E014 – Prion Diseases

Objectives and lines of research


The work of our group focuses on investigating the role of the misfolding of certain proteins in the mechanisms that trigger certain encephalopathies. Specifically, we investigate three diseases, prion diseases, Celia’s encephalopathy and schizophrenia.
Prion diseases are deadly neurodegenerative diseases caused by misfolding of the prion protein, PrP. Once misfolded, PrP becomes a prion, that is, a protein capable of spreading its misfolded conformation to other PrP units.
Our work focuses on elucidating the structure of the prion, which is essential to understand the mechanism of spread of the disease. For this we use biochemical, electron microscopy and NMR techniques.
Celia’s encephalopathy is a rare inherited neurodegenerative disease caused by a particular mutation of the gene that encodes seipin. It was discovered and described by David Araujo just a few years ago, in collaboration with our group. Seipin is a protein involved in the formation of fat droplets, for example in adipocytes, but also abundantly expressed in the brain.
Finally, schizophrenia is a well-known and prevalent disease, although its molecular mechanisms are poorly understood, beyond alterations in dopaminergic and glutamatergic signaling systems, well characterized but whose ultimate cause is a mystery. Starting from the hypothesis recently formulated by Carsten Korth, according to which the misfolding and aggregation of the brain protein DISC1 could play an important role in the pathology of schizophrenia, we are studying this protein and characterizing its functions through proteomic approaches.



Research team
Rodríguez Requena, Jesús
Predoctoral researchers
Bugallo Codeseira, Yaiza
Fernández Flores, Leticia
López Lorenzo, Nuria



Technical support staff
Veiga Sans, Sonia

Lead researcher

Jesús Rodríguez Requena

Jesús Rodríguez Requena