Jane Osbourn

Last updated

Jane Osbourn

OBE
Born
Jane Katharine Osbourn

CitizenshipUnited Kingdom
Education Bingley Grammar School
Queens' College, Cambridge (BSc)
John Innes Centre, Norwich (PhD)
Known for Antibody engineering
Cambridge Antibody Technology
MedImmune
AstraZeneca
STEM
Scientific career
Fields Biotechnology
Thesis Evidence that nucleocapsid disassembly and a later step in virus replication are inhibited in transgenic tobacco protoplasts expressing TMV coat protein  (1991)
Doctoral advisor T. Michael A. Wilson

Jane Osbourn, OBE, is a scientist and former chair of the UK BioIndustry Association. [1]

Contents

A Natural Sciences graduate of Queens' College, Cambridge, Osbourn completed several post-graduate qualifications before moving into industry at Cambridge Antibody Technology, that became MedImmune and AstraZeneca.

In the Queen's Birthday Honours list of 2019, Osbourn was awarded the Order of the British Empire medal for services to "Human Monoclonal Antibody Drug Research and Development and Biotechnology". [2]

Early life

Osbourn was born in Bingley, West Yorkshire, and attended Bingley Grammar School. She is married to John Richer, Professor of Physics at the Cavendish Laboratory, Cambridge. [3]

She is the sister of Professor Anne Osbourn FRS [4] who investigates plant natural product biosynthesis.

Academic career

Osbourn went on to study at the Queens' College, Cambridge, where she obtained a 1st class degree in Natural Sciences (Biochemistry). She was recognised in 1986 for playing netball at Queens, [5] and was awarded both a third year Foundation Scholarship and The Henry Mosseri prize. [6]

She went on to complete a PhD degree at the John Innes Centre for Plant Science Research in Norwich, which resulted in the publication of Evidence that nucleocapsid disassembly and a later step in virus replication are inhibited in transgenic tobacco protoplasts expressing TMV coat protein. [7] Following this, she completed a post-doctoral position at Rutgers University, New Jersey, United States, undertaking research directed towards clarification of the sequence elements responsible for the translational enhancement effect conferred by the 5' untranslated region of Tobacco Mosaic Virus known as omega. [8]

Osbourn then moved into medical research through a British Heart Foundation Post-Doctoral Fellowship at the Department of Medicine at Addenbrooke's Hospital in Cambridge. [9]

Career in industry

In 1993 she moved to a small, Cambridge-based, start-up biotechnology company called Cambridge Antibody Technology [10] . CAT, as it was called, would pioneer the use of Phage Display technology that ultimately discovered important drugs such as Humira. [11]

She was the key author of several scientific papers, including Human Antibodies with Sub-nanomolar Affinities Isolated from a Large Non-immunized Phage Display Library, Nature Biotechnology, 1996 [12] and Human Antibodies by Design, Nature Biotechnology, 1998. [13] She is co-author of several others pertaining to antibody discovery and development:

Osbourn is listed as an inventor on several patents, which are (in chronological order):

Osbourn also created a technique to assist with the discovery of proximity-guided selection of antibodies, so called Proximol. [30]

CAT was acquired by AstraZeneca in 2006 [31] and in the following year was merged with a US-based company called MedImmune [32] to form AstraZeneca’s global biologics R&D arm. During this time Osbourn began to speak about opportunities for diversity in science. [33]

In 2013, AstraZeneca announced its decision to relocate its headquarters to Cambridge, UK. [34] Jonathan Burroughs, of Creative Places, wrote in 2015 that Osbourn had an influence over this decision. [35]

In February 2019, it was announced that Osbourn would be leaving AstraZeneca. [36] Since November 2019, Osbourn has been Chief Scientific Office of antibody therapeutics discovery company Alchemab Therapeutics.

Recognition

Her early interest in science has grown into a passion for science education, supporting and championing life science education programmes and she is established as an advisor and mentor to many young researchers in the life science sector. She has been acknowledged by a number of different pharmaceutical media groups for these qualities.[ citation needed ]

In 2014 Osbourn was elected to join the board of the BioIndustry Association, becoming Chair in 2016; [1] and in this role she has been working to support the development of the biotechnology sector in the UK. She also does this through her roles as a Director of Babraham Bioscience Technologies [44] and as a Director of Cambridge Enterprise, the technology transfer organisation for University of Cambridge. [45]

Osbourn has presented at a number of parliamentary Select Committees. At the Business, Innovation and Skills Committee, on Tuesday 13 May 2014, she gave evidence on behalf of AstraZeneca as it faced a potential takeover from Pfizer. [46] [47]

On 1 July that year, Osbourn gave evidence to the Science and Technology Select Committee: Priorities for Scientific Research. [48]

