Preliminary Agenda 

When expressing protein, there are a variety of expression systems to choose from. CHO is seen as the ‘king’ in the industry, but does it meet all needs of rapid production and budget constraints? This meeting will explore Optimizing Protein Expression through understanding and enhancing expression systems, and will especially focus on CHO cells and other mammalian systems, E.coli and yeasts. Other host systems, such as baculovirus and algae, will be touched on as well. Along with case studies, the meeting will feature experts who reveal the underlying mechanisms and insights into the varying systems in order to enhance protein expression. Comparing and contrasting systems will also be featured to provide greater understanding of how these systems function within the context of the results achieved.

Day 1 | Day 2 | Download Brochure | Register 

Recommended Pre-Conference Short Course* 

SC12: Production Challenges for Complex Biologics: ADCs, Bispecifics and Fusion Proteins  

*Separate registration required.


7:00 am Registration and Morning Coffee


Optimizing Processes for Greater Productivity & CHO Expression 

8:00 Chairperson’s Remarks

Case StudyChristopher W. Kemp, Ph.D., President, Kempbio, Inc.


Innovations in Protein Expression Technologies to Deliver New Biotherapeutics

Pranhitha Reddy, Ph.D., Director, BioProcess & Analytical Sciences, Seattle Genetics, Inc.

Advances in protein expression and related technologies have enabled the establishment of expression platforms and flexible manufacturing to help deliver high yield, rapid development timelines and desired product quality profile. In addition, protein and process engineering efforts have led to development of new bio therapeutic modalities, including high potency molecules. Examples of different antibody therapeutics, their development challenges, and innovations to meet these challenges will be reviewed. The evolving use of new information on genome structure and cell metabolism for expression optimization will be discussed.

8:40 Featured Presentation:
Enhanced Protein Production in Mammalian and Insect Cells by Precise Genome Editing with the Cas9/CRISPR Technology

Lorenz Mayr, Ph.D., Vice President, Reagents & Assay Development, AstraZeneca

We will describe recent developments for transient gene expression (TGE) and precise genome editing (PGE) in mammalian and insect cells. We predict that PGE with the novel Cas9/CRISPR technology will change the way how recombinant proteins will be produced in the future.

9:10 Using the Endoplasmic Reticulum as a Physiological Test Tube: Predicting Poor Solution Behaviors of mAb Clones during Transient Expression in cellulo

Haruki Hasegawa Ph.D., Principal Scientist, Therapeutic Discovery, Amgen, Inc.

Have you picked a lead candidate mAb clone that looked very promising until tested in formulation? How can we avoid selecting physicochemically unfavorable mAb clones unknowingly? In this talk, I will discuss the predictive values of overexpression-induced cellular phenotypes in assessing the solution behavior properties of individual mAb clones. Our approach paves the way for a preemptive elimination of unfavorable mAb clones from the lead panel from the very beginning.

9:40 Featured Presentation:
MicroRNAs: Targets for Improving CHO Cells as Protein Factories

Colin Clarke, Ph.D., Bioinformatics Research Fellow, National Institute for Cellular Biotechnology (NICB), Dublin City University

MicroRNAs (miRNAs) have emerged as an exciting means of engineering the expression of multiple proteins or even entire pathways to build better CHO cells. A number of studies have reported the association of miRNAs with desirable industrial phenotypes and demonstrated how the manipulation of miRNA expression levels can improve CHO cell culture performance. This presentation will give an overview of the current state-of-the-art in the field.

10:10 GeneOptimizer Program-Assisted cDNA Reengineering Enhances sRAGE Autologous Expression in Chinese Hamster Ovary Cells

Case StudyLi Lin, Ph.D., Senior Research Fellow, Laboratory of Cardiovascular Science, National Institute on Aging, National Institutes of Health (NIH)

Soluble receptor for advanced glycation end products (sRAGE) functions as a decoy to counter-react RAGE signaling-resultant pathological conditions, and has high therapeutic potential. Our studies showed that recombinant human sRAGE expressed in CHO cells is modified by specific N-glycosylation, and exhibits higher bioactivity than that expressed in other host systems. We reengineered sRAGE cDNA using the GeneOptimizer program and the resultant cDNA augmented sRAGE expression over 2 fold and maintained bioactivity.

