Prion Biology Laboratory

Phone: +39 040 3787 760
Fax: +39 040 3787 702
Office: 545
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 It is now recognized that familial prion diseases are caused by insertion and point mutations found throughout the prion protein gene. They have been linked to Gerstmann-Sträussler-Scheinker syndrome, fatal familial insomnia, and familial Creutzfeldt-Jakob disease. The mechanism by which these mutations promote generation from the normal PrPC to the pathogenic PrPSc conformation is still unclear. They may increase the likelihood of misfolding by thermodynamic destabilization of PrPC, or PrP mutants may escape quality control cellular pathway and accumulate inside the cell. In addition, mutations may change surface properties promoting an abnormal interaction between PrP and other not yet identified interactors.
Gabriele Giachin’s project is focused on the effect of pathological point mutations on the prion protein structure. The lab uses different approaches, including recombinant DNA technology, NMR and biophysical studies using recombinant prion protein produced via fermenter system. Current research interests include the following projects: I) NMR study on the human prion protein carrying pathological point mutation; II) biophysical studies on HuPrP mutants (i.e. circular dichroism, fluorimetric analysis); III) role of mutation in the binding activity between PrP and some interactors.

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