Osbourn has also has previously served as a Member of the UK Medical Research Council Industry Grant Award Assessment Panel. [49]

In 2018 the Nobel Prize for Chemistry was awarded jointly to Sir Greg Winter, George Smith and Frances Arnold. Winter received his award for the phage display of peptides and antibodies. [50] Sir Greg and David Chiswell had founded Cambridge Antibody Technology to exploit this science. Osbourn says of this time, "There was a cohort of really able intellect in Cambridge – in CAT and other companies, in the MRC LMB and in the University – and what happened was a condensation of that focus… Once we decided to make phage display work, we set some really tough goals and then just got on with it." [51] To recognise Jane’s contribution to the prize, she, along with David Chiswell and John McCafferty, accompanied Sir Greg to the Nobel ceremony. [51]

On 7 June 2019 she was awarded an OBE for services to Human Monoclonal Antibody Drug Research and Development and Biotechnology. [2] CEO of AstraZeneca, Pascal Soriot, said of the award "On behalf of AstraZeneca, I am delighted to congratulate Dr Jane Osbourn for her award of an OBE in recognition of her services to human monoclonal antibody drug research and development and biotechnology. This well-deserved honour reflects her contribution to biopharmaceutical science over more than 25 years, from Cambridge Antibody Technology to AstraZeneca and MedImmune. Jane’s leadership in UK life sciences includes championing the biotech sector through her position as chair of the BIA and contributing to the growth of the UK’s scientific ecosystem. I would also like to recognise her authentic commitment to building skills through STEM and education outreach, in particular for women in science". [52] [53]

Related Research Articles

<span class="mw-page-title-main">Monoclonal antibody</span> Antibodies from clones of the same blood cell

A monoclonal antibody is an antibody produced from a cell lineage made by cloning a unique white blood cell. All subsequent antibodies derived this way trace back to a unique parent cell.

<span class="mw-page-title-main">AstraZeneca</span> British pharmaceutical company

AstraZeneca plc is a British-Swedish multinational pharmaceutical and biotechnology company with its headquarters at the Cambridge Biomedical Campus in Cambridge, England. It has a portfolio of products for major diseases in areas including oncology, cardiovascular, gastrointestinal, infection, neuroscience, respiratory, and inflammation. It has been involved in developing the Oxford–AstraZeneca COVID-19 vaccine.

<span class="mw-page-title-main">Phage display</span> Biological technique to evolve proteins using bacteriophages

Phage display is a laboratory technique for the study of protein–protein, protein–peptide, and protein–DNA interactions that uses bacteriophages to connect proteins with the genetic information that encodes them. In this technique, a gene encoding a protein of interest is inserted into a phage coat protein gene, causing the phage to "display" the protein on its outside while containing the gene for the protein on its inside, resulting in a connection between genotype and phenotype. These displaying phages can then be screened against other proteins, peptides or DNA sequences, in order to detect interaction between the displayed protein and those other molecules. In this way, large libraries of proteins can be screened and amplified in a process called in vitro selection, which is analogous to natural selection.

Adalimumab, sold under the brand name Humira, among others, is a monoclonal antibody used to treat rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, ulcerative colitis, plaque psoriasis, hidradenitis suppurativa, uveitis, and juvenile idiopathic arthritis. It is administered by injection under the skin.

<span class="mw-page-title-main">Gregory Winter</span> English biochemist (born 1951)

Sir Gregory Paul Winter is a Nobel Prize-winning English molecular biologist best known for his work on the 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.

mRNA display

mRNA display is a display technique used for in vitro protein, and/or peptide evolution to create molecules that can bind to a desired target. The process results in translated peptides or proteins that are associated with their mRNA progenitor via a puromycin linkage. The complex then binds to an immobilized target in a selection step. The mRNA-protein fusions that bind well are then reverse transcribed to cDNA and their sequence amplified via a polymerase chain reaction. The result is a nucleotide sequence that encodes a peptide with high affinity for the molecule of interest.

Bertilimumab is a human monoclonal antibody that binds to eotaxin-1, an important regulator of overall eosinophil function.

Mapatumumab (HGS-ETR1) is an experimental human monoclonal antibody undergoing clinical trials for the treatment of cancer. It targets TRAIL-R1, also known as DR4, which is expressed on the surface of many tumor cell types.

An anti-CD22 immunotoxin is a monoclonal antibody linked to a cytotoxic agent. They are being studied in the treatment of some types of B-cell cancer.

<span class="mw-page-title-main">Cambridge Antibody Technology</span> Defunct British biotechnology company

Cambridge Antibody Technology was a biotechnology company headquartered in Cambridge, England, United Kingdom. Its core focus was on antibody therapeutics, primarily using Phage Display and Ribosome Display technology.

