Thursday 3 March 2022
Spring Interdisciplinary Research Lecture: From a Chemistry degree to Structural Biologist in five career moves
- Speaker: Dr Pietro Roversi, Italian National Research Council (CNR) Institute of agricultural, biology and biotechnology
- Time: 5.00pm – 6.00pm (GMT)
- Location: TBC (email email@example.com for further details)
The seminar will include a brief discussion of Dr. Roversi’s professional journey, and will focus on the transition from Chemistry to Biology over the course of more than 25 years in academic research (with a three-year stint in industry).
Dr. Roversi's biography
As of June 1st 2021, Pietro works at the Institute of Agricultural Biology and Biotechnology of the Italian National Research Council in Milano, Italy.
Pietro grew up in Verona, Italy and studied Chemistry at the University of Milano (1987-1993) where he graduated with honours and a passion for structural science. He stayed on in Milano to study for a PhD in structural chemistry under the supervision of Prof. Riccardo Destro, working on the multipole and Maximum Entropy modelling of charge densities in crystalline solids (1993-1997). Dr. Destro's helium cryostat allowed diffraction at temperatures as low as 18 K. During his PhD Pietro was fortunate enough to spend a year in Cambridge, working with Dr. Gerard Bricogne at the MRC Laboratory of Molecular Biology; and he returned there as a postdoc after his PhD (1997-2000), funded by a Marie Curie Training and Mobility of Researchers Fellowship. With Dr. Bricogne Pietro learnt macromolecular crystallographic theory and computing, and contributed to the writing of the macromolecular crystallography refinement package Buster-TNT. He continued working with Dr. Bricogne at Global Phasing Ltd. after leaving the MRC-LMB (2000-2003).
Pietro then moved to the group of Prof. Susan Lea in the Biochemistry Department of Oxford University, where he was given a chance of learning basic biochemistry skills, growing his own protein crystals and determining macromolecular structures of human complement proteins and bacterial proteins involved in infection mechanisms (2003-2006). In 2006 Pietro followed Prof. Lea to her new lab in the Oxford Sir William Dunn School of Pathology. Pietro has been involved in the teaching of macromolecular crystallography and biochemistry to graduate students in the lab and at the occasional international school. For the five years' stint 2008-2012 he was responsible for running the Biochemistry Honour school at Lincoln College, Oxford. In 2011 Pietro managed to determine the crystal structure of human complement Factor I that he spent seven years purifying from plasma under the guidance of Prof. Bob Sim. This is where Pietro's interest for glycoprotein folding started (some of the mutants of human complement Factor I were not secreted but it was not immediately clear why from the structure).
After nine years with Prof. Lea, in 2012 Pietro won a one-year Fellowship offered by the Basque Foundation of Science (aka Ikerbasque) to spend a sabbatical year in the Basque Country and returned to Oxford in 2013 to join Prof. Nicole Zitzmann's laboratory at the Oxford Glycobiology Institute of the Biochemistry Department of Oxford University. In the six years in Prof. Zitzmann's lab (2013-2018) Pietro and colleagues determined the three most important structures of the Endoplasmic Reticulum glycoprotein folding control: ER Glu I, ER Glu II and UGGT.
In 2017 Pietro was appointed to a LISCB Wellcome Trust ISSF Fellowship 2018-2021 and in July 2018 started his own research group at LISCB at Leicester University. In 2019 came the appointment to an open-ended teaching and research contract to teach Chemistry to the undergraduate students of the Natural Sciences BSc and MSc courses.
Pietro left Brexit Britain in 2021 to join the National Research Council Institute of Agricultural Biology and Biotechnology (IBBA-CNR) in Milano, Italy. Back where he started! Pietro retains an Honorary Lectureship at the University of Leicester.
In order to develop and test ERQC/ERAD partial inhibitors as broad-spectrum rescuers of secretion for responsive mutant glycoproteins, Pietro and his group investigate the molecular mechanisms by which the eukaryotic cell either retains misfolded glycoproteins in the ER and/or degrades them by ERAD. Cryo-EM and X-ray crystallography of recombinantly expressed purified ERQC/ERAD proteins and their complexes with misfolded substrates will be used to generate a range of biochemical and biological hypotheses, then tested by in vitro and in cellula assays, and in vivo experiments using the plant as a model organism.