- 表现优化 -
The pursuit for biotherapeutic proteins in basic research, clinical diagnostics and therapy continues at an exponential pace. Consequently, the demands for efficient expression and production of these valuable biomolecules face challenges to improve quantity and quality while minimising time and cost. Thus, 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, since each protein can vary in terms of expression and production.

Final Agenda


07:45 Registration and Morning Coffee


08:30 Chairperson’s Opening Remarks

Peter Schmidt, PhD, Director, Recombinant Technologies, CSL Behring

08:35 KEYNOTE PRESENTATION: Tag-on-Demand: Exploiting Amber Codon Suppression Technology for the Enrichment of High-Expressing Membrane Protein Cell Lines

Trevor Wilkinson, PhD, Associate Director, Antibody Discovery & Protein Engineering, AstraZeneca Biopharmaceuticals UnitTrevor Wilkinson, PhD, Associate Director, Antibody Discovery & Protein Engineering, AstraZeneca Biopharmaceuticals Unit






09:05 Technologies for High-Level (Membrane) Protein Production in Mammalian Cells

Jonathan Elegheert, PhD, Team Leader, Interdisciplinary Institute for NeuroScience (IINS), CNRS, University of Bordeaux

Structural, biochemical, and biophysical studies of soluble and membrane proteins typically require their production in milligram quantities. Difficult-to-produce eukaryotic proteins are generally best expressed from close-to-native mammalian cell types. I will compare different approaches for the production of soluble and membrane proteins from mammalian cells and discuss their strengths and weaknesses in function of the protein target and application, as well as their practical implementation.

09:35 High-Yield Production of “Difficult-to-Express” Proteins in an Improved Cell-Free System

Takanori Kigawa, DSci, Team Leader, Center for Biosystems Dynamics Research, RIKEN

We have developed a new method of E. coli cell extract-based cell-free protein synthesis optimal at lower temperatures (20-25 ºC) achieving high-yield production comparable to the conventional method (30-37 ºC). This method is suitable for expressing proteins that tend to aggregate and/or be insoluble at optimal temperatures for the conventional method (30-37 ºC). Therefore, our new method is particularly useful for expressing “difficult-to-express” proteins.

Berkeley Lights

10:05 Presentation to be Announced

10:35 Coffee Break in the Exhibit Hall with Poster Viewing

11:15 Production of Hard-to-Produce Proteins Using Genome Engineered CHO Cells

Bjørn Voldborg, MSc, Director, CHO Cell Line Development, The Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark

Using our in-house developed high throughput CHO cell line engineering platform, we have engineered the glycosylation machinery to make a panel of CHO cell lines for the expression of recombinant proteins with tailored N-glycans. Using these cells, we have produced a therapeutic protein that until now has only been available from natural human sources. The produced protein resembles the human derived proteins with respect to N-glycan profile and activity.

11:45 The IC-Tagging Platform and Its Use for the Expression of Difficult Proteins

Jose M. Martinez-Costas, PhD, Profezsor Titular, Centro Singular de Investigación en Química Biolóxica e Materiais Moleculares (CIQUS); Departamento de Bioquímica e Bioloxía Molecular, Universidade de Santiago de Compostela

We have developed a platform that programs cells to construct nano/microspheres that integrate any protein of interest and that are easily purified. Between the multiple applications of this technology, we have recently shown its potential in the expression of difficult/toxic proteins by expressing, between others, the highly demanded diabetogenic auto-antigen protein IGRP opening the possibility of further studies on type 1 diabetes.

12:15 HEK293 Cell Lines Allow Rescue of Proteins that are Difficult to Produce in CHO – Learning Lessons from Endogenous Secretory Pathway Expression

Magdalena Malm, PhD, MSc, Researcher & Lab Manager, Wallenberg Center for Protein Research, KTH Royal Institute of Technology

Evaluation of the recombinant expression of 24 secreted human difficult-to-express proteins showed generally improved expression in HEK293 compared to CHO cells. Transcriptomic analysis was used to identify key differences between the secretory pathways of the two cell lines and to study genes differentially activated upon transgene expression. The findings suggest lessons to be learnt from each cell line based on endogenous secretory pathway gene expression.

