Aβ concentration in the brain.”
BackgroundAmyloid-beta immunotherapy: the hope for Alzheimer disease?
Barrera-Ocampo, A. A., & Lopera, F. J. (2016) · Colombia medica · doi:10.25100/cm.v47i4.2640 · Cited by 64
Piazza, F., Caminiti, S. P., Zedde, M., Presotto, L., DiFrancesco, J. C., Pascarella, R., Giossi, A., Sessa, M., Poli, L., Basso, G., et al. (2022) · Neurology · doi:10.1212/wnl.0000000000200892 · Cited by 64
Passive immunotherapy for Alzheimer's disease
Guo, X., Li, Y., Zhang, D., & Zhao, Y. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102192 · Cited by 69
“…monoclonal IgG1 antibody developed by phage display technologies, recognizes conformational epitopes consisting of the N-terminal (amino acids 3 – 11) and central portions of A β (amino acids 18 – 27) and binds A β fibrils with subnanomolar affinity (Bohrmann et al., 2012; Crespi et al., 2015).”
BackgroundPardridge, W. M., Boado, R. J., Patrick, D. J., Hui, E. K., & Lu, J. Z. (2018) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.8b00730 · Cited by 62
Receptor-mediated drug delivery of bispecific therapeutic antibodies through the blood-brain barrier
Pardridge, W. M. (2023) · Frontiers in Drug Delivery · doi:10.3389/fddev.2023.1227816 · Cited by 62
Alkhalifa, A. E., Mokhlf, A. A., Ali, H., Al-Ghraiybah, N. F., & Syropoulou, V. (2025) · Journal of Personalized Medicine · doi:10.3390/jpm15090437 · Cited by 68
Wang, H., Xu, X., Pan, Y., Yan, Y., Hu, X., Chen, R., Ravoo, B. J., Guo, D., & Zhang, T. (2020) · Advanced Materials · doi:10.1002/adma.202006483 · Cited by 61
Antibody Approaches To Treat Brain Diseases
Neves, V., Aires‐da‐Silva, F., Côrte‐Real, S., & Castanho, M. A. R. B. (2015) · Trends in biotechnology · doi:10.1016/j.tibtech.2015.10.005 · Cited by 63
Panza, F., Lozupone, M., Dibello, V., Greco, A., Daniele, A., Seripa, D., Logroscino, G., & Imbimbo, B. P. (2018) · Immunotherapy · doi:10.2217/imt-2018-0119 · Cited by 63
Developing therapeutic vaccines against Alzheimer’s disease
Wısnıewskı, T., & Drummond, E. (2015) · Expert Review of Vaccines · doi:10.1586/14760584.2016.1121815 · Cited by 60
Emerging drugs to reduce abnormal β-amyloid protein in Alzheimer’s disease patients
Panza, F., Seripa, D., Solfrizzi, V., Imbimbo, B. P., Lozupone, M., Leo, A., Sardone, R., Gagliardi, G., Lofano, L., Creanza, B. C., et al. (2016) · Expert Opinion on Emerging Drugs · doi:10.1080/14728214.2016.1241232 · Cited by 61
“In vivo, gantenerumab crosses the blood–brain barrier and binds specifically and dose dependently to Aβ SPs in APP751 Swedish xPS2N141I (PS2APP) transgenic mice [91].”
BackgroundInfluentialSöderberg, L., Johannesson, M., Gkanatsiou, E., Nygren, P., Fritz, N., Zachrisson, O., Rachalski, A., Svensson, A.-S., Button, E. B., Dentoni, G., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-61691-2 · Cited by 62
Passive antiamyloid immunotherapy for Alzheimer's disease
Loureiro, J. C., Pais, M. V., Stella, F., Radanovic, M., Teixeira, A. L., Forlenza, O. V., & de Souza, L. C. (2020) · Current Opinion in Psychiatry · doi:10.1097/yco.0000000000000587 · Cited by 57
“Gantenerumab (RO4909832) is the first fully humanized IgG1 mAb, designed to bind to fibrillary Ab, with affinity to N-terminal (Ab3–12) and middle portion (Ab18–27) domains of the peptide [19].”
