Reactions to the news that the Nobel Prize in Chemistry has been awarded to three scientists for ‘harnessing the power of evolution’, including Sir Gregory Winter from the Laboratory of Molecular Biology in Cambridge.
Dr Mene Pangalos, Executive Vice President, Innovative Medicines & Early Development Biotech Unit, AstraZeneca, said:
“Congratulations to Sir Gregory Winter from all at AstraZeneca and MedImmune on his much deserved Award. Greg’s pioneering work with George Smith on phage display has been instrumental in allowing researchers across the world develop new medicines for some of the toughest diseases. It’s a proud day for Greg, for the MRC, for Cambridge, and for UK science. Coming on top of Monday’s Nobel Award in Physiology and Medicine to James P. Allison and Tasuku Honjo for their work in immuno-oncology it’s clear evidence of how today’s science is driving better health and healthcare across the world.”
Dr Jane Osbourn, Vice President, Research and Development, MedImmune, said:
“Congratulations to Gregory. Over the past 30 years the development of antibody therapeutics has delivered a step change in the quality of life for many patients. Underpinning this, the technique of phage display provided a fundamental platform from which, in 2002, the world’s first fully human therapeutic antibody was launched, blazing the trail for many other antibody-based medicines. Greg passionately pioneered and championed the development of this innovative technology, and his intellectual insights and dynamism as a world-leader in antibody engineering were invaluable in the development of the field. He was also entrepreneurial in his approach to ensuring the impact of his discoveries went beyond the academic applications and he played a pivotal role in the establishment of Cambridge Antibody Technology, now MedImmune, the global biologics R&D arm of AstraZeneca.”
Prof Magdalena Zernicka-Goetz, Professor of Mammalian Development and Stem Cell Biology, University of Cambridge, said:
“Truly outstanding breakthrough. This acknowledges the first manipulation of proteins to give them ‘designer’ functions that have medical applications.
“I am delighted that Greg Winter and George Smith share this prize with Frances Arnold, a pioneering woman scientist in this field and a wonderful human being.”
Prof Sir Robert Lechler PMedSci, President of The Academy of Medical Sciences, said:
“I am delighted to hear the great news that our Fellow Gregory Winter has jointly won this year’s Nobel Prize in Chemistry. His pioneering drug discovery work has already provided life-changing medicines to those suffering from rheumatoid arthritis, inflammatory bowel diseases and psoriasis and may transform the future treatments of metastatic cancers and autoimmune diseases.
“This is a shining example of how a curious, expert mind can lead to the development of live-saving techniques and medicines within the field of basic scientific research.”
Prof Jeremy Farrar, Director of Wellcome, said:
“Congratulations to the new Nobel laureates, their work transformed all our lives and will do so for decades to come. It is work of critical importance, supporting long term discovery, science and translation. I’d like to pay tribute to the MRC, the MRC LMB, NIH & many others, for their contribution to science, innovation, entrepreneurship and human health.
“It is impossible to overstate the implications of this work in all our daily lives – biofuels, chemicals, environment, medicine and so much more e.g. treatment of cancer, arthritis, Crohn’s, UC and infections – there are patients with Ebola being treated today with antibody therapies. This has impacted so much of modern medicine.
“Plus, it is a huge role these three have played in science, mentorship, providing a rewarding diverse exciting research culture and environment, the convergence of science – physical sciences as drivers of biology and health. Plus translation, start-ups commercialisation and economic growth.
“There are few better examples of why it is so important for governments, industry, and philanthropy to invest in long-term blue-sky science, in people, ideas and teams, to take risks on infrastructure and let people follow their ideas and their dreams. Science is part of all our culture.”
Dr Iain Foulkes, Cancer Research UK’s executive director of research and innovation, said:
“It’s wonderful to see this research honoured in today’s Nobel Prize for Chemistry, and congratulations to all three recipients. The ability to directly manipulate proteins and create new pharmaceuticals is a phenomenally powerful technique, allowing researchers to make rapid progress in the search for the next generation of cancer drugs.
“This work has directly influenced Cancer Research UK’s efforts to accelerate the development of new biological therapies. In particular, George Smith’s work on phage display is fundamental to our antibody discovery and engineering laboratory in Cambridge, where we’ve partnered with MedImmune – a company co-founded by Greg Winter – to create a resource for UK researchers who are working on new ways to treat and diagnose cancer. We’re also working with Bicycle Therapeutics, another company Greg Winter co-founded, to run trials of an entirely new class of cancer drugs which could more precisely target tumour cells.”
Prof Sir Mark Walport, UK Research and Innovation Chief Executive, 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.”
Prof Anne Cooke FMedSci, Emeritus Professor of Immunobiology, University of Cambridge, said:
“Greg Winter is an enormously creative scientist who has made major contributions to translational medicine through basic science.”
Prof Fiona Watt, Executive Chair of the Medical Research Council, 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’!”
Dr Louisa James, Lecturer in Immunology, Blizard Institute, Queen Mary University of London, said:
“It is fantastic that phage display has been recognised with a Nobel Prize, this technique revolutionised our ability to harness antibodies for the diagnosis and treatment of disease.
“In phage display billions of individual molecules, such as antibodies, are displayed on the surface of small particles called phages. The molecules with desirable properties can then be singled out from the billions of others. The beauty of phage display is that the genetic information – the instruction manual for making that molecule of interest – is preserved on the phage particle so it can then be produced in much larger quantities.
“Phage display has been particularly valuable for antibody technology because every antibody molecule has a unique genetic code and it is impossible to identify antibodies that have useful properties just by looking at that genetic code. Phage display allows us to fish out that one in a billion antibody that can treat or even cure disease.”
