January 13 - 17, 2014
Renaissance Hotel and Palm Springs Convention Center Palm Springs, California

A Community Dedicated to the
Evolving Field and Future of Biotherapeutics
Archived Content

Choosing Designing and Optimizing Hosts and Platforms 


The high demand for larger amounts of protein,  in shorter periods of time continues to plague protein researchers.  Sometimes this requires new technologies and strategies, other times it requires a re-working or re-engineering of existing resources to improve outcomes.  The central issue of this work is making wise and effective choices in the selection of the host for protein expression.  This conference explores the newest data and innovations relating to the best choices in hosts/systems, as well as ways to “rescue” existing systems and make them work more effectively to produce the quantity and quality of your proteins.

Day 1 | Day 2 | Download Brochure 

TUESDAY, JANUARY 10

1:30 pm Conference Registration

2:00 BuzZ Session A 

2:45 Refreshment Break in the Exhibit Hall with Poster Awards

3:30 - 4:15 BuzZ Session B 

 


WEDNESDAY, JANUARY 11

7:00 am Conference Registration

7:30 Breakfast Presentation (Sponsorship Opportunity Available) or Morning Coffee

 

Getting More for Your Money in Eukaryotes 

8:15 Chairperson's Opening Remarks


» KEYNOTE PRESENTATION

8:20 Protein Expression in Drug Discovery – New Challenges, New Solutions

Lorenz Mayr, Ph.D., Executive Director, CPC/EPP, Novartis Pharma AG

This presentation will describe our comprehensive and contemporary framework of protein expression technologies, including: an overview of established protein expression technologies at Novartis; novel trends and demands for proteins in hit discovery and lead optimization; novel technologies and trends for protein expression in drug discovery research; case studies for difficult-to-express proteins and protein complexes; finding the balance between in-house efforts and outsourcing; and a summary and outlook.


9:00 Optimizing the Baculovirus-Insect Cell Platform for Recombinant Glycoprotein Expression

Donald Jarvis, Ph.D., Professor, Molecular Biology, University of Wyoming

The baculovirus platform is constrained by the fact that the insect cell lines used as hosts for baculovirus expression vectors have relatively primordial protein glycosylation pathways that fail to produce sialylated glycoproteins. We addressed this problem by glycoengineering the baculovirus-insect cell system to humanize the protein N-glycosylation pathway. In this presentation, I will report the results of our latest glycoengineering efforts and their impact on our efforts to optimize the baculovirus insect cell platform for recombinant glycoprotein expression.

9:30 Early Markers of Production Instability of Recombinant Chinese Hamster Ovary Cell Lines

Ulrich Göpfert, Ph.D., Pharma Research and Early Development, Roche Diagnostics Gmb

We have established methylation-specific real-time qPCR for the rapid and sensitive measurement of hCMV-MIE methylation in multiple cell lines and provide evidence that hCMV-MIE methylation and transgene copy numbers can be used as early markers to predict production instability of recombinant CHO cell lines. These markers should provide the opportunity to enrich stable producers early in cell line development.

10:00 Networking Coffee Break in the Exhibit Hall with Poster Viewing

 

Maximizing Success in Prokaryotes 

10:45 Generation and Screening of Pichia pastoris Strains with Enhanced Protein Production by Use of Microengraving

J. Christopher Love, Ph.D., Associate Professor, Department of Chemical Engineering, Massachusetts Institute of Technology

The selection of highly productive cell lines remains a key step for manufacturing therapeutic proteins. Microengraving was used to screen chemically mutagenized populations of Pichia pastoris for increased production of an Fc fragment. Clones retrieved following three rounds of mutagenesis yielded titers 2.65-fold greater than those of the parental strain.

11:15 Engineering of Escherichia coli for Endotoxin-Free Production of Recombinant Proteins and Plasmid DNA

Uwe Mamat, Ph.D., Research Professor, Center for Medicine and Biosciences, Research Center Borstelpeaker

It has previously been impossible to generate a truly viable E. coli strain that completely lacks LPS. This new series of strains solves this important problem of protein and DNA production in E. coli for the first time. Efficient and cost-effective elimination of endotoxin is a challenging task, and none of the downstream applications described thus far remove endotoxin entirely. Presented here are E. coli strains that lack outer membrane agonists for TLR4/MD-2 activation.

11:45 E. coli Periplasmic Expression of Fab' Fragments at 2-5g/l

Mark Ellis, Sr. Scientist, Protein Expression and Purification, UCB Celltech

We have engineered variants of wild type E. coli strains in order to significantly improve periplasmic expression yields. In combination with plasmids co-expressing E. coli host proteins and process refinements we have achieved purified Fab' yields in the 2 to 5g/l range with a number of clinically relevant Fab's. These technological improvements have also enabled the expression of a variety of 'difficult' proteins at several hundred mg/l and hence have the potential for a broad impact on both the production of novel therapeutic formats and supply of research reagents.

