Prof. Dr. Giuseppe Legname
Scuola Internazionale Superiore di Studi Avanzati, Trieste, Italy
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Academic Career Length
36Years (1991-Present)
(Calculated once Scilit publication data is synced: current year − year of first publication + 1)
Representative Publications
View All Publications30 July 2004 in Science
Journal Article
Giuseppe LegnameIBIlia V. Baskakov
Ilia V. Baskakov
HNHoang-Oanh B. Nguyen
Hoang-Oanh B. Nguyen
DRDetlev Riesner
Detlev Riesner
FCFred E. Cohen
Fred E. Cohen
SPStanley B. Prusiner
Stanley B. Prusiner +1
Recombinant mouse prion protein (recMoPrP) produced in Escherichia coli was polymerized into amyloid fibrils that represent a subset of β sheet–rich structures. Fibrils consisting of recMoPrP(89–230) were inoculated intracerebrally into transgenic (Tg) mice expressing MoPrP(89–231). The mice developed neurologic dysfunction between 380 and 660 days after inoculation. Brain extracts showed protease-resistant PrP by Western blotting; these extracts transmitted disease to wild-type FVB mice and Tg mice overexpressing PrP, with incubation times of 150 and 90 days, respectively. Neuropathological findings suggest that a novel prion strain was created. Our results provide compelling evidence that prions are infectious proteins.
16 August 2001 in Nature
Journal Article
DPDavid Peretz
David Peretz
RWR. Anthony Williamson
R. Anthony Williamson
KKKiotoshi Kaneko
Kiotoshi Kaneko
JVJulie Vergara
Julie Vergara
ELEstelle Leclerc
Estelle Leclerc
SPStanley B. Prusiner
Stanley B. Prusiner
+7
1 June 2002 in Journal of Biological Chemistry
Journal Article
IBIlia V. Baskakov
Ilia V. Baskakov
Giuseppe LegnameMBMichael A. Baldwin
Michael A. Baldwin
SPStanley B. Prusiner
Stanley B. Prusiner
FCFred E. Cohen
Fred E. Cohen
In vivo under pathological conditions, the normal cellular form of the prion protein, PrPC (residues 23–231), misfolds to the pathogenic isoform PrPSc, a β-rich aggregated pathogenic multimer. Proteinase K digestion of PrPSc leads to a proteolytically resistant core, PrP 27–30 (residues 90–231), that can form amyloid fibrils. To study the kinetic pathways of amyloid formation in vitro, we used unglycosylated recombinant PrP corresponding to the proteinase K-resistant core of PrPSc and found that it can adopt two non-native abnormal isoforms, a β-oligomer and an amyloid fibril. Several lines of kinetic data suggest that the β-oligomer is not on the pathway to amyloid formation. The preferences for forming either a β-oligomer or amyloid can be dictated by experimental conditions, with acidic pH similar to that seen in endocytic vesicles favoring the β-oligomer and neutral pH favoring amyloid. Although both abnormal isoforms have high β-sheet content and bind 1-anilinonaphthalene-8-sulfonate, they are dissimilar structurally. Multiple pathways of misfolding and the formation of distinct β-sheet-rich abnormal isoforms may explain the difficulties in refolding PrPSc in vitro, the need for a PrPSc template, and the significant variation in disease presentation and neuropathology.
1 December 2001 in Journal of Molecular Biology
Journal Article
GSGerold Schmitt-Ulms
Gerold Schmitt-Ulms
Giuseppe LegnameMBMichael A Baldwin
Michael A Baldwin
HBHaydn L Ball
Haydn L Ball
NBNicole Bradon
Nicole Bradon
SPStanley B Prusiner
Stanley B Prusiner
+5
13 December 2013 in Cell Death & Differentiation
Journal Article
PJP Joshi
P Joshi
ETE Turola
E TurolaAMAna Ruiz Moreno
Ana Ruiz MorenoABA Bergami
A Bergami
DLD D Libera
D D LiberaCFChiara Fenoglio
Chiara Fenoglio +8
15 May 2003 in Biochemistry
Journal Article
CBColin S. Burns
Colin S. BurnsEAEliah Aronoff-Spencer
Eliah Aronoff-Spencer
Giuseppe LegnameSPStanley B. Prusiner
Stanley B. Prusiner
WAWilliam E. Antholine
William E. Antholine
GMGlenn L. Millhauser
Glenn L. Millhauser +2
About Me
Giuseppe Legname earned his Doctor of Philosophy at the University of Warwick, UK. After a long spell in industry in the field of
immunotherapy, he moved to the National Institute for Medical Research (NIMR), Medical Research Council in London, UK, as a Research Associate. In 1999, Giuseppe Legname became an Assistant Adjunct Professor and later an Associate Adjunct Professor at the Institute for Neurodegenerative Diseases (IND), University of California, San Francisco, USA. In 2006, he joined the faculty of SISSA in Trieste as an Associate Professor at the Department of Neuroscience. Currently, Giuseppe Legname is a Full Professor of Biochemistry at SISSA (Scuola Internazionale Superiore di Studi Avanzati, Trieste, Italy), specializing in neuroscience and neurodegenerative diseases, particularly prion biology. His work covers molecular and cellular biochemistry, focusing on the structural mechanisms of protein misfolding and its implications in neurodegeneration. Over the course of his career, he has extensively contributed to understanding the structural traits of prion proteins, their functional interactions, and therapeutic strategies for related diseases. He has over 20 years of teaching and mentoring experience, including the supervision of Ph.D. students, and has been involved in numerous international collaborations and scientific organizations.