Protein macro-assembly and Prion diseases

Prion diseases are deadly infectious neurodegenerative diseases affecting human and other mammalian species. The etiology of prion disease differs from the conventional infectious diseases and leads to introduce the general concept of infectious amyloidosis.

Our main field of investigation address the molecular mechanism of structural information transference during mammalian prion replication and the neurotoxicity mechanisms of misfolded proteins.

Our investigations cover a broad panel of expertises: from physical-chemistry and drug design to the molecular characterisation of the prion propagation on transgenic mice and cell models.

We also intensively contribute to the development of new methodology and tools in the field of infectious proteins.

The most percussive results obtained by our group address major topics in prion field. We identified the minimal structural perturbation that ignites the replication process and established a relation between infectivity and size of PrPSc assemblies.

The accumulation of fundamental knowledge leads us to design ligand that inhibits the prion replication ex vivo. The characterization of the prion passage from animals to human was one of the important topics that we also addressed using transgenic mice.

Beside these results, our group intensively built gateways between prion disease and other amyloidosis as Alzheimer and type 1 Parkinson. As our group have a multidisciplinary approach, our perspective is to gain from fundamental research to go further in the etiology of infectious amyloidosis and rational drug design.

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