BackgroundPardridge, W. M. (2016) · Expert Opinion on Biological Therapy · doi:10.1080/14712598.2016.1230195 · Cited by 55
Vaccination against β-Amyloid as a Strategy for the Prevention of Alzheimer’s Disease
Mantile, F., & Prisco, A. (2020) · Biology · doi:10.3390/biology9120425 · Cited by 56
Recent advancement in therapeutic strategies for Alzheimer’s disease: Insights from clinical trials
Khan, T., Waseem, R., Shahid, M., Ansari, J., Ahanger, I. A., Hassan, M. I., & Islam, A. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102113 · Cited by 60
Castro, P., Zaman, S. H., & Holland, A. J. (2016) · Journal of Neurology · doi:10.1007/s00415-016-8308-8 · Cited by 59
Jung, M., Lee, S., Park, S., Hong, J., Kim, C., Cho, I., Sohn, H. S., Kim, K. H., Park, I. W., Yoon, S., et al. (2022) · Advanced Materials · doi:10.1002/adma.202207719 · Cited by 59
Drug delivery strategies with lipid-based nanoparticles for Alzheimer’s disease treatment
Jang, Y.-J., Kang, S.-J., Park, H. S., Lee, D., Kim, J. H., Kim, J.-E., Kim, D., Chung, C., Yoon, J., & Bhang, S. H. (2025) · Journal of Nanobiotechnology · doi:10.1186/s12951-025-03109-3 · Cited by 64
Dhage, P. A., Sharbidre, A. A., Dakua, S. P., & Balakrishnan, S. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111634 · Cited by 53
Zielinski, M., Reyes, F. S. P., Gremer, L., Schemmert, S., Frieg, B., Schäfer, L. U., Willuweit, A., Donner, L., Elvers, M., Nilsson, L. N. G., et al. (2023) · Nature Neuroscience · doi:10.1038/s41593-023-01484-4 · Cited by 53
“Structural differences in human and murine Aβ fibrils might help to improve our understanding of why fibril-targeting drug candidates show efficacy when tested in mouse models but then fail to show the desired effect in clinical trials 20,29–34 .”
BackgroundMably, A. J., Liu, W., Donald, J. M. M., Dodart, J., Bard, F., Lemere, C. A., O’Nuallain, B., & Walsh, D. M. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.07.008 · Cited by 55
“Several aggregatepreferring antibodies have been shown to decrease Aβ deposition (Bohrmann et al., 2012; Lord et al., 2009; Tucker et al., 2015) and synapse loss (Dorostkar et al., 2014), and in at least 3 different mouse models aggregate-preferringmAbs have been shown to preserve cognition (Lee et…”
Efficacy and safety studies of gantenerumab in patients with Alzheimer’s disease
Panza, F., Solfrizzi, V., Imbimbo, B. P., Giannini, M., Santamato, A., Seripa, D., & Logroscino, G. (2014) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.2014.945522 · Cited by 51
Resveratrol-mediated cleavage of amyloid β1–42 peptide: potential relevance to Alzheimer's disease
Al-Edresi, S., Alsalahat, I., Freeman, S., Aojula, H. S., & Penny, J. I. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.04.012 · Cited by 53
Weisová, P., Cehlár, O., Škrabana, R., Žilková, M., Filipčík, P., Kováčech, B., Prčina, M., Wojčiaková, Ľ., Fialová, Ľ., Smolek, T., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0770-y · Cited by 53
Feinberg, H., Saldanha, J. W., Diep, L., Goel, A. S., Widom, A., Veldman, G. M., Weis, W. I., Schenk, D., & Basi, G. S. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt261 · Cited by 52
“While 12A11 captures an extended conformation of the peptide that is highly conserved among antibodies binding this epitope [25,26,37,38], 3D6 binds Aβ in a 310-helix conformation (Figure 5A).”
