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Day 1 | Day 2
Tuesday, August 25, 2009
7:30am Morning Coffee (Sponsorship Opportunity Available)
8:25 Chairperson’s Remarks
Fabien Walas, Ph.D., Senior Scientist/Project Leader, ERA Biotech
8:30 Plant-Produced Human Cholinesterases and Plant Cholinesterase(s)
Tsafrir Mor, Ph.D., Associate Professor, School of Life Sciences, The Biodesign Institute, Arizona State University-Tempe
Bioscavenging of organophosphates by human cholinesterases is emerging as a promising medical intervention for prophylaxis and post-exposure treatment against chemical warfare nerve agents and pesticides, meeting considerable success in pre-clinical studies. Cholinesterases are very efficient in sequestering organophosphates that become covalently bound at the active site. As an alternative to mammalian expression systems that are supply-restricted, of limited scalability, expensive and potentially contaminated with human pathogens and prions, we have introduced plants as a production system for human cholinesterases.
9:00 Micro-Algae as a Platform for the Production of Therapeutic Proteins
Steve P. Mayfield, Ph.D., Associate Dean, Department of Cell Biology, The Skaggs Institute for Chemical Biology, The Scripps Research Institute
The use of micro-algae as a biotechnology platform lags behind other organisms, especially bacteria and yeast. This is somewhat surprising given the ability of algae to be grown at very large scale in a cost-effective manner. Eukaryotic algae offer tremendous potential for the large-scale and cost-effective production of recombinant proteins, including human and animal therapeutics.
9:30 Engineered Micro-Algae to Produce Glycosylated Proteins
Aude Carlier, Ph.D., CSO and Co-Founder, ALGENICS
AlgBiosys™ is a promising platform using micro-algae as a novel cell factory for the production of glycosylated proteins. Host cells with high industrial capabilities have been identified among the tremendous biodiversity of micro-algae. The ability to perform complex N-glycosylation devoided of immunogenic epitopes was an essential criteria in the species selection. This screening has led to the identification of algae lacking the plant xylose and fucose immunogenic epitopes. Surprisingly, Chlamydomonales was rejected due to the presence of these undesired epitopes in several species of this Order. As a proof of concept, the diatom Phaeodactylum tricornutum was chosen to express murine erythropoietin (EPO), a major therapeutic glycoprotein. EPO secretion into the media was achieved conferring an outstanding advantage to this host.
10:00 Sponsored Presentation (Opportunity Available – Please contact Suzanne Carroll at firstname.lastname@example.org)
10:15 Networking Coffee Break with Exhibit and Poster Viewing
MAKING IT WORK
11:00 In vivo Encapsulation of Recombinant Proteins as Universal Production Platform
The encapsulation of functional proteins in StorPro® organelles is a host independent technology that increases expression levels in eukaryotic cells and is compatible to existing productivity enhancing systems. On one hand cells are protected from potentially toxic proteins, but on the other hand encapsulation prohibits proteolysis and degradation of proteins. Further advantages are the simplified downstream processing that relies on the efficient separation of the organelles from contaminating proteins. This shortens process times and lowers cost of goods. We will show case studies on productivity gains and novel applications in the area of therapeutic proteins, enzymes, and vaccine production and results from a HT platform.
11:30 Expression, Refolding and Purification of a Human Therapeutic Protein for Clinical Use
Peter Sondermann, Ph.D., Chief Scientific Officer, SuppreMol GmbH
The production of soluble receptor for the Fc portion of IgG (sFcgRIIb) is hampered by the low yields of secretion in both mammalian and prokaryotic expression systems. Using an alternative approach we expressed sFcgRIIb in E.coli inclusion bodies. With an elaborated refolding process using standard chromatography material, we were able to circumvent immunogenic affinity tags and/or an affinity column with limited suitability for the production of clinical grade material. Altogether, we are able to present an economic process delivering high yields of pure sFcgRIIb for clinical studies to be conducted this year.
12:00pm Baculovirus Generated Proteins for Structure-Based Drug Design: Lessons Learned
James Groarke, Ph.D., Biologics Center, Novartis Institutes for BioMedical Research, Cambridge
Generation of recombinant proteins in heterologous systems (specifically baculovirus infected insect cells) has become the workhorse for supplying proteins to support structure based drug design. Whilst these systems are generally reliable, many obstacles still remain in utilizing these expression systems to their full potential (expression levels, insolubility, scale-up issues, post-translational modification for example). This talk will focus on recent advances in techniques and technologies that are being employed to overcome these aforementioned obstacles. Case Studies will be presented from the baculovirus expression platform that highlights utilization of these technologies and improvements in the throughput process.
