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

Protein Expression: Choosing, Designing & Optimizing Hosts & Platforms header 

Day 1 | Day 2 | Download Brochure 

 

Conference Short Courses*View Details 

Sunday, January 9 - 3:00 pm - 6:00 pm 

  • Protein Crystallization - Delineating Protein Structure
  • DoE and QbD: Tools for Optimizing the Bioprocess

Thursday, January 13 - 6:30 pm - 9:00 pm 

  • Rational Design of Protein Solutions
 

 

Great strides have been made in the expression of proteins for biotherapeutics; however, with these strides have come new hurdles. Higher-throughput expression and purification, as well as more flexible expression systems and techniques are in even greater demand now to support the needs of the research pipeline. This meeting explores the newest data and innovations relating to the expression and characterization of proteins for biological understanding and therapeutics, as well as strategies to make the eventual expression of these proteins more effective, efficient and trouble-free. Attention is given to new hosts and platforms, as well as how to select, engineer and optimize these hosts.

TUESDAY, JANUARY 11 


1:30 pm Conference Registration

2:00 BuzZ Session ABuzz 

2:45 Refreshment Break, Exhibit Viewing and Poster Awards

3:30 BuzZ Session BBuzz 

4:15 End of Day

4:30 Dinner Short Courses 



WEDNESDAY, JANUARY 12 


7:00 am Conference Registration

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

 

ENGINEERING PROTEINS FROM THE GROUND UP 

8:15 Chairperson’s Opening Remarks

M. Raafat El-Gewely, Ph.D., Institute of Medical Biology, University of Tromsø

 

Keynote Presentation 

8:20 Significant Enhanced Expression and Solubility of Human Proteins in Escherichia coli by Fusion with Protein S from Myxococcus xanthus 

Masayori InouyeMasayori Inouye, Ph.D., Distinguished Professor, Center for Advanced Biotechnology and Medicine, Robert Wood Johnson Medical School

N-terminal fusion of human proteins with protein S, a major spore coat protein of Myxococcus xanthus significantly enhances their expression and solubility in E. coli. Fusion proteins can be readily purified in one step with myxospores in the presence of Ca2+. This PST technology with SPP (Single-Protein Production) technology opens a new avenue for functional and structural studies of human proteins.

9:00 Structural Insights into Bacteriophage Protein Complexes Revealed by Hybrid Methods

David Veesler, Researcher, Architecture et Fonction des Macromolécules Biologiques, Université de Provence – Université de la Méditerranée

The combination of robust expression strategies with biophysical approaches (static plus dynamic light scattering, BIAcore) and structural methods (X-ray crystallography, electron-microscopy) allowed us to obtain multi-resolution data on these large macromolecular ensembles and to infer functional and evolutionary aspects. This presentation will thus highlight the crucial impact of hybrid methods to structurally characterize protein-protein complexes and yield a comprehensive view of such biological systems.

9:30 Secretion and Proteolysis of Heterologous Proteins Fused to the Escherichia coli Maltose Binding Protein in Pichia pastoris 

Geoffrey Lin-Cereghino, Ph.D., Department of Chemistry, University of the Pacific

E. coli maltose binding protein (MBP) was explored as a fusion partner to improve the expression and secretion of foreign proteins in Pichia pastoris, a yeast used for recombinant protein production. Proteolysis was found to occur in MBP-cargo protein fusions at different locations in the region C-terminal to the MBP domain but MBP enhanced the secretion of certain cargo proteins.

10:00 Coffee Break, Exhibit and Poster Viewing

10:45 Use of the Design-of-Experiments Approach for the Development of a Refolding Technology for Progenipoietin-1, a Recombinant Human Cytokine Fusion Protein from Escherichia coli Inclusion Bodies

Denis M. Boyle, Ph.D., Director, Biologics Piloting, Pfizer Animal Health R & D

11:15 Overcoming Bottle-Neck Problems in Producing Recombinant Therapeutic Proteins at Early Stages and the Potential Impact of Novel Conformases/Foldases on the Field

M. Raafat El-Gewely, Ph.D., Institute of Medical Biology, University of Tromsø

This presentation will discuss the fact that primary structure is not all that dictates the tertiary structure of proteins. I will also discuss how improving the molecular and genetic environment in the host (initially E. coli) by our novel conformases/foldases (patents pending) can help reduce the impact of the bottle-neck problems in the recombinant field.

    Sponsored by
Pfenex Inc. 
11:45 Rapid Production of High Quality Protein Enabled by Pfenex Expression Technology™
Diane Retallack, Ph.D., Director Molecular Biology, Pfenex Inc.
Platforms for the rapid production of proteins are a 21st century imperative. Pfēnex Expression Technology™ is the most comprehensive expression platform available today, consisting of an extensive, integrated, toolbox of expression components and unique host strains. Case studies describing the expression of challenging proteins, including reagent proteins, will be presented.