InfluentialAntibody Therapeutics Targeting Aβ and TauPreprint
Gallardo, G., & Holtzman, D. M. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024331 · Cited by 55
Diagnosis and Treatment of Alzheimer’s Disease:
Bomasang-Layno, E., & Bronsther, R. (2021) · Delaware Journal of Public Health · doi:10.32481/djph.2021.09.009 · Cited by 60
Mukherjee, S., Perez, K. A., Lago, L., Klatt, S., McLean, C., Birchall, I. E., Barnham, K. J., Masters, C. L., & Roberts, B. R. (2021) · Brain Communications · doi:10.1093/braincomms/fcab028 · Cited by 48
Makowski, E. K., Wang, T., Zupancic, J. M., Huang, J., Wu, L., Schardt, J. S., Groot, A. S. D., Elkins, S. L., Martin, W. D., & Tessier, P. M. (2023) · Nature Biomedical Engineering · doi:10.1038/s41551-023-01074-6 · Cited by 55
Joseph‐Mathurin, N., Llibre‐Guerra, J. J., Li, Y., McCullough, A. A., Hofmann, C., Wojtowicz, J., Park, E., Wang, G., Preboske, G. M., Wáng, Q., et al. (2022) · Annals of Neurology · doi:10.1002/ana.26511 · Cited by 48
“Interpretation: In DIAD, solanezumab was not associated with ARIA.”
BackgroundInfluentialRosenberg, R. N., Fu, M., & Lambracht‐Washington, D. (2018) · Alzheimer s Research & Therapy · doi:10.1186/s13195-018-0441-4 · Cited by 50
NPT088 reduces both amyloid‐β and tau pathologies in transgenic mice
Levenson, J. M., Schroeter, S., Carroll, J. C., Cullen, V., Asp, E., Proschitsky, M., Chung, C. H. ‐., Gilead, S., Nadeem, M., Dodiya, H. B., et al. (2016) · Alzheimer's & Dementia: Translational Research & Clinical Interventions · doi:10.1016/j.trci.2016.06.004 · Cited by 47
Bard, F., Fox, M., Friedrich, S. W., Seubert, P. A., Schenk, D., Kinney, G. G., & Yednock, T. A. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.07.022 · Cited by 47
“A similar long-lasting binding to amyloid plaques of another antibody to Aβ has been observed in hAPP transgenic mice (Bohrman et al., 2012).”
BackgroundBreaching the Blood-Brain Barrier for Drug Delivery
Bell, R. D., & Ehlers, M. (2014) · Neuron · doi:10.1016/j.neuron.2013.12.023 · Cited by 47
Lathuilière, A., Mach, N., & Schneider, B. L. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160510578 · Cited by 48
An effective treatment for Alzheimer's disease must consider both amyloid and tau
Lansdall, C. J. (2014) · Bioscience Horizons The International Journal of Student Research · doi:10.1093/biohorizons/hzu002 · Cited by 46
“Gantenerumab is reported to cause Fc receptor/ microglia-mediated phagocytosis of amyloid, followed by lysosomal degradation (Bohrmann et al., 2012).”
BackgroundLathuilière, A., Laversenne, V., Astolfo, A., Kopetzki, E., Jacobsen, H., Stampanoni, M., Bohrmann, B., Schneider, B. L., & Aebischer, P. (2016) · Brain · doi:10.1093/brain/aww036 · Cited by 49
“enhance phagocytosis by mouse microglial cells, a mechanism that has been proposed to mediate the clearance of amyloid plaques (Bard et al. , 2000; Bohrmann et al. , 2012; Demattos et al. , 2012).”
BackgroundMethodInfluentialSelf-citationBastrup, J., Hansen, K. H., Poulsen, T. B. G., Kastaniegaard, K., Asuni, A. A., Christensen, S., Belling, D., Helboe, L., Stensballe, A., & Volbracht, C. (2021) · Journal of Alzheimer's Disease · doi:10.3233/jad-200715 · Cited by 46
Meilandt, W. J., Maloney, J. A., Imperio, J., Lalehzadeh, G., Earr, T., Crowell, S., Bainbridge, T. W., Lu, Y., Ernst, J. A., Fuji, R. N., et al. (2019) · Alzheimer's Research & Therapy · doi:10.1186/s13195-019-0553-5 · Cited by 45
Profile of gantenerumab and its potential in the treatment of Alzheimer's disease
Nisticò, R., Novakovic, D., Feligioni, M., Scaccianoce, S., Piccinin, S., Mercuri, N. B., Nicoletti, F., Caruso, A., Schepisi, C., & Errico, F. (2013) · Drug Design Development and Therapy · doi:10.2147/dddt.s53401 · Cited by 50
“25 Accordingly, in both wild-type and PS2APP mice, gan-tenerumab exhibited a biphasic appearance with approximately dose-proportional increases in maximum concentration (C max ) and area-under-the-curve parameters.”