    Sponsored by
MaxCyte 
12:15 pm Accelerating Biotherapeutic Development Pipelines by Producing Gram-level Quantities of Antibodies Using Large-volume, Transient Transfection of CHO Cells
James Brady, Ph.D., Director, Technical Applications, MaxCyte, Inc.Data will be presented showing rapid production of antibodies with the correct post-translational modifications using scalable transient transfection of up to 1E10 CHO cells via MaxCyte flow electroporation.  MaxCyte transient transfection simultaneously (co)transfected CHO cells with heavy and light chain plasmids with high efficiency and high cell viability. Following optimization of post electroporation culture conditions secreted protein titers indicate that production of more than one gram of antibody is possible from a single transfection thereby eliminating the need to conduct antibody development in non-CHO based systems. 

12:30 Luncheon Presentations (Sponsorship Opportunity Available) or Lunch on Your Own

 

Stepping Up to High-Throughput Expression 

2:00 Chairperson's Remarks

Dominic Esposito, Ph.D., Director, Protein Expression Laboratory, SAIC-Frederick, Inc.

2:05 Maximizing the Success of Protein Expression in High-Throughput Fashion

Yvonne Franke, Ph.D., Scientist, Structural Biology, Genentech, Inc.

We have implemented a high-throughput cloning and protein expression platform which enables us to increase efficiency and effectiveness of successfully producing soluble proteins amenable for various applications. Our platform is combining strategies such as restriction-independent cloning, plasmid purifications using Phynexus technology, small scale baculovirus infections in multiwell blocks, and analysis of expression levels using Ni-NTA Phytips. Our process enables us to quickly assess protein quality and prioritize constructs for further downstream applications.

2:35 Improving Protein Production in Insect and Mammalian Cells Using Combinatorial Libraries of Expression-Enhancing Elements

Dominic Esposito, Ph.D., Director, Protein Expression Laboratory, SAIC-Frederick, Inc.

Our lab has developed a platform for combinatorial clone production which allows us to rapidly generate large numbers of expression clones in a cheap and efficient manner. With these clones, we have been able to improve our chances of successful protein production in insect and mammalian cells using a combination of promoters, transcriptional enhancers, fusion tags, and expression conditions. The platform technology and a number of case studies will be discussed.

3:05 Genetic Engineering for Enhanced Expression of Difficult-to-Express Proteins in E.coli 

Tomohiro Makino, Ph.D., Associate Senior Researcher, Faculty of Discovery and Biotechnology II, Asubio Pharm Co., Ltd.

Protein expression in Escherichia coli is the most facile approach for the preparation of non-glycosylated proteins for preparative purposes. However, the optimization of recombinant expression has largely remained a matter of trial and error. To solve these problems, we provide the genetic and strain engineering approach useful for enhancing the expression of hard-to-produce proteins, including GPCR and full length IgG. 

Sponsored by
Pfenex Inc.
3:35 Discovery Protein Expression Enabled by Pfenex Expression Technology™

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

Discovery scientists first step in every product development program is the acquisition of active protein. Leveraging the high throughput Pfenex Expression Technology platform, milligram amounts of purified proteins can be produced in support of early stage in vitro and in vivo evaluation. Case studies will provide an overview regarding how Pfenex scientists accomplish this task.

3:50 Refreshment Break in the Exhibit Hall with Poster Viewing

 

Improving Expression and Throughput 

4:30 High-Level Antibody Expression by Adenovirus and Its Application in High Throughput Screening

Changshou Gao, Ph.D., Principal Scientist, Technology, Department of Antibody Discovery and Protein Engineering, MedImmune LLc

5:00 Self-Cleaning Fermentors and Auto-Inducing Media for High-Throughput Parallel Expression in 1–5 l Scale

Alvar Gossert, Ph.D., Investigator, Structural Biology Platform, Novartis Institutes for BioMedical Research

Disassembly, cleaning, re-assembly and sterilization of fermentors is very time consuming (...and dull). We have overcome this major disadvantage of high cell density fermentation by designing a module for cleaning and sterilization in place for laboratory fermentors. With our setup consisting of 8 fermentors with CIP/SIP capability and using modified auto-inducing media for high cell density fermentation, a single person can easily run 16 large scale E.coli fermentations per week and produce large quantities (1–100 mg) of several protein constructs for structure-based drug design by X-ray and NMR.

5:30 - 6:30 Reception in the Exhibit Hall with Poster Viewing


Day 1 | 
Day 2 | Download Brochure 


Links to Companion Meetings

Pipeline 4 

Engineering Genes, Vectors, Constructs and Clones 

Overcoming Challenges, Finding Solutions 

Japan-Flag Korea-Flag China-Simplified-Flag China-Traditional-Flag 


PTK Event APP 
New this year!
The PepTalk App will allow attendees to browse the agenda, create custom schedules, navigate the exhibit hall and explore poster presentations.

2014 Brochure Cover 

Right Arrow Download the Brochure 

Right Arrow Event at-a Glance 

      Premier Sponsors: 

EMD Millipore 

 Novozymes (white) 

PerkinElmer NEW 2009 

 Protein Simple  

  

Right Arrow View All Sponsors 

Right Arrow View Media Partners 

Add to Outlook Add to Outlook 

Training Seminars 

Mon-Tues, January 13-14 

Biologics Formulation and Delivery  

 


Buzz Sessions
BuzZ Sessions are facilitated, small-group discussions. Interactive participation leads to problem-solving solutions and future collaborations around focused topics.
Click here for BuzZ topics