University of Cambridge’s Professor Sir Greg Winter shares 2018 Nobel Prize in Chemistry
PUBLISHED: 13:44 03 October 2018 | UPDATED: 11:52 04 October 2018
Illustrations: © Niklas Elmehed, firstname.lastname@example.org
The master of Trinity College said it “came as a shock” after he was honoured for phage display work that led to new antibody drugs
The University of Cambridge’s Professor Sir Greg Winter has been jointly awarded the 2018 Nobel Prize in Chemistry for pioneering work that has led to a host of new medicines.
Prof Winter, the master of Trinity College, shares the prize with US-based Frances Arnold and George Smith, for his use of phage display for the directed evolution of antibodies.
The first pharmaceutical based on the method, adalimumab, was approved in 2002 and is the world’s biggest-selling drug, trading as Humira. It is used to treat rheumatoid arthritis, psoriasis and inflammatory bowel diseases.
Since then, phage display has produced antibodies that can neutralise toxins, counteract autoimmune diseases and cure metastatic cancer.
Announcing the £770,000 prize this morning (Wednesday October 3, 2018), the Royal Swedish Academy of Sciences awarded one half to Frances Arnold, of the California Institute of Technology, for the “directed evolution of enzymes” and the other half jointly to George Smith, a professor at the University of Missouri, and Prof Winter, “for the phage display of peptides and antibodies”.
The Nobel Assembly said: “The 2018 Nobel Laureates in Chemistry have taken control of evolution and used it for purposes that bring the greatest benefit to humankind.
“Enzymes produced through directed evolution are used to manufacture everything from biofuels to pharmaceuticals. Antibodies evolved using a method called phage display can combat autoimmune diseases and in some cases cure metastatic cancer.”
Born in 1951 in Leicester, Sir Greg studied natural sciences at Trinity College, Cambridge, and was awarded his PhD, also from Cambridge, in 1977.
He was a senior research fellow before becoming master, and has had a distinguished career in Cambridge.
A genetic engineer, he is best known for his work on humanised and human therapeutic antibodies.
He founded Cambridge Antibody Technology, which was acquired by AstraZeneca for £702million in 2006, and was responsoble for the technology that created Humira. He also founded Domantis, which was acquired by GlaxoSmithKline, and Bicycle Therapeutics, based at Babraham Research Campus.
He founded these while based at the Medical Research Council’s Laboratory of Molecular Biology (MRC LMB) and the MRC Centre for Protein Engineering (CPE).
Prof Winter said: “It came as a bit of a shock, and I felt a bit numb for a while. It’s almost like you’re in a different universe. For a scientist, a Nobel Prize is the highest accolade you can get, and I’m so lucky because there are so many brilliant scientists and not enough Nobel Prizes to go around.
“When I was working on antibodies at the LMB, I had no idea they would be commercially successful. We had to convince people that they could be used as therapeutics.
“I had fantastic mentors here, including Fred Sanger and César Milstein... There’s a culture here that we should tackle really difficult problems, which sometimes take many years.
“The commitment to long-term research is so important.”
Prof Winter becomes the 107th Nobel Affiliate of Cambridge. In 2017, the MRC Laboratory of Molecular Biology’s Richard Henderson shared the Nobel Prize in Chemistry for his work on cryo-electron microscopy, making it two in a row for the lab, which now has an incredible 12 Nobel Prizes to its name, including nine in chemistry and three in physiology or medicine.
Professor Fiona Watt, executive chair of the MRC, said: “Huge congratulations to Professor Sir Gregory Winter on this well-deserved accolade.
“The pioneering breakthrough work by Sir Greg and his colleagues at the MRC Laboratory of Molecular Biology to develop humanised, and human, therapeutic antibodies has initiated a pharmaceutical revolution and led to the establishment of a whole new class of drugs which have helped millions of patients worldwide.
“Today, monoclonal antibodies account for a third of all new treatments, such as the arthritis drugs adalimumab and Humira, the multiple sclerosis drug Lemtrada and the breast cancer drug Herceptin.
“The MRC is proud to have funded Sir Greg Winter over many years to conduct this research. His success is a testament to the MRC’s strategy for long-term investment of taxpayers’ money in fundamental discovery research. This is the second Nobel celebration in two years at the MRC Laboratory of Molecular Biology – no wonder it’s known as the ‘Nobel Prize factory’.“
Prof Winter’s research at the LMB spanned from 1973 to 2014. He was a programme leader, became joint head of the protein and nucleic acid chemistry division, then deputy director of the LMB and deputy director of CPE. He has been emeritus at the LMB since 2014.
Jan Löwe, LMB director, added: “I am most delighted that an LMB scientist has been given the ultimate scientific accolade. It highlights the LMB’s unique culture, but more importantly, rewards one of the most innovative and entrepreneurial scientists of his generation.”
Prof Patrick Maxwell, Regius professor of physic and head of the School of Clinical Medicine at the University of Cambridge, said: “I am absolutely delighted that Sir Greg’s work has been recognised with a Nobel Prize. The work for which the prize is awarded was carried out on the Cambridge Biomedical Campus. It directly led to the power of monoclonal antibodies being harnessed for treatment of disease. Medicines based on Sir Greg’s discovery have transformed the lives of patients around the world. His inventions really have produced silver bullets that have transformed the way medicine is practised.”
Prof Sir Alan Fersht, former master of Gonville & Caius, said: “Greg Winter is an outstandingly creative scientist of a practical bent. He has applied his skills and imagination to the benefit of humankind to create, amongst other inventions, novel engineered antibodies that have formed the basis of a new pharmaceutical industry to treat disease and cancer. It is a thoroughly worthy Nobel Prize.”
Prof Dame Carol Robinson, Royal Society of Chemistry president, said: “Today’s Nobel Prize in chemistry highlights the tremendous role of chemistry in contributing to many areas of our lives including pharmaceuticals, detergents, green catalysis and biofuels. It is a great advert for chemistry to have impact in so many areas.
“Directed evolution of enzymes and antibody technology are subjects that I have followed with keen interest; both are now transforming medicine. It would have been hard to predict the outcome of this research at the start – this speaks to the need for basic research.
“I am delighted to see these areas of chemistry recognised and congratulate all three Nobel Laureates.”
Prof Winter was elected a member of the European Molecular Biology Organisation in 1987, a fellow of the Royal Society in 1990 and fellow of the Academy of Medical Sciences in 2006. He is a fellow or honorary fellow of many other professional organisations. He received a knighthood for services to molecular biology in 2004.
UK Research and Innovation chief executive Professor Sir Mark Walport said: “Sir Greg Winter’s pioneering research, much of it supported by the Medical Research Council, has made major contributions to global health and wellbeing.
“The phage display method he developed led to a new range of targeted therapies and effective treatments for conditions such as rheumatoid arthritis and cancer.
“On behalf of UKRI, I would like to send our warmest congratulations to Sir Greg on the extremely well-deserved award of the Nobel Prize in Chemistry. We are all delighted for him.”
Frances Arnold, who becomes only the fifth woman to win the Nobel Prize for Chemistry, won the prize for the “directed evolution of enzymes”- these are proteins that catalyse chemical reactions.
She has since refined those methods, which are now routinely used to develop new catalysts. Her enzymes have helped to create more environmentally-friendly manufacturing of chemical substances, such as pharmaceuticals, and the production of renewable fuels for a greener transport sector.
George Smith developed phage display in 1985. It uses a bacteriophage – a virus that infects bacteria – to evolve new proteins.