 

    Sponsored by
Merck12:00 Luncheon Presentation 
Setting off in the Right Direction  – Using pAVEwayTM and Modular Development to Choose the Best Production Route
Andy Topping, Ph.D., Director of Development, Biomanufacturing, Merck BioManufacturing Network
Selecting the most appropriate mode of protein expression and production is an important early step in process development and often defines how the product will be made for its entire clinical and commercial life. Despite the importance of this decision, the time and resources required at the very earliest stages of development often mean that limited options are explored. The use of the standardized pAVEwayTM expression system and pre-defined modules for the development of refolding steps allows more data to be obtained and more routes considered.




1:00 Luncheon Presentation (Sponsorship Opportunity Available) or Lunch on your own

 

Optimizing and Automating 

2:00 Chairperson’s Remarks

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

2:05 A Toolbox for High-Throughput Parallel Clone Construction for Protein Expression Optimization in Multiple Host Systems

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

We have developed a recombination cloning platform which allows simple, cheap, and highly parallel generation of combinatorial clone elements including promoters, antibiotic resistance markers, solubility and purification tags, and reporter elements. This system can be used to rapidly produce expression constructs for use in different host systems, allowing truly comparative expression optimization to choose the best host system and expression conditions for your protein of interest

2:35 When Proteins Misbehave, Try a Little Pressure: Refolding Pol nu

Robert M. Petrovich, Ph.D., Head, Protein Expression Core Facility, Laboratory of Structural Biology, NIEHS, National Institutes of Health

Heterologous expression of proteins in E. coli is still the first option of most laboratories. The use of solubilization tags, chaperones, specialized cell stains, codon optimization, low temperatures and media formations has yielded a success rate of between 30 and 40 percent of these targets. In my core facility we are using high hydrostatic pressure to refold proteins at high protein concentrations.

3:05 Prediction of Protein Solubility in Escherichia coli Using Logistic Regression

Roger G. Harrison, Ph.D., Associate Professor, College of Engineering, University of Oklahoma-Norman

A new and more accurate model for the prediction of the solubility of proteins overexpressed in the bacterium E. coli is presented. The model uses the statistical technique of logistic regression. To build this model, 32 parameters that could potentially correlate well with solubility were used. The model exhibits excellent overall prediction accuracies: 94% for the model and 87% by cross-validation.

3:35 Sponsored PresentationSponsored by
Thermo Scientific logo
 

Human In Vitro Translation Systems for Rapid Production of Functional ProteinsPeter A. Bell, Director Proteomics R&D, Thermo Fisher Scientific
In vitro expression systems provide a quick route to the production of functional proteins.  We report here the use of a novel system derived from human cell lines for the production of microgram to milligram quantities.  Examples of >100 proteins, including Akt, MAPK, Aurora A kinases and membrane proteins are given. Application of in vitro translated proteins in co-immunoprecipitation, rapid mutational analysis, nucleic acid-protein interactions and drug screening are also presented.



3:50 Networking Refreshment Break 

4:30 Development of a Fully Automated, Miniaturized Bioreactor System for Optimization of Protein Production Processes

Jacques Bellalou, Ph.D., Head, Platform for Recombinant Protein Production in Microorganisms, Structural Biology & Chemistry Department, Institut Pasteur

The ability to cultivate various cell species under parallel and a wide variety of controlled environments and to evaluate the effect of operational parameters on cell growth and protein expression is actually limited by a lack of versatile and automated system. Our currently commercialized version of the device, termed Biopod 800, is an innovative engineering technology developed to control parallel and fully automated culture conditions of novel host vector combinations.

5:00 High-Throughput Protein Expression Using an Improved Drosophila S2 Expression System

Wian de Jongh, Ph.D., Team Leader, Insect Cell Expression, University of Copenhagen, The Novo Nordisk Foundation - Center for Protein Research

The Drosophila S2 insect cell expression system is very well suited to the task of expressing complex proteins of medical relevance. In this work we further developed the system as a high-throughput platform for protein expression. The method is based on high-throughput cloning and protein expression in 96-well format. This simple, rapid and robust method should lead to significant time-savings in protein screening projects. Furthermore, as the S2 expression system has been used for clinical material manufacture (up to phase II), the results from protein screening can be directly applied to pre-clinical and clinical research, without changing host organism.

5:30 Reception in the Exhibit Hall

6:30 Close of Day

 

Day 1 | Day 2 | Download Brochure 



Links to Companion Meetings

Pipeline 1 

Targeting Genes, Engineering Vectors, Designing Constructs and Optimizing Clones 

Overcoming Protein Expression Challenges with Solutions 

Membrane Proteins 

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