John McCafferty is a British scientist, one of the founders of Cambridge Antibody Technology alongside Sir Gregory Winter and David Chiswell. He is well known as one of the inventors of scFv antibody fragment phage display, a technology that revolutionised the monoclonal antibody drug discovery. McCafferty and his team developed this process following failures previously generating antibodies by immunizing mice. Later improvements of antibody phage display technology enables the display of millions of different antibody fragments on the surface of filamentous phage and subsequent selection of highly specific recombinant antibodies to any given target. This technology is widely exploited in pharmaceutical industry for the discovery and development of therapeutic monoclonal antibodies to treat mainly cancer, inflammatory and infectious diseases. One of the most successful was HUMIRA (adalimumab), 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 phage display derived fully human antibody, which achieved annual sales exceeding $1bn therefore achieving blockbuster status. Humira went on to dominate the best-selling drugs lists - in 2016: The best selling drugs list researched by Genetic Engineering & Biotechnology News, published in March 2017, details that Humira occupied the number 1 position for 2015 and 2016. Whilst for 2017, Abbvie reports that Humira achieved $18.427billion of sales in 2017

The pharmaceutical industry in the United Kingdom directly employs around 73,000 people and in 2007 contributed £8.4 billion to the UK's GDP and invested a total of £3.9 billion in research and development. In 2007 exports of pharmaceutical products from the UK totalled £14.6 billion, creating a trade surplus in pharmaceutical products of £4.3 billion.

Moxetumomab pasudotox, sold under the brand name Lumoxiti, is an anti-CD22 immunotoxin medication for the treatment of adults with relapsed or refractory hairy cell leukemia (HCL) who have received at least two prior systemic therapies, including treatment with a purine nucleoside analog. Moxetumomab pasudotox is a CD22-directed cytotoxin and is the first of this type of treatment for adults with HCL. The drug consists of the binding fragment (Fv) of an anti-CD22 antibody fused to a toxin called PE38. This toxin is a 38 kDa fragment of Pseudomonas exotoxin A.

<span class="mw-page-title-main">Tralokinumab</span>

Tralokinumab sold under the brand names Adtralza (EU/UK) and Adbry (US) among others, is a human monoclonal antibody used for the treatment of atopic dermatitis. Tralokinumab targets the cytokine interleukin 13.

<span class="mw-page-title-main">LifeArc</span>

LifeArc is a British life science medical research charity. It was established in 2000 as MRC Technology to translate the work of UK Medical Research Council (MRC) research scientists.

Creative Biolabs, Inc. is a life-science company which produces and supplies biotech products and services for early drug discovery and development, including various phage display libraries such as pre-made libraries, phage display services, antibody sequencing, and antibody humanization. Customers include pharmaceutical companies, academic institutions, government agencies, clinical research organizations and biotechnology companies.

Recombinant antibodies are antibody fragments produced by using recombinant antibody coding genes. They mostly consist of a heavy and light chain of the variable region of immunoglobulin. Recombinant antibodies have many advantages in both medical and research applications, which make them a popular subject of exploration and new production against specific targets. The most commonly used form is the single chain variable fragment (scFv), which has shown the most promising traits exploitable in human medicine and research. In contrast to monoclonal antibodies produced by hybridoma technology, which may lose the capacity to produce the desired antibody over time or the antibody may undergo unwanted changes, which affect its functionality, recombinant antibodies produced in phage display maintain high standard of specificity and low immunogenicity.

Stefan Dübel is a German biologist. Since October 2002, he has been a full professor at the University of Braunschweig and head of the Biotechnology Department of the Institute of Biochemistry, Biotechnology and Bioinformatics. His work is centred around protein engineering, phage display and recombinant antibodies.

<span class="mw-page-title-main">Ruth March</span> British genomic scientist

Ruth Eleanor March is a British genomic scientist who is Senior Vice President of Precision Medicine at AstraZeneca. She specialises in precision medicine and oncology. During the COVID-19 pandemic, March developed a diagnostic test for COVID-19.

James Allen Wells is a Professor of Pharmaceutical Chemistry and Cellular & Molecular Pharmacology at the University of California, San Francisco (UCSF) and a member of the National Academy of Sciences. He received his B.A. degrees in biochemistry and psychology from University of California, Berkeley in 1973 and a PhD in biochemistry from Washington State University with Ralph Yount, PhD in 1979. He completed his postdoctoral studies at Stanford University School of Medicine with George Stark in 1982. He is a pioneer in protein engineering, phage display, fragment-based lead discovery, cellular apoptosis, and the cell surface proteome.

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