People
are our inspiration
Home / People / NOMIS Awardee / Adriano Aguzzi

Adriano Aguzzi

Adriano Aguzzi

Adriano Aguzzi is a 2019 NOMIS awardee and has been full professor of neuropathology and director of the Institute of Neuropathology at the University of Zurich (Zurich, Switzerland) since 1997.

Born in Pavia, Italy, Aguzzi earned an MD from the University of Freiburg Medical School (Freiburg, Germany) in 1986. Following postdoctoral studies in Vienna, he obtained the venia legendi in neuropathology at the University of Zurich in 1993. Among numerous other honors, Aguzzi has been awarded the Ernst Jung Prize, the Robert Koch Award, the EMBO Gold Medal of the European Molecular Biology Organization, the Marcel Benoist Swiss Science Prize and the Baillet Latour Health Prize, as well as two ERC Advanced Grants from the European Research Council. He holds three honorary doctorates from the Universities of Bologna, Teramo and Liège.

Aguzzi is studying the molecular basis of prion diseases (rare progressive neurodegenerative disorders), combining transgenetics with molecular and immunological techniques. His pioneering work uncovered the crucial steps in the pathogenesis of the disease, revealed the cells and molecules involved in prion neuroinvasion, and elucidated the mechanisms leading to brain damage in these diseases. Currently, Aguzzi is investigating the fundamental mechanisms of neurodegeneration. His project, Exploring the Locales of Cognitive Decline: Cellular and Molecular 3D Atlases of Brain Pathology in Aging and in Neurodegeneration, proposes combining high-content three-dimensional morphology with sophisticated fluorochrome chemistry and molecular methods of genome interrogation/perturbation. These techniques will enable the creation of detailed atlases of the cell types that drive damage in various models of neurodegeneration.

Adriano Aguzzi | Awards Film

Adriano Aguzzi | Insights Film

Adriano Aguzzi's News

NOMIS Awardee Adriano Aguzzi and colleague Martin Kampmann have published a review article in Science exploring progress in treatment for neurodegenerative diseases. They ask the question, “What accounts for the […]

NOMIS Awardee Adriano Aguzzi and colleague Elena De Cecco published an article in Science on Oct. 2, 2020, exploring the evolution of prions. Paradigm shifts are drivers of scientific progress, […]

Dear NOMIS friends and partners, We would like to remind you that following the 2019 NOMIS Distinguished Scientist and Scholar Award you will be able to view additional photos in […]

Adriano Aguzzi's Insights

Abstract: The progressive accumulation of insoluble aggregates of the presynaptic protein alpha-synuclein (α-Syn) is a hallmark of neurodegenerative disorders including Parkinson's disease (PD), Multiple System Atrophy, and Dementia with Lewy Bodies, commonly referred to as synucleinopathies. Despite considerable progress on the structural biology of these aggregates, the molecular mechanisms mediating their
Abstract: Conventional methods of measuring affinity are limited by artificial immobilization, large sample volumes, and homogeneous solutions. This protocol describes microfluidic antibody affinity profiling on complex human samples in solution to obtain a fingerprint reflecting both affinity and active concentration of the target protein. To illustrate the protocol, we analyze the
Abstract: Effective public health measures against SARS-CoV-2 require granular knowledge of population-level immune responses. We developed a Tripartite Automated Blood Immunoassay (TRABI) to assess the IgG response against three SARS-CoV-2 proteins. We used TRABI for continuous seromonitoring of hospital patients and blood donors (n = 72′250) in the canton of Zurich
Abstract: The cellular prion protein PrPC mediates the neurotoxicity of prions and other protein aggregates through poorly understood mechanisms. Antibody-derived ligands against the globular domain of PrPC (GDL) can also initiate neurotoxicity by inducing an intramolecular R208-H140 hydrogen bond (“H-latch”) between the α2-α3 and β2-α2 loops of PrPC. Importantly, GDL that