Prof Venki Ramakrishnan, President of the Royal Society, said:
“Thanks to Greg Winter’s pioneering research into monoclonal antibodies at the MRC’s Laboratory of Molecular Biology, people who have breast cancer, arthritis, asthma and leukemia the world over are already benefiting from new drugs, with many more in development. UK companies developing antibody technologies based on Greg’s work have also been a startup success story, with these drugs being worth billions globally. I am delighted that his great achievement has been recognised with the Nobel. It is a richly deserved honour for him, the MRC’s Laboratory of Molecular Biology, which has produced so many Nobel Prize winners, and British science.”
Daniel Davis, Professor of Immunology, University of Manchester, and author of The Beautiful Cure, which discusses the work that lead to this Nobel Prize, said:
“This is thrilling. The use of phage display to create new antibodies has been exceptionally important in science and medicine. As one example, Humira, developed with this technology, is used by thousands of people for the treatment of rheumatoid arthritis and other auto-immune diseases. With this medicine, far fewer people with rheumatoid arthritis are forced to use a wheelchair. This, along with the Nobel Prize for new cancer treatments awarded on Monday, is also exciting on another level – because it shows how curiosity about how things work leads us to blockbuster medicines to improve our lives.”
Mary Archer, Chair, Science Museum Group, said:
“So thrilled to see Greg Winter’s stunning lifetime of work recognised by the Nobel Committee. From his work as a posytdoc with Campath onwards, he’s always been a winner.”
Dr Oliver Jones, Associate Professor of Chemistry, RMIT University in Melbourne, Australia, said:
“Many congratulations to Professors Arnold, Smith and Winter. This award is great news. At first glance it may seem that the Chemistry Nobel has been ‘biologised’ again. It is sometimes hard to see how an enzyme, or a phage, are ‘chemistry’ – but they are! It is chemistry that governs the shape of these molecules, which in turn affects their function. It is chemistry that controls how enzymes interact with their substrates or phages bind to bacteria and how antibodies neutralise toxins and cure disease. Chemistry underpins so many things in our lives, even if it is not always immediately obvious and it is great that these discoveries are getting recognised. Congratulations again to all!”
Dr Andrea Sella, Professor of Inorganic Chemistry, UCL, said:
“A lot of people in chemistry Departments will be perhaps feel miffed this morning because, once again, the Nobel Prize has ‘gone to biologists’. And yet, this really misses a very important point.
“At the end of the 19th century it was clear that biology could not advance without an understanding of its chemical basis. Starting perhaps with chromatography, chemistry began to provide the tools that allowed scientists to deconstruct the biological, but also a lot of parts of the physical, world that one might think of as ‘condensed matter’. In parallel with the growth of traditional chemistry was the rise of biochemistry and molecular biology, but also of geochemistry and lots of solid state physics, all of which came to rely on the methods and tools that were being developed by chemists. The result was that chemistry came to invade and become an integral part of the rest of science, including molecular biology and biochemistry.
“People with chemistry degrees are everywhere from forensics labs to electrical engineering departments. All of those phrases like genomics, metabolomics and so involve the application and automation of highly refined chemical tools to attack higher order systems questions in other disciplines.
“The key consequence is that now chemistry encompasses huge tracts of other disciplines. For chemists, this is both their triumph and their curse. Chemistry is everywhere.”
Prof Herman Waldmann, Sir William Dunn School of Pathology, University of Oxford, said:
“Greg has pioneered ways of obtaining human antibodies using bacteriophages so obviating the need for any immunisation of animals or humans to generate them. His technology has also enabled the generation of improvements in the binding power of any given antibody.
“This was a far sighted discovery achieved at a time when immunologists were grappling with difficulties around immunisation to produce desirable antibodies, and will have broad implications in medical diagnosis and treatment, as well as enabling the generation of valuable research reagents.”
Prof Lawrence Young, Director of Cancer Research Centre, University of Warwick, said:
“Phage display is a way of presenting proteins or peptides and selecting them for specific properties/functions. Think of phage display as a library where every book is a separate protein and you can select a book based on a particular feature – fiction or non-fiction, genre (crime, thriller, biography etc.) or more specifically on author, publication year etc. So it is with phage display where you can select proteins or bits of proteins for specific properties e.g. ability to bind to another specific protein (useful for drug discovery), generating antibodies and improving their activity, identifying the targets of the immune response in autoimmune disease and cancer etc. etc.”
Further information from the Royal Society of Chemistry about one of the winners, Prof Frances Arnold (please note there is an image available of Prof Frances Arnold giving a talk at the RSC; if you’d like that please let me know):
Nobel laureate Professor Frances Arnold recently spoke to the Royal Society of Chemistry about her research. She said: “Chemists are inspired and awed by the biological world but what they should really be inspired by is the process by which biology discovers chemistry: that’s called evolution. I practise evolution in the laboratory. We can evolve enzymes, these amazing catalysts that biology has, to do chemistry that was invented by humans, not by nature.
“This marvellous process by which innovation happens in the biological world, I contain that in the laboratory and I can make enzymes that catalyse wonderful reactions, making molecules that chemists have a very hard time making. It is a thrilling time to be in the biological chemistry interface.”
Prof Alan Boyd, President, Faculty of Pharmaceutical Medicine, said:
“This is great news that Sir Greg Winter, together with Frances Arnold and George Smith have been awarded the Noble Prize for Chemistry for the pioneering work that they did that led to the development of antibodies. The use of antibodies has resulted in a paradigm shift in the way that we now treat so many diseases which has brought significant benefits to patients across the world and will continue to do so for years to come.”
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 Douglas Kell, Professor of Bioanalytical Science, University of Manchester, said:
“Fantastic news. Really well deserved. Nobels commonly go to folk who develop methods that revolutionise practice or understanding. These methods are entirely general and have done both.”
The original press release can be found here.