Passive Aβ Immunotherapy: Current Achievements and Future Perspectives
Schilling, S., Rahfeld, J., Lues, I., & Lemere, C. A. (2018) · Molecules · doi:10.3390/molecules23051068 · Cited by 48
Comparing the efficacy and neuroinflammatory potential of three anti-abeta antibodies
Fuller, J. P., Stavenhagen, J. B., Christensen, S., Kartberg, F., Glennie, M. J., & Teeling, J. L. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1484-2 · Cited by 46
Modulation of innate immunity of patients with Alzheimer's disease by omega‐3 fatty acids
Fiala, M., Kooij, G., Wagner, K. M., Hammock, B. D., & Pellegrini, M. A. (2017) · The FASEB Journal · doi:10.1096/fj.201700065r · Cited by 44
Cabral, C. M., McGovern, K. E., MacDonald, W. R., Franco, J., & Koshy, A. A. (2017) · ASN NEURO · doi:10.1177/1759091417724915 · Cited by 44
“…have been made to target Ab by administration of monoclonal antibodies, but only recently has one of these antibody treatments shown promise in removing Ab in AD patients (Bohrmann et al., 2012; Farlow et al., 2012; Garber, 2012; Sperling et al., 2012; Moreth et al., 2013; Sevigny et al., 2016).”
BackgroundRecent advancements toward therapeutic vaccines against Alzheimer’s disease
Herline, K., Drummond, E., & Wısnıewskı, T. (2018) · Expert Review of Vaccines · doi:10.1080/14760584.2018.1500905 · Cited by 46
Portron, A., Jordan, P., Draper, K., Muenzer, C., Dickerson, D., van Iersel, T. M., & Hofmann, C. (2019) · Clinical Therapeutics · doi:10.1016/j.clinthera.2019.11.015 · Cited by 43
Li, Y., Zhao, Y., Tan, X., Liu, J., Zhi, Y., Yi, L., Bai, S., Du, Q., Li, Q. X., & Dong, Y. (2020) · Mediators of Inflammation · doi:10.1155/2020/8704146 · Cited by 44
“Long-lasting inflammation damages the brain, which is common in neurodegenerative diseases [44, 45].”
BackgroundSerotonin and Melatonin Show Different Modes of Action on Aβ42 Protofibril Destabilization
Gong, Y., Zhan, C., Zou, Y. F., Qian, Z., Wei, G., & Zhang, Q. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00038 · Cited by 46
Alzheimer’s Disease: Drug Discovery
Huang, X. (2020) · Exon Publications eBooks · doi:10.36255/exonpublications.alzheimersdisease.2020 · Cited by 49
Zhao, P., Xu, Y., Fan, X., Li, L., Li, X., Arase, H., Tong, Q., Zhang, N., & An, Z. (2022) · mAbs · doi:10.1080/19420862.2022.2107971 · Cited by 46
Monoclonal Antibody Therapy in Alzheimer’s Disease
Neațu, M., Covaliu, A., Ioniță, I., Jugurt, A., Davidescu, E. I., & Popescu, B. O. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics16010060 · Cited by 46
“After only 26 enrollments, the trial was terminated because there was inadequate scientific evidence to potentially show a tangible benefit of solanezumab [119,123–125].”
