Gregory Winter

Sir Gregory Paul Winter CBE FRS FMedSci (born

Sir
14 April 1951)[6][7] is a Nobel Prize-winning English
molecular biologist best known for his work on the Gregory Winter
CBE FRS FMedSci
therapeutic use of monoclonal antibodies. His research
career has been based almost entirely at the MRC
Laboratory of Molecular Biology and the MRC Centre
for Protein Engineering, in Cambridge, England.

He is credited with having invented techniques to both

humanize (1986) and, later, to fully humanize using
phage display, antibodies for therapeutic
uses. [5][8][9][10][11][12][13] Previously, antibodies had
been derived from mice, which made them difficult to
use in human therapeutics because the human immune
system had anti-mouse reactions to
them. [6][14][15][16][17][18] For these developments
Winter was awarded the 2018 Nobel Prize in
Chemistry along with George Smith and Frances
Arnold.[19][20]
Winter in 2016
He is a Fellow of Trinity College, Cambridge and was Master of Trinity College, Cambridge
appointed Master of Trinity College, Cambridge on 2 In office
October 2012, remaining in office until 2019. From 2012–2019
2006 to 2011, he was Deputy Director of the
Preceded by Baron Rees of Ludlow
Laboratory of Molecular Biology, Medical Research
Council, acting Director from 2007 to 2008 and Head Succeeded by Dame Sally Davies
of the Division of Protein and Nucleic Acids Personal details
Chemistry from 1994 to 2006. He was also Deputy Born Gregory Paul Winter
Director of the MRC Centre for Protein Engineering 14 April 1951
from 1990 to its closure in 2010.[21][22] Leicester, Leicestershire,
England
Website LMB web page (https://www2.
Education mrc-lmb.cam.ac.uk/group-lead
ers/emeritus/greg-winter/)
Winter was educated at the Royal Grammar School,
Newcastle upon Tyne.[6] He went on to study Natural Education Royal Grammar School,
Sciences at the University of Cambridge graduating Newcastle upon Tyne
from Trinity College, Cambridge in 1973. He was Alma mater Trinity College, Cambridge
awarded a PhD degree, from the MRC Laboratory of (MA, PhD)
Molecular Biology, for research on the amino acid Known for Cambridge Antibody
sequence of tryptophanyl tRNA synthetase from the Technology
bacterium Bacillus stearothermophilus in 1977[23] Domantis[4]
supervised by Brian S. Hartley.[24] Later, Winter Bicycle Therapeutics[5]
completed a term of post-doctoral fellowship at Antibody engineering
Imperial College London, and another at the Institute Awards Colworth Medal (1986)
of genetics in University of Cambridge.[25] EMBO Member (1987)[1]
Louis-Jeantet Prize for
Medicine (1989)[2]
Career and research Knight Bachelor (2004)
Royal Medal (2011)
Following his PhD, Winter completed postdoctoral Prince Mahidol Award (2016)[3]
research at the Laboratory of Molecular Biology in Nobel Prize in Chemistry
Cambridge.[26][27] He continued to specialise in (2018)
protein and nucleic acid sequencing and became a Copley Medal (2024)
Group Leader at the MRC Laboratory of Molecular Scientific career
Biology in 1981. He became interested in the idea that
Fields Biochemistry
all antibodies have the same basic structure, with only
small changes making them specific for one target. Institutions University of Cambridge
Georges J. F. Köhler and César Milstein had won the Laboratory of Molecular
1984 Nobel Prize for their work at the Laboratory of Biology
Molecular Biology, in discovering a method to isolate Imperial College London
and reproduce individual, or monoclonal, antibodies Thesis The amino acid sequence of
from among the multitude of different antibody tryptophanyl tRNA synthetase
proteins that the immune system makes to seek and from Bacillus
destroy foreign invaders attacking the body.[28] These stearothermophilus (http://etho
monoclonal antibodies had limited application in s.bl.uk/OrderDetails.do?uin=u
human medicine, because mouse monoclonal k.bl.ethos.477727) (1977)
antibodies are rapidly inactivated by the human Doctoral Brian S. Hartley
immune response, which prevents them from providing advisor
long-term benefits.

Winter pioneered a technique to "humanise" mouse monoclonal antibodies; a technique used in the
development of Campath-1H by the Laboratory of Molecular Biology and University of Cambridge
scientists.[29] This antibody now looks promising for the treatment of multiple sclerosis. Humanized
monoclonal antibodies form the majority of antibody-based drugs on the market today and include
several blockbuster antibodies, such as Keytruda.