12:45  Sponsored Presentation (Opportunity Available)

13:15 Luncheon Presentation I to be Announced

13:45 Luncheon Presentation II to be Announced


14:15 Session Break


14:30 Chairperson’s Remarks

Richard Altman, MS, Staff Scientist, Life Science Solutions, Thermo Fisher Scientific

14:35 The Use of Design of Experiments in Recombinant Protein Production: Concepts and Case Studies

Barry Ryan, BSc (Hons), PGDip, MSc, MA, PhD, Lecturer, Food Science and Environmental Health, College of Health and Science, Technological University Dublin

Many factors, both intrinsic and extrinsic, can influence recombinant protein yield; however, identifying the most important factors, individually or synergistically, for optimum yield can be time consuming and expensive. Statistical models, such as Design of Experiments (DoE), can be used as efficient approaches to recombinant protein production optimisation. Fundamental concepts of DoE, with supporting case studies, will underpin an overview of the potential of this method for enhanced recombinant protein production.

15:05 Tuning Recombinant Protein Expression to Match Secretion Capacity

Neil Dixon, PhD, Research Group Leader, Manchester Institute of Biotechnology, University of Manchester

Translocation of recombinant protein across cellular membranes can greatly facilitate the isolation of high quality and highly pure product. However, translocation processes are a major cellular bottleneck that are prone to capacity overload. Here we will report upon recent advances to avoid this capacity overload. Specifically, how we can employ fine-tuning of gene expression to match the secYEG-dependent secretion capacity in E. coli for the production of antibody fragments.

15:35 Refreshment Break in the Exhibit Hall with Poster Viewing

16:15 A Recovery Toolbox: Molecular Approaches to Enhance Protein Folding and Soluble Yield from Bacterial Expression Systems

Christopher H. Gray, PhD, Team Leader (Structural Biology), Drug Discovery Program, CRUK Beatson Institute

Optimising protein folding during expression improves the quantity and quality of product. We have developed innovations that manipulate the dynamics of protein translation and folding to enhance bacterial expression systems. Manipulation of synonymous codon usage and the use of novel “auto-cleaving” solubilizing tags markedly improve the success of Escherichia coli expression systems. Examples presented will demonstrate how yield, utility, and activity of products is improved by these approaches.

16:45 Improved Production of Recombinant Proteins from Insect Cells through Promoter, Virus, and Strain Enhancements

Dominic Esposito, PhD, Director, Protein Expression Laboratory, Frederick National Laboratory for Cancer Research

Baculovirus-based insect cell expression platforms are often successfully used for production of pharmaceutically relevant proteins. However, the insect cell system remains suboptimal in terms of technology development related to controlling the level of protein production, stability of baculoviruses for large-scale production, and modification of host insect cell lines for improved performance. We have begun to address some of these deficiencies and demonstrate the use of these improved systems for production of clinically relevant drug targets.

17:15 Choosing Right between Transient and Stable Protein Expression Systems While Supporting Fast-Paced Biologics Discovery

Kinjal Mehta, PhD, Principal Scientist, Protein Sciences, Jounce Therapeutics

17:45 Networking Reception in the Exhibit Hall with Poster Viewing

18:45 Problem-Solving Breakout Discussions*

19:45 End of Day


08:00 Registration and Morning Coffee


08:30 Chairperson’s Remarks

Renate Kunert, PhD, Professor, Department of Biotechnology, University of Natural Resources and Life Sciences (BOKU)

08:35 Developing a Fit-For-Multi-Purpose Rapid Material Supply Process

Claire Pearce, PhD, Senior Research Scientist, CHO Expression Team Leader, Biopharmaceutical Development, Kymab Ltd.