BackgroundVaccination strategies in tauopathies and synucleinopathies
Braczynski, A. K., Schulz, J. B., & Bach, J. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14207 · Cited by 44
Chen, Y., Chen, Z., Sun, Y., Lei, J., & Wei, G. (2018) · Nanoscale · doi:10.1039/c8nr01041b · Cited by 42
Gupta, S., & Dasmahapatra, A. K. (2019) · Physical Chemistry Chemical Physics · doi:10.1039/c9cp04162a · Cited by 43
Panza, F., Seripa, D., Lozupone, M., Solfrizzi, V., Imbimbo, B. P., Barulli, M. R., Tortelli, R., Capozzo, R., Bisceglia, P., Dimitri, A., et al. (2018) · Expert Opinion on Biological Therapy · doi:10.1080/14712598.2018.1389885 · Cited by 41
Amyloid-β and α-Synuclein Immunotherapy: From Experimental Studies to Clinical Trials
Nimmo, J., Kelly, L., Verma, A. K., Carare, R. O., Nicoll, J. A. R., & Dodart, J. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.733857 · Cited by 40
Sharma, H., & Chandra, P. (2023) · International Journal of Pharmaceutical Investigation · doi:10.5530/ijpi.14.1.15 · Cited by 47
Ricci, G. (2019) · Behavioural Neurology · doi:10.1155/2019/8720904 · Cited by 43
“One of these drugs is crenezumab consisting of monoclonal antibodies targeting betaamyloid, and the other is gantenerumab, a human IgG1 antibody centrally acting to disassemble and degrade amyloid plaques [32].”
Liu, N., Liang, X., Chen, Y., & Xie, L. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102199 · Cited by 44
Lecanemab preferentially binds to smaller aggregates present at early Alzheimer's disease
Fertan, E., Lam, J. Y. L., Albertini, G., Dewilde, M., Wu, Y., Akingbade, O. E. S., Böken, D., English, E. A., Strooper, B. D., & Klenerman, D. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70086 · Cited by 39
Jin, Y., Sun, Y., Lei, J., & Wei, G. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c8cp01631c · Cited by 40
Anti-amyloid Therapy of Alzheimer’s Disease: Current State and Prospects
Kozin, S. A., Barykin, E. P., Mitkevich, V. A., & Makarov, A. А. (2018) · Biochemistry (Moscow) · doi:10.1134/s0006297918090079 · Cited by 39
Wagemann, O., Liu, H., Wang, G., Shi, X., Bittner, T., Scelsi, M. A., Farlow, M. R., Clifford, D. B., Supnet, C. B., Santacruz, A. M., et al. (2024) · JAMA Neurology · doi:10.1001/jamaneurol.2024.0991 · Cited by 40
Lessons from Anti-Amyloid-β Immunotherapies in Alzheimer Disease: Aiming at a Moving Target
Wang, Y., Yan, T., Lu, H., Yin, W., Lin, B., Fan, W., Zhang, X., & Fernández-Fúnez, P. (2017) · Neurodegenerative Diseases · doi:10.1159/000478741 · Cited by 39
Anti-amyloid-beta to tau-based immunization: developments in immunotherapy for Alzheimer's disease
Lambracht‐Washington, D., & Rosenberg, R. N. (2013) · ImmunoTargets and Therapy · doi:10.2147/itt.s31428 · Cited by 39
“In vitro studies showed that gantenerumab can induce phagocytosis of Aβ fibrils by brain microglia.(48) In patients,”
Aβ-Immunotherapeutic strategies: a wide range of approaches for Alzheimer's disease treatment
Montoliu‐Gaya, L., & Villegas, S. (2016) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2016.11 · Cited by 39
Targeting Beta-Amyloid at the CSF: A New Therapeutic Strategy in Alzheimer’s Disease
Menéndez‐González, M., Padilla-Zambrano, H., Alvarez, G., Capetillo‐Zarate, E., Tomás‐Zapico, C., & Costa, A. D. D. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00100 · Cited by 38
“This antibody acts centrally to disassemble and degrade amyloid plaques by recruiting microglia and activating phagocytosis (Ostrowitzki et al., 2012) but it does not alter plasma Aβ (Bohrmann et al., 2012).”