Winter founded Cambridge Antibody Technology in 1989,[30][31] and Bicycle Therapeutics.[32][33] He

worked on the Scientific Advisory Board of Covagen,[34][35] (now part of Cilag) and is also the chairman
of the Scientific Advisory Board for Biosceptre International Limited.

In 1989, Winter was a founder of Cambridge Antibody Technology, one of the early commercial biotech
companies involved in antibody engineering. One of the most successful antibody drugs developed was
HUMIRA (adalimumab), which was discovered by Cambridge Antibody Technology as D2E7, and
developed and marketed by Abbott Laboratories. HUMIRA, an antibody to TNF alpha, was the world's
first fully human antibody,[36] which went on to become the world's top selling pharmaceutical with sales
of over $18Bn in 2017[37] Cambridge Antibody Technology was acquired by AstraZeneca in 2006 for
£702m.[38]
In 2000, Winter founded Domantis to pioneer the use of domain antibodies, which use only the active
portion of a full-sized antibody. Domantis was acquired by the pharmaceutical GlaxoSmithKline in
December 2006 for £230 million.[4][39]

Winter subsequently founded another company, Bicycle Therapeutics Limited as a start up company
which is developing very small protein mimics based on a covalently bonded hydrophobic core.[40]

Awards and honours

Winter was elected a Fellow of the Royal Society (FRS) in 1990[41] and
awarded the Royal Medal by the society in 2011 "for his pioneering work
in protein engineering and therapeutic monoclonal antibodies, and his
contributions as an inventor and entrepreneur".[42] He was given the
Scheele Award in 1994.

In 1995, Winter won several international awards including the King

Faisal International Prize for Medicine (Molecular Immunology) and in
1999, the Cancer Research Institute William B. Coley Award. Winter was
formerly the Joint Head of the Division of Protein and Nucleic acid
Chemistry-Biotechnology, and was Deputy Director,[43] at the Laboratory
of Molecular Biology, Cambridge, an institution funded by the UK
Medical Research Council. He was also Deputy Director of the MRC's Greg Winter during Nobel
press conference in
Centre for Protein Engineering until its absorption into the Laboratory of
Stockholm, December 2018
Molecular Biology. He is a member of the Advisory Council for the
Campaign for Science and Engineering.[44] Winter was appointed
Commander of the Order of the British Empire (CBE) in 1997 and Knight Bachelor in 2004. He served as
Master of Trinity College, Cambridge from 2012 to 2019.[45][46] In 2015 he received the Wilhelm Exner
Medal.[47]

Along with George Smith, Winter was awarded half of the Nobel Prize in Chemistry on 3 October 2018
for his work on phage displays for antibodies (while Frances Arnold received the other half of the prize
that same year "for the directed evolution of enzymes").[19] In 2020 he was featured on The Times'
'Science Power List'.[48][49] In 2024 he received the Copley Medal of the Royal Society.[50]

References
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(1991). "Multi-subunit proteins on the surface of filamentous phage: Methodologies for
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gene of a human influenza virus H1 subtype". Nature. 292 (5818): 72–5.
Bibcode:1981Natur.292...72W (https://ui.adsabs.harvard.edu/abs/1981Natur.292...72W).
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16. Fields, S.; Winter, G.; Brownlee, G. G. (1981). "Structure of the neuraminidase gene in
human influenza virus A/PR/8/34". Nature. 290 (5803): 213–7.
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doi:10.1038/290213a0 (https://doi.org/10.1038%2F290213a0). PMID 7010182 (https://pubm
ed.ncbi.nlm.nih.gov/7010182). S2CID 8051512 (https://api.semanticscholar.org/CorpusID:80
51512).
17. Riechmann, L.; Clark, M.; Waldmann, H.; Winter, G. (1988). "Reshaping human antibodies
for therapy" (https://doi.org/10.1038%2F332323a0). Nature. 332 (6162): 323–7.
Bibcode:1988Natur.332..323R (https://ui.adsabs.harvard.edu/abs/1988Natur.332..323R).
doi:10.1038/332323a0 (https://doi.org/10.1038%2F332323a0). PMID 3127726 (https://pubm
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18. Marks, J. D.; Hoogenboom, H. R.; Bonnert, T. P.; McCafferty, J.; Griffiths, A. D.; Winter, G.
(1991). "By-passing immunization". Journal of Molecular Biology. 222 (3): 581–97.
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This article incorporates text (https://royalsociety.org/people/gregory-winter-12548/)
available under the CC BY 4.0 license.

External links
Gregory Winter (https://www.nobelprize.org/laureate/965) on Nobelprize.org including the
Nobel Lecture on 8 December 2018 Harnessing Evolution to Make Medicines

Retrieved from "https://en.wikipedia.org/w/index.php?title=Gregory_Winter&oldid=1242756498"