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The utilisation of engineered therapeutic proteins for basic research, clinical diagnostics, and therapy continues to expand. Consequently, the efficient expression and production of these valuable biomolecules face challenges in improving their quantity and quality while minimizing time and cost. To meet these demands, an increasing variety of recombinant production platforms called cell factories are being developed. Unfortunately, there is no universal production system which can guarantee high yields, particularly as every protein itself causes its own issues in terms of expression and production. Through case studies, the Optimising Expression Platforms conference offers comparisons, evaluations, and solutions that enable protein expression researchers to efficiently express the therapeutic protein of their choice.

Sunday, 13 November

Recommended Short Courses*14:00

SC3: Use and Troubleshooting of Eukaryotic Expression Systems
*Separate registration required. See short courses page for details.

Tuesday, 15 November

Registration and Morning Coffee (Garden Room)07:30




Chairperson's Opening Remarks

Eva-Kathrin Ehmoser, PhD, Head of Institute for Synthetic Bioarchitectures, NanoBio Technologie DNBT, University of Natural Resources & Life Sciences


Cell-Free Protein Synthesis of Viral (Membrane) Proteins for Structural Studies

Anja Böckmann, PhD, Research Director, Biology & Chemistry of Proteins, MMSB CNRS, Université de Lyon

With excessive demands on sample amounts progressively decreasing, cell-free protein synthesis (CFPS) systems are gaining momentum as tools for structural biology applications to complex proteins. Out of the available CFPS systems, wheat germ cell-free protein synthesis (WG-CFPS) merges the highest yields, compatible with structural approaches, with the use of a eukaryotic ribosome. This makes it an excellent approach for the study of complex viral proteins including, for example, large protein complexes and membrane proteins. 


Enhancing the Cell-Free Expression of Native Membrane Proteins by in silico Optimization of the Coding Sequence – An Experimental Study of the Human Voltage-Dependent Anion Channel

Eva-Kathrin Ehmoser, PhD, Head of Institute for Synthetic Bioarchitectures, NanoBio Technologie DNBT, University of Natural Resources & Life Sciences

Studying biological systems represents a challenging task due to the inherent complexity of living cells and, still, the lack of quantitative and reproducible data sets. Attempts to create membrane proteins outside living cells, namely from cell lysates, have brought us to an alternative route of protein synthesis, eventually bypassing the inherent regulation processes of protein synthesis pathways occurring in living cells. Such novel combinations of cell-free protein synthesis with artificial membranes with an optimized translation initiation model are subsumed as a bottom-up synthesis of natural versus non-natural systems aiming to understand membrane proteins.


A Cost-of-Goods Modelling Analysis Comparing a Novel Cell-Free Platform to a Conventional Cell-Based Bioprocess for the Production of Highly Potent Neurotoxins

Williams Olughu, PhD, Senior Principal Scientist, Ipsen

A decisional tool was developed to evaluate a cell-free synthesis system's economic and operational performance compared to an E. coli process used to manufacture highly potent biotherapeutic proteins. The real-world simulated scenarios highlighted areas where the cell-free platform offered up to 35% savings. Ultimately, the advantage of identifying when the cell-free platform outperforms was equivalent to reducing process development times by up to 18 person-months—potentially accelerating life-saving medicines to patients. 

10:00 Human IgG Fc Production through Methanol-Free Pichia pastoris Fermentation

Ying Yang, PhD, Eppendorf, Inc.

Therapeutic mAbs are predominantly produced with mammalian cell culture systems such as those using Chinese hamster ovary (CHO) cells. The yeast P. pastoris has become a substantial workhorse for recombinant protein production. However, the N-linked glycosylation in P. pastoris, namely high mannose glycosylation, is significantly different from that in CHO or other mammalian cells. This presentation showcases the potential of P. pastoris as a next-generation mAb production platform.