BackgroundNanotechnology approaches for enhanced CNS delivery in treating Alzheimer's disease
Arya, M. A., Kumar, M. K. M., Sabitha, M., Menon, K. N., & Nair, S. C. (2019) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2019.03.022 · Cited by 37
Zhan, C., Lao, Z., Tang, Y., Qiao, Q., & Wei, G. (2021) · Chemical Communications · doi:10.1039/d1cc00404b · Cited by 37
Luo, J., Lee, S., VandeVrede, L. A., Qin, Z., Aissa, M. B., Larson, J., Teich, A. F., Arancio, O., D’Souza, Y., Elharram, A., et al. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0103-6 · Cited by 37
Therapeutic Antibodies by Phage Display
Shim, H. (2016) · Current Pharmaceutical Design · doi:10.2174/1381612822666160923113714 · Cited by 36
Saeedi, M., & Mehranfar, F. (2022) · Recent Patents on Biotechnology · doi:10.2174/1872208316666220302115901 · Cited by 36
Gustavsson, T., Metzendorf, N. G., Wik, E., Roshanbin, S., Julku, U. H., Chourlia, A., Nilsson, P., Andersson, K. G., Laudon, H., Hultqvist, G., et al. (2023) · Alzheimer s Research & Therapy · doi:10.1186/s13195-023-01236-3 · Cited by 37
Understanding the Molecular Mechanisms of Polyphenol Inhibition of Amyloid β Aggregation
Han, Y.-L., Yin, H., Chao, X., Bernards, M. T., He, Y., & Guan, Y. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00586 · Cited by 35
Immunotherapy for Alzheimer's Disease: Current Scenario and Future Perspectives
Usman, M. B., Bhardwaj, S., Roychoudhury, S., Kumar, D., Alexiou, A. T., Kumar, P., Ambasta, R. K., Prasher, P., Shukla, S. D., Upadhye, V. J., et al. (2021) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2021.52 · Cited by 37
“Therefore, the antibody shows a higher affinity for Aβ oligomers and fibrils than for Aβ monomers (116).”
InfluentialLessons from antiamyloid-β immunotherapies in Alzheimer's disease
Plascencia‐Villa, G., & Perry, G. L. (2023) · Handbook of clinical neurology · doi:10.1016/b978-0-323-85555-6.00019-9 · Cited by 35
Pradier, L., Blanchard-Brégeon, V., Bohme, A., Debeir, T., Ménager, J., Benoit, P., Barnéoud, P., Taupin, V., Bertrand, P., Dugay, P., et al. (2018) · Alzheimer s Research & Therapy · doi:10.1186/s13195-018-0447-y · Cited by 37
Current and Emerging Pharmacological Targets for the Treatment of Alzheimer’s Disease
Morsy, A., & Trippier, P. C. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190744 · Cited by 36
“[64–67] Gantenerumab (105, 225 or 1200 mg once a month) At Risk, Prodromal and Mild Stages Clinical outcome remains under investigation with five ongoing phase III trials (NCT03443973, NCT03444870, NCT02051608, NCT01224106, NCT01760005) [68, 69] Aducanumab (low-dose titration to 3 or 6 mg/kg based on ApoE4 carrier sta…”
BackgroundDong, X., Tang, Y., Zhan, C., & Wei, G. (2020) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2020.105024 · Cited by 34
Montoliu‐Gaya, L., Mulder, S. D., Herrebout, M. A. C., Baayen, J. C., Villegas, S., & Veerhuis, R. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.03.015 · Cited by 33
“Despite positive effects on Aβ load and cognition, passive as well as active immunization against Aβ generated side effects including meningoencephalitis and vasogenic edema (Montoliu-Gaya and Villegas 2016; Bohrmann et al. 2012; Ostrowitzki et al. 2012).”
Ni, J., Xie, Z., Quan, Z., Meng, J., & Qing, H. (2023) · Glia · doi:10.1002/glia.24465 · Cited by 33
RETRACTED ARTICLE: Gantenerumab for the treatment of Alzheimer's disease
Delrieu, J., Ousset, P., & Vellas, B. J. (2012) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2012.688022 · Cited by 32
RetractedInterpreting Alzheimer’s disease clinical trials in light of the effects on amyloid-β
Toyn, J. H., & Ahlijanian, M. K. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt244 · Cited by 31
“The potential of the current cohort of 'second generation' therapeutics, such as BACEis, which appear to provide potential for testing a broad range of Aβ lowering, and antibodies like crenezumab [127] and gantenerumab [128], is promising and may ultimately enable testing of the amyloid hypothesis.”
BackgroundPrion-like Mechanisms in Alzheimer's Disease
Yin, R., Tan, L., Jiang, T., & Yu, J. (2014) · Current Alzheimer Research · doi:10.2174/156720501108140910121425 · Cited by 33
Decourt, B., Noorda, K., Noorda, K. J., Shi, J., & Sabbagh, M. N. (2022) · Journal of Experimental Pharmacology · doi:10.2147/jep.s265626 · Cited by 33
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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