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25 results on '"Sonati, Tiziana"'

1. MY006: allergen-targeted antibodies for the treatment of peanut allergy

Author

Arena, Chiara, primary, Bieli, Dimitri, additional, Gasser, Pascal, additional, Götschi, Sandra, additional, Scheibling, Rahel, additional, Ilca, Tudor, additional, Paolucci, Marta, additional, Homère, Valentine, additional, Bouis, Delphine, additional, Martin-Rodriguez, Omayra, additional, Johansen, Pål, additional, Wang Yin, Kiave Ho, additional, Ballmer-Weber, Barbara, additional, Köhli, Alice, additional, Sonati, Tiziana, additional, Barberis, Alcide, additional, Pengo, Niccolo, additional, and Wuillemin, Natascha, additional

Published
2024
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3. Targeting Ara h 2 with human‐derived monoclonal antibodies prevents peanut‐induced anaphylaxis in mice

Author

Paolucci, Marta, primary, Wuillemin, Natascha, additional, Homère, Valentine, additional, Bieli, Dimitri, additional, Köhli, Alice, additional, Ballmer‐Weber, Barbara, additional, Waeckerle‐Men, Ying, additional, Pengo, Niccolò, additional, Kündig, Thomas M., additional, Sonati, Tiziana, additional, and Johansen, Pål, additional

Published
2023
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5. Multivariate allergen-specific analysis and profiling of serum antibodies from patients with peanut allergy

Author

Paolucci, Marta, Wuillemin, Natascha, Köhli, Alice, Ballmer-Weber, Barbara, Severin, Yannik, Waeckerle‐Men, Ying, Arena, Chiara, Homère, Valentine, Bieli, Dimitri, Kündig, Thomas M, Sonati, Tiziana, Johansen, Pål, University of Zurich, and Johansen, Pål

Subjects
2403 Immunology, Immunology, 2723 Immunology and Allergy, 10177 Dermatology Clinic, Immunology and Allergy, 610 Medicine & health
Published
2023

7. Multivariate allergen‐specific analysis and profiling of serum antibodies from patients with peanut allergy

Author

Paolucci, Marta, primary, Wuillemin, Natascha, additional, Köhli, Alice, additional, Ballmer‐Weber, Barbara, additional, Severin, Yannik, additional, Waeckerle‐Men, Ying, additional, Arena, Chiara, additional, Homère, Valentine, additional, Bieli, Dimitri, additional, Kündig, Thomas M., additional, Sonati, Tiziana, additional, and Johansen, Pål, additional

Published
2022
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9. The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein

Author

Sonati, Tiziana, Reimann, Regina R., Falsig, Jeppe, Baral, Pravas Kumar, O'Connor, Tracy, Hornemann, Simone, Yaganoglu, Sine, Li, Bei, Herrmann, Uli S., Wieland, Barbara, Swayampakula, Mridula, Rahman, Muhammad Hafizur, Das, Dipankar, Kav, Nat, Riek, Roland, Liberski, Pawel P., James, Michael N.G., and Aguzzi, Adriano

Subjects
Viral antibodies -- Dosage and administration, Prions -- Physiological aspects -- Health aspects, Drug interactions -- Research, Antibodies -- Dosage and administration, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Prion infections cause lethal neurodegeneration. This process requires the cellular prion protein ([PrP.sup.C]; ref. 1), which contains a globular domain hinged to a long amino-proximal flexible tail (2). Here we [...]

Published
2013
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10. The Priority position paper: protecting Europe´s food chain from prions

Author

Requena, Jesús R, Kristensson, Krister, Korth, Carsten, Zurzolo, Chiara, Simmons, Marion, Aguilar-Calvo, Patricia, Aguzzi, Adriano, Andreoletti, Olivier, Benestad, Sylvie L, Böhm, Reinhard, Brown, Karen, Calgua, Byron, del Río, José Antonio, Espinosa, Juan Carlos, Girones, Rosina, Godsave, Sue, Hoelzle, Ludwig E, Knittler, Michael R, Kuhn, Franziska, Legname, Giuseppe, Laeven, Paul, Mabbott, Neil, Mitrova, Eva, Müller-Schiffmann, Andreas, Nuvolone, Mario, Peters, Peter J, Raeber, Alex, Roth, Klaus, Schmitz, Matthias, Schroeder, Björn, Sonati, Tiziana, Stitz, Lothar, Taraboulos, Albert, Torres, Juan María, Yan, Zheng-Xin, Zerr, Inga, University of Zurich, and Requena, Jesús R