10:15 Rebuilding the Cell-Free System and the Applications for R&D of Biologics

Takashi Ebihara, PhD, COO, GeneFrontier Corporation

Our unique platform technology, PUREfrex, is a fully reconstituted (or rebuilt) cell-free protein expression system. It's easy to customize the system for various applications, and useful for high throughput screening of various kinds of biologics as well. Plus, we established robust ribosome display with customized PUREfrex and named PUREfrexRD, which has great advantage in screening of highly diversified library to generate new biologics such as antibodies or cyclic peptides.

Session Break and Transition into Plenary Keynote10:30




Plenary Keynote Introduction

Ahuva Nissim, PhD, Professor, Antibody and Therapeutic Engineering, William Harvey Research Institute, Queen Mary University of London

E. Sally Ward, PhD, Director, Translational Immunology; Professor, Molecular Immunology, Centre for Cancer Immunology, University of Southampton


Evolution of Antibody Technologies

Jane K. Osbourn, PhD, CSO, Alchemab Therapeutics Ltd.

It is nearly fifty years since the discovery of monoclonal antibodies, the first drug approval coming soon after in 1986. From this early success, approval rates took time to ramp up and significant efforts were focused on building a range of technologies to deal with the technical challenges of antibody-drug discovery. This talk will discuss how antibody technologies have evolved and consider where future innovation may lie.

Coffee Break in the Exhibit Hall with Poster Viewing (Verdi and Vivaldi 1&2)11:30


Cell-Free Synthesized G-Protein Coupled Receptors for Structural Evaluation by Cryo-Electron Microscopy and Combined in vitro/in vivo Studies

Frank Bernhard, PhD, Lab Leader, Institute of Biophysical Chemistry, Goethe University

The cotranslational insertion of nascent GPCRs and other membrane proteins into MSP or SapA-based nanoparticles by cell-free protein synthesis generates high-quality samples for functional and structural studies. We demonstrate strategies for cell-free GPCR/nanoparticle formation, their lipid-dependent functional analysis, and the cryo-electron microscopy characterization of GPCR/G-protein complexes. GPCRs were further transferred from nanoparticles into membranes of living cells to study their activity and interactions with endogenous proteins.

12:45 How to Reach Biopharma Quality and Productivity Goals? Having a Versatile Platform in Place

Lars Stöckl, Managing Director, FyoniBio GmbH

  • Versatile expression platform for different quality needs of biopharmaceutical: CHOnamite vs GEX
  • Special emphasis on glycosylation from different host cell systems of crucial importance for biosimilar development
  • Increase of quality (e.g., glycosylation) and productivity by process optimization

Session Break13:15

13:20 Selexis DNA-FISH/Karyotyping Platform: An Industrial Platform For High-Throughput Data Analysis

Ghislaine Arib, PhD, Genomics Director, Cell Line Development R&D, Selexis

Speed and cost-effectiveness are the main features of Selexis’ cytogenetics industrial platform for high throughput karyotype data analysis. It enables routine investigation of clonality assessment by overcoming the key limitations of the FISH (fluorescence in situ hybridization) and karyotyping assay.

FISH karyotyping can detect transgene integration sites and chromosomes rearrangements without performing a subcloning step, thus making it a suitable method for clonality assessment of randomly generated recombinant cell lines.

Luncheon Presentation (Sponsorship Opportunity Available) or Enjoy Lunch on Your Own13:50

Session Break14:20



Chairperson's Remarks

Richard Altman, MS, Field Application Scientist, Life Science Solutions, Thermo Fisher Scientific


Suitability of Transiently Expressed Antibodies for Clinical Studies

Sara Rodriguez Conde, PhD, Associate Director, Cell Culture & Fermentation Sciences, BioPharmaceuticals Development, R&D, AstraZeneca

Traditionally, transient gene expression (TGE) has been the technology used for production of therapeutic proteins at early drug development stages as it allows for rapid production of high-quality material. In this study, two anti-viral mAbs were produced using AstraZeneca’s proprietary CHO-based transient expression system. To assess the suitability of transiently-generated material for clinical studies, batch-to-batch product quality consistency as well as process scalability were investigated.


