Commercialisation of a platform technology for production of diagnostic and theraputic reagents
Submitting InstitutionQueen's University Belfast
Unit of AssessmentAllied Health Professions, Dentistry, Nursing and Pharmacy
Summary Impact TypeTechnological
Research Subject Area(s)
Biological Sciences: Biochemistry and Cell Biology
Summary of the impact
Protein reagent production techniques developed at QUB, were transferred
to UK-based biotechnology company, Fusion Antibodies Ltd, to increase
their competitiveness in the production of diagnostic and therapeutic
reagents. These techniques were commercialised by the company as the
Fusion Expression TechnologyTM (FET) platform technology, to
deliver contract research orders. The transfer of this technology allowed
Fusion to accelerate its completion of orders and secure higher value
projects. This increased competitiveness led to the tripling its technical
workforce (at graduate and doctoral levels), securing new orders from over
15 countries and producing on average £300K per annum (from 2008 onwards)
Dr Chris Scott (postdoctoral researcher in the School of Pharmacy from
Sept 1999-July 2001 and subsequently lecturer from 2003 onwards, and now
Chair in Biomolecular Science) was approached by Fusion Antibodies Ltd.,
to examine issues that they were having in the rapid production of
recombinant proteins as part of their contract research business.
Specifically, these problems included the ability to produce the protein
solubly at useful levels, which was limiting purification and the speed at
which projects could be completed — which routinely took 3 months.
The Scott lab had developed know-how to improve the levels and speed of
recombinant protein production using bacterial systems. This research
involved the development of new promoters, translation initiation motifs
and new fusion protein tags or partners which were fused to the target
protein and elicited their own biophysical characteristics onto the target
protein, including factors such as stability, solubility and expression
yields. Scott and his team had been examining such technologies as part of
a programme for the recombinant production of proteases — a programme that
Scott originally worked on as a post-doctoral fellow (1999-2001)1
and then took up again as a new lecturer from April 2003 onwards. This
research interest was further pursued by Scott and was the focus of a
BBSRC award to Scott and Prof Brian Walker (2004-2007).2
The Scott lab and Fusion Antibodies initiated a collaborative project,
funded through the Knowledge Transfer Partnership (KTP) scheme. This
project ran for 30 months from late 2004 to early 2007 with one KTP
associate, Dr. Hang Fai (Henry) Kwok, employed. Dr Jill Caswell was also
involved as a researcher in these technologies as an employee of Fusion
Antibodies, but enrolled on an industrial part-time PhD program in 2005
with the School of Pharmacy, under the supervision of Dr Scott and Prof
Walker. The focus of this project was to develop improvements in the
production of recombinant proteins — from gene sequence to purified
proteins, such that milligram quantities of protein could be prepared
within 4 weeks of orders placed.
The research led to skills being transferred to the company in terms of
selecting portions or domains of proteins that are more likely to be
expressed solubly and in useful quantities. In one case, this has led to
the production of a panel of bovine tuberculosis antigens that have
subsequently been licensed to Enfer Scientific, Ireland for the
development of a new mycobacterium tuberculosis (TB) diagnostic kit.3
Another example of technology adoption and transfer was the development of
a fusion protein purification and solubility tag, based on the bacterial
protease sortase which Scott and Walker had been researching. This led to
the development of a new tag (Solubility Enhancing Ubiquitious Tag, SNUT)
which was found to improve synthesis, solubility and purification of
References to the research
1. Scott C.J, McDowell A, Martin SL, Lynas JF, Vandenbroeck K,
Walker B Irreversible inhibition of the bacterial cysteine
protease-transpeptidase sortase (SrtA) by substrate-derived affinity
labels (2002). Biochem J. 366, 953-8.
2. Quinn D.J., Cunningham S, Walker B, Scott CJ.
Activity-based selection of a proteolytic species using ribosome display.
(2008). Biochem Biophys Res Commun. 370, 77-81.
3. Kwok HF, Scott CJ, Snoddy P, Buick RJ, Johnston JA, Olwill SA
Expression and purification of diagnostically sensitive mycobacterial
(Mycobacterium bovis) antigens and profiling of their humoral immune
response in a rabbit model (2010) Res Vet Sci. 89, 41-7.
4. Caswell J, Snoddy P, McMeel D, Buick RJ, Scott CJ.
Production of recombinant proteins in Escherichia coli using an N-terminal
tag derived from sortase. (2010) Protein Expr Purif. 70, 143-50.
References 3 and 4 involve work that was undertaken prior to 2008, but
only released for publication at a later date for commercial reasons
I. BBSRC. C.J. Scott, B. Walker. High Throughput methodologies for
the identification and characterisation of protease species 2004-2007.
II. Knowledge Transfer Partnership C.J. Scott. Recombinant Protein
Production Methodologies 2004 - 2007. £140,000.
Details of the impact
Fusion Antibodies is a UK-based biotechnology company that offers
contract research offerings to third parties to produce custom proteins
and antibodies. The impact of the research undertaken by the Scott lab was
to improve the company's ability to rapidly produce high-quality purified
proteins, thus improving the speed and cost effectiveness of their service1.
On average, the company were able to speed turnaround of protein orders
from 3 months to around 1 month. Furthermore, the innovations led to the
successful production of reagents that previously had not been
successfully produced, thereby increasing the reputation and
competitiveness of the company. This research was carried out from
2004-2007 as part of a Knowledge Transfer Partnership (KTP) scheme2,
and then subsequently commercialised under Fusion Expression TechnologyTM
(FETTM)3. The KTP associate employed under
the project, Dr Henry Kwok, won the best regional KTP scheme award4,5
in 2008 and was shortlisted for the UK award5. Dr Jill
Caswell was awarded her PhD from the School of Pharmacy in 2012.
The FETTM platform has been marketed internationally by Fusion
Antibodies since 2008 and is the underpinning technology platform for the
contract research service that they provide1, 3. This
service supports the employment of 12 people (from 4 original members of
staff) and has generated, on average, £300,000 income per annum. The
application of the FETTM platform is marketed worldwide and to
date international orders from biotechnology and pharmaceutical companies
have been secured from Austria, USA, Canada, Croatia, France, Germany,
Denmark, Italy, Israel, Switzerland, Norway, Finland, Sweden, Ireland,
Spain and Portugal1.
A particular example of the impact has been the development of a range of
mycobacterium tuberculosis protein antigens by Fusion Antibodies. These
antigens have now been licensed to Enfer Scientific Ireland, who have
developed them into the EnferplexTM TB assay6,
which is currently undergoing clinical trials in Ireland, UK and USA.
Sources to corroborate the impact
1. Fusion Antibodies CEO, www.fusionantibodies.com
2. Knowledge Transfer Partnership (KTP) Head, KTP & Business
3. FETTM Technology http://fusionantibodies.com/services/recombinant-proteins/
4. KTP awards
5. KTP final report available upon request from KTP
6. EnferplexTM TB assay
(websites accessed 23rd September 2013)