Subjects
1307 Cell Biology, prion, atypical scrapie, CJD, 1303 Biochemistry, scrapie, 10208 Institute of Neuropathology, 2804 Cellular and Molecular Neuroscience, 570 Life sciences, biology, 610 Medicine & health, 2725 Infectious Diseases, atypical BSE, BSE
Published
2016
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12. Differential toxicity of antibodies to the prion protein

Author

Reimann, Regina R, Sonati, Tiziana, Hornemann, Simone, Herrmann, Uli S, Arand, Michael; https://orcid.org/0000-0003-2413-3177, Hawke, Simon, Aguzzi, Adriano; https://orcid.org/0000-0002-0344-6708, Reimann, Regina R, Sonati, Tiziana, Hornemann, Simone, Herrmann, Uli S, Arand, Michael; https://orcid.org/0000-0003-2413-3177, Hawke, Simon, and Aguzzi, Adriano; https://orcid.org/0000-0002-0344-6708

Abstract

Antibodies against the prion protein PrPC can antagonize prion replication and neuroinvasion, and therefore hold promise as possible therapeutics against prion diseases. However, the safety profile of such antibodies is controversial. It was originally reported that the monoclonal antibody D13 exhibits strong target-related toxicity, yet a subsequent study contradicted these findings. We have reported that several antibodies against certain epitopes of PrPC, including antibody POM1, are profoundly neurotoxic, yet antibody ICSM18, with an epitope that overlaps with POM1, was reported to be innocuous when injected into mouse brains. In order to clarify this confusing situation, we assessed the neurotoxicity of antibodies D13 and ICSM18 with dose-escalation studies using diffusion-weighted magnetic resonance imaging and various histological techniques. We report that both D13 and ICSM18 induce rapid, dose-dependent, on-target neurotoxicity. We conclude that antibodies directed to this region may not be suitable as therapeutics. No such toxicity was found when antibodies against the flexible tail of PrPC were administered. Any attempt at immunotherapy or immunoprophylaxis of prion diseases should account for these potential untoward effects.

Published
2016

13. The Priority position paper: Protecting Europe's food chain from prions

Author

Requena, Jesús R., primary, Kristensson, Krister, additional, Korth, Carsten, additional, Zurzolo, Chiara, additional, Simmons, Marion, additional, Aguilar-Calvo, Patricia, additional, Aguzzi, Adriano, additional, Andreoletti, Olivier, additional, Benestad, Sylvie L., additional, Böhm, Reinhard, additional, Brown, Karen, additional, Calgua, Byron, additional, del Río, José Antonio, additional, Espinosa, Juan Carlos, additional, Girones, Rosina, additional, Godsave, Sue, additional, Hoelzle, Ludwig E., additional, Knittler, Michael R., additional, Kuhn, Franziska, additional, Legname, Giuseppe, additional, Laeven, Paul, additional, Mabbott, Neil, additional, Mitrova, Eva, additional, Müller-Schiffmann, Andreas, additional, Nuvolone, Mario, additional, Peters, Peter J., additional, Raeber, Alex, additional, Roth, Klaus, additional, Schmitz, Matthias, additional, Schroeder, Björn, additional, Sonati, Tiziana, additional, Stitz, Lothar, additional, Taraboulos, Albert, additional, Torres, Juan María, additional, Yan, Zheng-Xin, additional, and Zerr, Inga, additional

Published
2016
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15. Prion infections and anti-PrP antibodies trigger converging neurotoxic pathways

Author

Herrmann, Uli S, Sonati, Tiziana, Falsig, Jeppe, Reimann, Regina R, Dametto, Paolo, O'Connor, Tracy, Li, Bei, Lau, Agnes, Hornemann, Simone, Sorce, Silvia, Wagner, Uli, Sanoudou, Despina, Aguzzi, Adriano; https://orcid.org/0000-0002-0344-6708, Herrmann, Uli S, Sonati, Tiziana, Falsig, Jeppe, Reimann, Regina R, Dametto, Paolo, O'Connor, Tracy, Li, Bei, Lau, Agnes, Hornemann, Simone, Sorce, Silvia, Wagner, Uli, Sanoudou, Despina, and Aguzzi, Adriano; https://orcid.org/0000-0002-0344-6708