Producing Challenging Protein Targets for Drug Discovery

Bryony Ackroyd, PhD, Senior Protein Scientist, Discovery Biology & Discovery Sciences R&D, AstraZeneca

Targets for drug discovery projects are becoming more diverse and challenging. They are chosen based on evidence linking them to human disease and not on the challenges, which need to be overcome to express these proteins in suitable quantity and quality to support drug discovery projects. A number of examples of recent AstraZeneca projects will be presented, in which difficult expression/purification challenges have been overcome.

15:35 Warp Speed: Scalable, 4-8 g/L CHO Production Processes in 8 Weeks

Joeri Kint, PhD, Head of Business Development, Marketing and Sales, ExcellGene

The development of cell lines and production processes for biologics has always been a painstakingly slow process. When the COVID-19 pandemic hit, companies and governments underwent pressure to adapt, and procedures that were seemingly cast in stone changed. Fortunately, we were at the front line during this paradigm-changing event. Here, we present our journey on how we reduced our timelines for our cell line and process development without compromising quality and yield.

Refreshment Break in the Hall with Poster Viewing (Verdi and Vivaldi 1&2)16:05


Compartmentalisation of Transcription and Translation in Cell-Free Protein Synthesis Using a Membrane Reactor Design

Beatrice Melinek, PhD, Bioprocess Engineer, University College London

Advances in cell-free protein synthesis (CFPS) offer the prospect of industrially-relevant production processes for stratified and personalised protein therapeutics, with the potential for greater development and production speed, control over process environment, and improved consistency. We present studies of how a membrane reactor can be used to improve the economics, titre, and product quality, by recreating the localised enzyme concentrations seen in the cellular environment.


Cell-Free Expression of the Outer Membrane Protein OprF of Pseudomonas aeruginosa for Vaccine Purposes

JeanLuc Lenormand, PhD, Professor, Team Leader, University of Grenoble Alpes

Pseudomonas aeruginosa is the second leading cause of nosocomial infections and pneumonia in hospitals. The outer membrane protein OprF is a well conserved and immunogenic porin playing an important role in quorum sensing and in biofilm formation. We used a bacterial cell-free expression system to reconstitute OprF under its native forms and in active open oligomerized state in liposomes and we demonstrated that the resulting OprF proteoliposomes can be used as a fully functional recombinant vaccine against P. aeruginosa. Our approach thus represents an easy and efficient way for producing bacterial membrane antigens exposing native epitopes for vaccine purposes.


POSTER HIGHLIGHT: A Unique Screening System to Develop E. coli Mutants for the Efficient Production of Difficult to Express Therapeutic Proteins

Michael Deghelt, PhD, de Duve Institute, University of Louvain


POSTER HIGHLIGHT: Chemical Filtering: A Post-Transfection Directed Evolution Strategy to Improve Productivity of Difficult-to-Express Antibodies in CHO Cell Lines

Chillel Jawara, Graduate Student, Chemical & Biological Engineering, University of Sheffield


Protein Production Lab Challenges: Methodologies, Strategies, and the Art of Managing Multiple Projects


Richard Altman, MS, Field Application Scientist, Life Science Solutions, Thermo Fisher Scientific

There are many challenges and rewards in operating a protein production lab. This panel will focus on the following topics: ​

  • Lessons learned from managing a protein production workflow during a pandemic.
  • Strategies on how to manage multiple “top priority” projects.
  • Strategies for supporting the professional growth and career development of direct reports.
  • How do we make time for technical development and process optimization?
  • Troubleshooting strategies or how much time should be spent before moving to the next option?

Nicola Burgess-Brown, PhD, Director of Enzymology and Protein Engineering, Exact Sciences Innovation

Peter Schmidt, PhD, Director, Recombinant Technologies, R&D, CSL Behring GmbH

Bjørn Voldborg, MSc, Head, National Biologics Facility, DTU Bioengineering, Technical University of Denmark

Close of Optimising Expression Platforms Conference19:00