MDS Newsroom

News Release

Contributed by Dr. Roger A. Barker
Consultant Neurologist
John van Geest Centre for Brain Repair and Department of Neurology
University of Cambridge
Cambridge, UK

September 2013

Maria Grazia Spillantini is the Professor of Molecular Neurology at the University of Cambridge and this summer she became a Fellow of the Royal Society for her work on neurodegenerative disorders of the central nervous system. This accolade came as no surprise to those who know Maria and have followed her work over the years, even though to her it came as a big surprise - I know as I was sitting next to her in a meeting when the email informing her of her election arrived!

Maria arrived in Cambridge in the 1980s after completing her undergraduate and some postgraduate studies at the University of Florence. She started working in the MRC Laboratory of Molecular Biology (MRC-LMB) where she gained her PhD and subsequently moved into the then newly built Cambridge (now John van Geest) Centre for Brain Repair in 1997, where she has remained ever since. During her time at the MRC-LMB she started working with Michel Goedert and between them they have generated much, including seminal studies in tau and alpha synuclein biology and their related neurodegenerative diseases.

This work has been transformative and in particular Maria has made two major discoveries in this regard:

(i) She was the first to show that alpha synuclein is the major component of Lewy bodies. This finding in 1997 came shortly after the discovery of the first genetic cause of PD, a mutation in the alpha synuclein gene, and proved that this protein is associated with the defining pathological hallmark of PD which moved it centre stage where it has remained ever since. She then went on in the following year to show that this protein is the major component of the glial cytoplasmic inclusions characteristic of MSA. All of which gave rise to the concept of neurodegenerative disorders being defined by their protein pathology- the alpha synucleinopathies;

(ii) She was also (with Michel Goedert and colleagues) the first to describe the 6 different isoforms of tau and the existence of 4 repeat tau. She also showed that tau mutations could underlie certain forms of familial frontotemporal dementia. This again proved that abnormalities in tau could cause disease in their own right and as such may be a key player in the pathogenesis of a range of neurodegenerative disorders and not just linked to Alzheimer’s disease.

She has subsequently gone on to make further substantial contributions in both these fields, especially around the mechanism of disease pathogenesis and how these proteins could, and do, contribute to disease states. This led to her challenging the mechanism by which alpha synuclein causes disease as well as recognizing that the early pathology of PD starts at the synapse. She has also identified new functions of tau in axonal transport as well as ways in which alpha synuclein and tau may interact to cause neuronal loss.

This she has done with great imagination and determination and through this, she has inspired many who have worked and collaborated with her. All of this is coupled with a generosity and curiosity that makes her such a popular and exceptional scientist. But for me what distinguishes Maria is her genuine desire to solve a problem, her modesty and kindness and her encyclopaedic knowledge of this field – a field which she has helped define over the last 25 years.