Abstract

Prions induce lethal neurodegeneration and consist of PrPSc, an aggregated conformer of the cellular prion protein PrPC. Antibody-derived ligands to the globular domain of PrPC (collectively termed GDL) are also neurotoxic. Here we show that GDL and prion infections activate the same pathways. Firstly, both GDL and prion infection of cerebellar organotypic cultured slices (COCS) induced the production of reactive oxygen species (ROS). Accordingly, ROS scavenging, which counteracts GDL toxicity in vitro and in vivo, prolonged the lifespan of prion-infected mice and protected prion-infected COCS from neurodegeneration. Instead, neither glutamate receptor antagonists nor inhibitors of endoplasmic reticulum calcium channels abolished neurotoxicity in either model. Secondly, antibodies against the flexible tail (FT) of PrPC reduced neurotoxicity in both GDL-exposed and prion-infected COCS, suggesting that the FT executes toxicity in both paradigms. Thirdly, the PERK pathway of the unfolded protein response was activated in both models. Finally, 80% of transcriptionally downregulated genes overlapped between prion-infected and GDL-treated COCS. We conclude that GDL mimic the interaction of PrPSc with PrPC, thereby triggering the downstream events characteristic of prion infection.

Published
2015

16. Polythiophenes inhibit prion propagation by stabilizing PrP aggregates

Author

Margalith, Ilan, Suter, Carlo, Ballmer, Boris, Schwarz, Petra, Tiberi, Cinzia, Sonati, Tiziana, Falsig, Jeppe, Nystrom, Sofie, Hammarstrom, Per, Aslund, Andreas, Nilsson, K Peter R, Yam, Alice, Whitters, Eric, Hornemann, Simone, Aguzzi, Adriano, University of Zurich, and Hornemann, Simone

Subjects
1307 Cell Biology, 1303 Biochemistry, 10208 Institute of Neuropathology, 1312 Molecular Biology, 570 Life sciences, biology, 610 Medicine & health
Published
2012

18. Prion Infections and Anti-PrP Antibodies Trigger Converging Neurotoxic Pathways

Author

Herrmann, Uli S., primary, Sonati, Tiziana, additional, Falsig, Jeppe, additional, Reimann, Regina R., additional, Dametto, Paolo, additional, O’Connor, Tracy, additional, Li, Bei, additional, Lau, Agnes, additional, Hornemann, Simone, additional, Sorce, Silvia, additional, Wagner, Uli, additional, Sanoudou, Despina, additional, and Aguzzi, Adriano, additional

Published
2015
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19. Prion pathogenesis is faithfully reproduced in cerebellar organotypic slice cultures

Author

Falsig, Jeppe, Sonati, Tiziana, Herrmann, Uli S, Saban, Dino, Li, Bei, Arroyo, Karina, Ballmer, Boris, Liberski, Pawel P, Aguzzi, Adriano; https://orcid.org/0000-0002-0344-6708, Falsig, Jeppe, Sonati, Tiziana, Herrmann, Uli S, Saban, Dino, Li, Bei, Arroyo, Karina, Ballmer, Boris, Liberski, Pawel P, and Aguzzi, Adriano; https://orcid.org/0000-0002-0344-6708

Abstract

Prions cause neurodegeneration in vivo, yet prion-infected cultured cells do not show cytotoxicity. This has hampered mechanistic studies of prion-induced neurodegeneration. Here we report that prion-infected cultured organotypic cerebellar slices (COCS) experienced progressive spongiform neurodegeneration closely reproducing prion disease, with three different prion strains giving rise to three distinct patterns of prion protein deposition. Neurodegeneration did not occur when PrP was genetically removed from neurons, and a comprehensive pharmacological screen indicated that neurodegeneration was abrogated by compounds known to antagonize prion replication. Prion infection of COCS and mice led to enhanced fodrin cleavage, suggesting the involvement of calpains or caspases in pathogenesis. Accordingly, neurotoxicity and fodrin cleavage were prevented by calpain inhibitors but not by caspase inhibitors, whereas prion replication proceeded unimpeded. Hence calpain inhibition can uncouple prion replication from its neurotoxic sequelae. These data validate COCS as a powerful model system that faithfully reproduces most morphological hallmarks of prion infections. The exquisite accessibility of COCS to pharmacological manipulations was instrumental in recognizing the role of calpains in neurotoxicity, and significantly extends the collection of tools necessary for rigorously dissecting prion pathogenesis.

Published
2012

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