10:40 Coffee Break in the Exhibit Hall with Poster Viewing


Bacteria/Escherichia Coli  

11:25 Hijacking E. coli’s Heat-Shock Response Enhances Recombinant Protein Production

Xin Zhang, Ph.D., Burroughs Wellcome–CASI Fellow, Scripps Research Institute

The production of high-yield and high-quality recombinant proteins from Escherichia coli is highly desirable for both academic and industrial settings. In this talk, I will describe a generally applicable method for this purpose, using a transcriptionally reprogrammed E. coli by overexpressing a heat-shock response transcription factor. Similar strategies of hijacking stress-responsive pathways should be useful to enhance cellular protein folding capacity and improve recombinant protein production in other cell types.

11:55 Using Chromosomal Engineering for Enhanced Protein Expression in Bacteria

Unpublished DataJoseph D. Kittle, Jr., Ph.D., Assistant Professor, Chemistry and Biochemistry, Ohio University; Founder, Molecular Technologies Laboratories LLC

Traditional protein expression systems rely on the use of plasmids for production of proteins from cloned genes. We present data showing the advantages of using synthetic DNA to rapidly engineer bacterial chromosomes to produce commercially important levels of high value proteins. The improved stability and lack of antibiotics in the fermentation media provide for impressive overall improvements in gene-to-commercial scale production.

12:25 pm Optimizing CHO Expression for Rapid Identification of Relevant Drug Candidates with Flow Electroporation

Weili Wang, Ph.D., Principal Scientist, Protein Production, MaxCyte

When preclinical research is done in a cell line other than the manufacturing cell line, promising candidates are overlooked while irrelevant candidates are put forward. Flow electroporation, a universal means of fully scalable TGE capable of producing multiple grams of antibodies, bispecifics, and non-antibody like recombinant proteins, enables R&D with CHO cells for rapid clinical-grade biotherapeutics. Using this technology and optimizing cell culture and transfection variables to further increase the amount of antibody produced will be discussed.

12:55 Luncheon Presentation I: Whole-System Expression Engineering

Mark Welch, Ph.D., Director, Research, DNA2.0 Inc.

With gene synthesis and current molecular biology technologies, expression systems can be readily engineered at the gene, vector, and host genome levels. We describe applications where engineering tools and machine learning are leveraged to systematically optimize protein production. Examples of gene, protein, vector and strain engineering are discussed for a range of target proteins and expression hosts.

1:25 Luncheon Presentation II to be Announced

1:55 Session Break


Baculovirus and Algae 

2:10 Chairperson’s Remarks

Sam Ellis, Vice President, Thomson Instrument Company

2:15 Baculovirus Expression of HSV-2 Vaccine Antigens: Challenges and Solutions

Unpublished DataRajiv Gangurde, Ph.D., Associate Director, Protein Production, Genocea Biosciences, Inc.

GEN-003 is a therapeutic HSV-2 subunit vaccine containing two antigens expressed independently in insect cells. The antigens were expressed as Histidine-tagged proteins as part of a successful Phase 1 campaign. For Phase 2 and beyond, we eliminated Histidine-tags and revised the expression parameters to significantly improve protein titer and control antigen-specific proteolysis. The approaches employed and resulting outcomes will be discussed.

2:45 Production of Antibody Toxin Fusions as a Next-Generation Targeted Therapy Using Algae Chloroplast

Miller Tran, Ph.D., Senior Scientist, Lead Discovery, Verdant Therapeutics, Inc.

Over the last decades, targeted antibody therapies including antibody-drug conjugates and recombinant immuntoxins have garnered increasing attention. However, their production has become increasingly complicated and expensive. To overcome the challenges associated with the production of targeted therapies, eukaryotic algae are being used to produce recombinant antibody toxin fusions that overcome the shortcomings of established technologies. With media cost in the cents per liter, the potential of algae are now being realized.

3:15 Cell Line Development Tool Box for Expression: E.coli, HEK293, CHO, Insect Cells

Sam Ellis, Vice President, Thomson Instrument Company

The conditions for E.coli, HEK293, CHO and Insect Cell lines need to be maintained at small scale and within fermentation. Data will be presented on techniques and technology that allow for mimicking large scale fermentation with non-controlled devices from 1mL-3L. All of these techniques are proven technologies for protein production, structural biology, and can lead to successful transfer from different protein groups.

