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THURSDAY, JANUARY 12
7:30 am Breakfast Presentation (Sponsorship Opportunity Available) or Morning Coffee
8:15 Chairperson's Opening Remarks
8:20 Production of Vaccines and Human Therapeutics in the Chloroplast of Chlamydomonas reinhardtii
James Gregory, Ph.D., Postdoctoral Researcher,Division of Biological Sciences, UC San Diego
We are developing the genetic tools to enable algae to produce biomass that can be harvested for bio-fuels, bio-products, and feedstock. To date we have successfully introduced biosynthetic enzymes to modify hydrocarbon biosynthesis, as well as a variety of genes that allow production of valuable protein co-products in micro-algae. The challenges, potential, and some early successes of utilizing the chloroplast of C. reinhardtii to produce a malarial transmission blocking vaccine will be discussed.
8:50 New HEK EBNA Cell Based High-Throughput Protein Production Platform
Bjorn Voldborg, Ph.D., Head, Protein Production Unit, University of Copenhagen
9:20 The Manufacture of Biotherapeutic Proteins and Vaccines in Whole Plants
Terence Ryan, Ph.D., Senior Vice President, R&D, iBio, Inc.
A wide range of biotherapeutics, including monoclonal antibodies, growth factors, replacement proteins and subunit vaccines can be rapidly and efficiently manufactured using transient expression systems in plants. The use of this technology to manufacture proteins used in several clinical trials will be presented, as well as the highly versatile nature of this expression system will be discussed.
9:50 Sponsored Presentation (Opportunity Available)
10:05 Networking Coffee Break in the Exhibit Hall, Poster Awards
10:45 The Baculovirus Expression Platform: Recent Advances & More Lessons Learned
James M. Groarke, Ph.D., Biortus Biosciences
11:15 Production of Recombinant Hydroxylated Collagenous Protein in Escherichia coli by Activation of Human Prolyl 4-Hydroxylase
Sheng Ding, Chemical Engineering, Schools of Medicine and of Engineering, Stanford University
We have created a strain of Escherichia coli that produces recombinant proteins with high levels of (2S,4R)-4-hydroxyproline, by biosynthesizing ascorbate-like molecules in bacteria that heterologously express human prolyl 4-hydroxylase (P4H). We explore P4H-mediated collagen folding in the new system by analyzing collagenous materials produced with varying hydroxylation levels. Our work creates a foundation for better understanding how ascorbate-dependent post-translational modifications affect proteins.
11:45 Higher Accumulation of F1-V Fusion Recombinant Protein in Plants after Induction of Protein Body Formation
Guy Cardineau, Ph.D., Director, Professor, Center of Agrobiotech, Tec de Monterrey
Our main goal was to increase recombinant protein accumulation in plants in order to enhance the efficiency of orally-delivered plant-made vaccines. As a part of a project to develop a plant-made plague vaccine, we expressed our model antigen, the Yersinia pestis F1-V antigen fusion protein, with and without a fused Zera domain. We demonstrated that Zera-F1-V protein accumulation was at least 3x higher than F1-V alone when expressed in three different host plant systems: Ncotianabenthamiana, Medicago sativa (alfalfa) and Nicotianatabacum NT1 cells. We confirmed the feasibility of using Zera technology to induce protein body formation in non-seed tissues.
12:15 pm Close of Morning Session
12:30 Luncheon Presentation
Protein Expression in CHO Cells: Comparison of GPEx® to a Traditional Cell Line Engineering Technology
Gregory T. Bleck, Ph.D., Research and Development Platform Lead-Biologics, Catalent Pharma Solutions
Speed, cell line stability, high productivity and excellent protein quality are the goals of any mammalian cell line engineering technology, but does the way cell lines are made have any impact on their ability to produce a hard to express protein? GPEx® is a versatile protein expression system which is capable of transferring genes of interest into a wide variety of mammalian host cells. A comparison was performed between GPEx® and a traditional cell line engineering technology. An antibody that was easy to express using traditional methods and three molecules that were poor producers and/or had poor cell line stability using traditional methods were analyzed. Cell lines expressing the four products were developed using both traditional methods and GPEx®. No significant difference was observed for the easy to express antibody between the two approaches, however for the other three problem molecules, GPEx® equivalent cell lines outperformed in both protein production and stability. Results of the analysis will be discussed.
1:00 Luncheon Presentation (Sponsorship Opportunity Available) or Lunch on Your Own
1:30 End of Conference
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Links to Companion Meetings
Engineering Genes, Vectors, Constructs and Clones
Overcoming Challenges, Finding Solutions