Pre-clinical material supply demands microgram amounts of several hundred potential lead molecules through to gram amounts of the top 2-5 lead candidates. This presentation will detail progress on the development of an in-house rapid material supply platform to meet these needs.

09:05 Humanization and Simultaneous Optimisation of Monoclonal and Bispecific Antibody

Christine X. Koo, PhD, Senior Scientist 1, Lead Optimisation, Chugai Pharmabody Research

Antibody humanization is an essential technology for reducing the potential risk of immunogenicity. For developing an antibody molecule as a pharmaceutical, simultaneous optimisation of critical antibody properties with humanization help to shorten the period necessary to identify a qualified clinical candidate. In addition, a system for purification of non-standard format antibodies such as bispecifics by using protein L chromatography is used to avoid over-engineering of antibody amino acid sequences.

09:35 Rapid Selection of CHO Clones Secreting Chimeric Antibody-Antigen Fusion Constructs Based on 2A-Peptide Cleavage and GFP

Bert Devriendt, PhD, Postdoctoral Scientist, Department of Virology, Parasitology, Immunology, Physiology, Ghent University

To enable large-scale recombinant antibody production, a high producer cell line is essential. Selecting such a cell line is however time consuming and labor intensive. By combining the design of a tri-cistronic vector expressing GFP and both antibody chains, separated by a GT2A sequence, with single cell sorting and automated image analysis, a CHO cell line was rapidly selected producing high amounts of recombinant antibodies, which showed minimal degradation.

10:05 Scaling Up and Scaling Out: Pushing the Boundaries of Transient Protein Production

Ian Wilkinson, CSO, Absolute Antibody Ltd.

Whilst transient yields have improved drastically in the last decade, scalable systems are time-consuming and costly to implement. Absolute Antibody has developed systems which scale up and scale out protein expression and purification, enabling the rapid and cost-effective production of milligram-to-gram quantities of large panels of proteins.

10:20 High Density (HD) Expression Platform: The One-Stop-Solution for Recombinant Antibody Production

Bowu Luan, PhD, Product Manager, GenScript USA, Inc.

GenScript has developed a novel reagent “Cocktail” compatible with HD expression system, which improves antibody yield by increasing cell viability and facilitating protein folding. This HD system works well with all species and low expressers, readily to scale down and up. Automatic workflow from transfection to purification ensures the quality.

10:35 Coffee Break in the Exhibit Hall with Poster Viewing

11:15 Influence of Somatic Mutations on mAb Expression and Thermal Stability Properties

Renate Kunert, PhD, Professor, Department of Biotechnology, University of Natural Resources and Life Sciences (BOKU)

The production potential of monoclonal antibody (mAb) expressing cell lines depends on the intrinsic antibody structure and its interaction with cellular compartments especially the folding and secretion machinery. To get a better understanding of such relations we expressed different mAbs under isogenic conditions in recombinant CHO cells and studied cellular biology and physicochemical properties of mAbs.

11:45 High Throughput Antibody Production and Purification: Day to Day Challenges and How to Overcome Them

Peter Schmidt, PhD, Director, Recombinant Technologies, CSL Behring

Monoclonal antibodies are the fastest growing segment in the drug market. The development of mAbs requires purification of large numbers of variants with sufficient yield. However, established high-throughput purification strategies have been limited by the binding capacity of established affinity matrices. The presentation will address some of the known and less known issues and suggest ways to overcome them.

Polyplus-Transfection 12:15 Luncheon Presentation I to be Announced


Glycotope 12:45 Luncheon Presentation II to be Announced


13:15 Dessert Break in the Exhibit Hall with Poster Viewing

14:00 End of Optimising Expression Platforms

17:00 Dinner Short Course Registration*

17:3020:30 Dinner Short Courses

* 活动内容有可能不事先告知作更动及调整。

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