3:45 Refreshment Break in the Exhibit Hall with Poster Viewing

4:45 Problem-Solving Breakout Discussions

5:45 Networking Reception in the Exhibit Hall with Poster Viewing

7:00 End of Day

Day 1 | Day 2 | Download Brochure | Register 


8:00 am Morning Coffee


Compare/Contrast Expression Systems 

8:30 Chairperson’s Remarks

Lorenz Mayr, Ph.D., Vice President, Reagents & Assay Development, AstraZeneca

8:35 E. coli and CHO Protein Expression Technology at Genentech

Case StudyDorothea E. Reilly, Ph.D., Associate Director, Early Stage Cell Culture, Genentech, Inc. – A Member of the Roche Group

9:05 Differences in Clearance of Recombinant Proteins Expressed in HEK and CHO Cells

Mengmeng Wang, Ph.D., Principal Scientist, PDM, Pfizer, Inc.

This investigation used in vitro cell-based uptake assay and in vivo PK studies to study the relationship between glycosylation and clearance of two monomeric versions of antibody that was produced either transiently by HEK293 cells or stably by CHO cells. We demonstrated that higher clearance of the HEK derived protein was likely due to its higher mannose receptor mediated clearance and co-administration of mannose receptor inhibitor, Mannan, can reduce the clearance.

9:35 A Comparison of Two Methods for the Transient Expression and Purification of Ebola Glycoprotein from HEK-293 and CHO Cells

Unpublished DataChristopher W. Kemp, Ph.D., President, Kempbio, Inc.

Advances in transient mammalian expression protocols allow proteins to be expressed at levels supportive of large-scale applications. The ability to rapidly produce diagnostic antigens is of particular interest in the area of emerging viral diseases. This presentation focuses on the comparison of PEI-mediated transient transfection and BacMam transduction for the expression of Ebola glycoprotein. The gene-to-protein approach illustrates the utility of these methods for the rapid production of diagnostic antigens.

10:05 Coffee Break in the Exhibit Hall with Poster Viewing



11:05 Optimizing the Quality of IgGs Produced in Yeast – Removal of Glycans at a Non-Consensus Asparagine Residue

Juergen Nett, Ph.D., Senior Principal Scientist, Adimab, LLC

Yeast cells offer a facile way to produce milligram quantities of IgGs for screening in high-throughput workflows. In order to avoid the addition of large, high-mannose glycans the consensus asparagine at position N297 is often removed by site directed mutagenesis. Despite this modification, IgGs produced in yeast often are decorated with additional, high molecular weight glycan structures. This talk will provide an overview on how sequence optimization and purification are able to remove these unusual post-translational modifications.

11:35 Double Digit-Titers and High Product Quality of Nanobodies® Using Pichia pastoris

Unpublished DataPeter Schotte, Ph.D., Section Head, CMC - Host Creation, Ablynx nv

Pichia pastoris is currently Ablynx’ preferred production host for Nanobodies, a novel class of therapeutic proteins based on single-domain antibody fragments, mainly because of its high expression yields and low amount of secreted host cell proteins, resulting in short process development timelines. This presentation will address the different aspects of Pichia process development for Nanobody production, from host creation to fermentation and downstream processing, with the main focus on the optimization of product yield and quality.

12:05 pm Meeting the Need for Rapid Protein Expression and Development with a Cloud-Based Informatics System

Diane Retallack, Ph.D., Director, Molecular Biology, Pfēnex, Inc.

Pfēnex Expression Technology™ has been developed as a protein production platform to rapidly identify strains that express high titers of soluble, active protein. Employing a combinatorial approach to strain engineering, thousands of unique expression strains are evaluated in parallel. Core LIMS™ enables tracking results from strain construction/ screening through fermentation and protein purification.

12:20 Sponsored Presentation (Opportunity Available)

12:35 End of Conference

5:15 Registration for Dinner Short Courses

Recommended Dinner Short Course* 

SC14: Strategic Bioassay Design and Analysis 

*Separate registration required.

Day 1 | Day 2 | Download Brochure | Register