12:30 Lunch on Your Own (Lunch Presentation Opportunity Available)
1:55 Chairperson’s Remarks
Paul Ramage, Ph.D., Senior Research Investigator 1, CPC/Protease Platform, Novartis Pharma AG
2:00 New Fluorescent Protein Scaffolding
Geoffrey S. Waldo, Ph.D., Team Leader, Biosciences, Los Alamos National Laboratory
2:30 Cell-Free Expression of Membrane Proteins for Functional and Structural Studies
Frank Bernhard, Ph.D., Lab Leader, Institute of Biophysical Chemistry, Goethe University Frankfurt
Cell-free expression eliminates most central problems associated with the conventional cellular production of membrane proteins and it allows completely new expression approaches by the direct synthesis of membrane proteins into defined artificial hydrophobic environments like detergents or lipids. We present the production of representative sets of membrane proteins involved in transport, efflux, signaling, metabolism or biosynthesis in mg amounts in a single ml of cell-free reaction mixtures by throughput optimization strategies. The quality of selected membrane proteins including eukaryotic solute carriers, G-protein coupled receptors and diverse types of transporters has been evaluated by a number of complementary techniques. We demonstrate the preparative scale production of pharmaceutical important targets such as G-protein coupled receptors or Alzheimer’s disease related proteins in high quality in less than 24 hours and we present new strategies for their specific labeling and their functional as well as structural evaluation in particular by NMR spectroscopy.
3:00 Recombinant Proteins Produced by PCR-based Gene Synthesis for Macromolecular Crystallization
Joseph D. Ng, Ph.D., ExtremoZyme, Inc.; Associate Professor, University of Alabama
A PCR-based gene synthesis method is used to assemble the coding regions of novel hyperthermophilic proteins for crystallization and X-ray crystallographic structure determination. The gene synthesis procedure is based on sequential assembly such that homogeneous DNA products can be obtained after each synthesis step without extensive manipulation or purification requirements. Coupling the gene synthesis procedure to in vivo homologous recombination techniques allowed efficient subcloning and error correction for the recombinant production and crystallization of PAZ (Piwi/Argonaute/Zwille) domain, a siRNA-binding domain of an Argonaute protein homologue and a deletion mutant of a family A DNA polymerase (PolA).
3:30 Networking Refreshment Break with Exhibit and Poster Viewing
4:00 Non-Viral Production of Human Interleukin-7 as a Soluble Recombinant Protein in Insect Cells
Satya Prakash, Ph.D., Director, Biomedical Technology and Cell Therapy Research Laboratory, McGill University
In a somewhat new approach we have used insect cell lines viz., Spodoptera frugiperda (Sf9), which have been stably transformed to express the reporter protein secreted alkaline phosphatase (SEAP). The system has also been studied for the production of a potential therapeutic glycoprotein, human Interleukin-7 (hIL-7). A comparison of protein expression using the Baculovirus system has been done and the culture of stably transfected Sf9 insect cell cultures in a conventional stirred tank bioreactor, disposable Wave bioreactor system, using batch and fed batch strategies has been studied. Details of these studies will be discussed.
4:30 Exploring the Myth of Glycosylation for Crystallization
5:00 Novel Eukaryotic Expression System Based on Protozoan Host Leishmania tarentolae
Reinhard Breitling, Ph.D., Group Leader, Protein Expression, Jena Bioscience GmbH
Leishmania tarentolae is a robust, fast-growing protozoan organism with full spectrum of eukaryotic protein modifications including the mammalian-type glycosylation. We have developed this organism into the flexible and efficient protein expression platform called LEXSY. Recombinant proteins can be expressed intracellularly, or be secreted into medium. Both constitutive or inducible expression architectures are available. Protein expression levels can be monitored directly during cultivation through a transcriptionally coupled fluorescence marker. Numerous proteins, including surface antigens, toxins, antibodies and membrane proteins have been expressed with LEXSY.
5:15 Development of Next Generation Hansenula polymorpha Strains for the Production of IFNalpha-2a
Andreas Kranz, Ph.D., Project Manager, Research, ARTES Biotechnology GmbH
Here we show a systematic expression optimization approach shifting this unfavorable stoichiometry towards almost 100% correctly processed IFNa-2a in this system is based on the expression of a fusion ORF encoding MFa prepro-IFNa. The methylotrophic yeast Hansenula polymorpha has proven to be a robust and cost-effective platform for the production of many types of pharmaceutically interesting proteins and technical enzymes. Several registered products prove the safety and efficacy of this system and its advantages over other yeast as well as bacteria.
5:30 End of Optimizing Cell Culture Technology and Specialized Protein Expression Systems Conferences
For exhibit and sponsorship information, please contact:Suzanne Carroll, Manager, Business Development
Cambridge Healthtech Institute
Phone: 781-972- 5452
250 First Avenue Suite 300Needham, MA 02494P: 781.972.5400F: 781.972.5425E: email@example.com
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