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EVENT FEATURES:
  • Protein Expression
  • High-Throughput Screening
  • Optimizing Protein Production
  • Breakthroughs in the Lab
  • Scale-Up & Manufacturing
  • Techniques & Technologies
  • Case Studies Presented – Current Successes

KEYNOTE PRESENTATION: 
Regulatory Evaluation of Baculovirus-Produced Vaccines
Philip R. Krause, Ph.D., Lead Research Investigator, Center for Biologics Evaluation & Research, U.S. Food & Drug Administration 

FEATURED SPEAKER: 
Quality Assessment of GSK’s Cervical Cancer Candidate Vaccine Manufactured with the Baculovirus Expression Vector System (BEVS) 
Michel Deschuyteneer, Ph.D., Scientist, Analytical R&D, GlaxoSmithKline Biologicals

“So much great information, I can't wait to get back to the lab!”

Susan H., Associate Scientist II, Novartis Institutes for BioMedical Research

“Very exciting conference. Covered a broad range from historical to state-of-the-art. Highly recommended.”

Imre B., Group Leader, Institute for Molecular Biology & Biophysics, ETH Zurich

TIPS Workshop – 
Titerless Infected-cell Preservation and Scale-up*
Thursday, September 20 • 2:00-5:00pm

Still titering your baculovirus stocks? Don’t!

Still worrying about the stability of baculovirus stocks? Don’t’ worry, be happy!

Have problems with unstable stocks or difficult-to-express proteins? Bring your projects!

Want to start scaling up to 100 liters and beyond in three weeks? Don’t miss this workshop!

Are you looking for some hot TIPS on how to efficiently express proteins with baculovirus using a very simple, fast, and versatile method? Then don’t miss the baculovirus TIPS workshop presented by Ed Lee from Pfizer.

In the workshop, Ed will:
(1) go over the principle and practice of TIPS (Titerless Infected-cell Preservation and Scale-up) first, (2) answer your questions and look at your projects, and (3) help you with hands-on experimental designs.

Come to the workshop, bring TIPS back to your workplace, and forever change the way you do your baculovirus work!

*Separate Registration Required

WEDNESDAY, SEPTEMBER 19 - DAY ONE

7:30am Registration and Morning Coffee

Baculovirus: The Big Picture

8:30 Chairperson’s Remarks

8:40 KEYNOTE PRESENTATION: 
Regulatory Evaluation of Baculovirus-Produced Vaccines
Philip R. Krause, Ph.D., Lead Research Investigator, Center for Biologics Evaluation & Research, U.S. Food & Drug Administration 

9:20 FEATURED SPEAKER: 
Quality Assessment of GSK’s Cervical Cancer Candidate Vaccine Manufactured with the Baculovirus Expression Vector System (BEVS) 
Michel Deschuyteneer, Ph.D., Scientist, Analytical R&D, GlaxoSmithKline Biologicals 

10:00 Networking Coffee Break

BEVS—More than Making Proteins in Insect Cells

10:35 Chairperson’s Remarks

10:40 Baculovirus Display: Targeting and Gene Delivery to Cancer Cells
Christian Oker-Blom, Ph.D., Professor in Biotechnology, Department of Biological and Environmental Science, University of Jyväskylä, Finland 
Baculovirus is a versatile tool for eukaryotic virus display and gene delivery to mammalian cells. Baculovirus display, a recently established molecular biology tool, allows combination of genotype with phenotype enabling presentation of foreign peptides or even complex proteins on the baculoviral envelope or capsid. Thus, the tropism of baculovirus can be modified – a feature of importance when targeting and gene and/or protein delivery to mammalian cells is concerned. The design and behavior of baculovirus-based tumor-targeted viral display vectors will be discussed. 

11:10 A Novel Baculovirus Vector for Reducing Proteolysis
Richard Hitchman, Ph.D., SLS, Oxford Expression Technologies, Oxford Brookes University
Viral chitinase is expressed in the late phase of virus replication and in conjunction with viral cathepsin promotes liquefaction of the larval host in the later stages of infection. Deletion of chitinase has been shown to improve the transition of recombinant proteins through the secretory pathway and deletion of both chitinase and cathepsin can significantly improve protein stability and integrity. We describe a novel baculovirus expression vector with complete deletions of both chitinase and cathepsin.

11:40 Unique Ability of Baculoviral Expression System to Produce Monomeric MD-2 Apoprotein and a Ligand for Toll-like Receptor 4, Monomeric Endotoxin:MD-2 Complex
Theresa Gioannini, Ph.D., Research Scientist, The Inflammation Program, University of Iowa
Defense against bacterial invasion depends upon molecular alarm systems that are sensitive and specific. The most sensitive alarm system for response to Gram negative bacteria depends on presentation of unique Gram-negative bacterial glycolipids (endotoxin) to Toll-like receptor 4 (TLR4) via the sequential action of the host proteins lipopolysaccharide-binding protein (LBP), CD14, MD-2 and Toll-like receptor 4 (TLR4). The ability to culture insect cells at 27°C and the stability of MD-2 monomer and E:MD-2 in insect culture medium has made possible production and purification of >1 mg E:MD-2/liter of conditioned medium. The stability in aqueous buffers of E:MD-2, in contrast to MD-2 alone, and the ability to produce discrete structural variants of E:MD-2 that are either TLR4 agonists or antagonists provide unique experimental tools to better characterize the structural basis of TLR4 activation by E (E:MD-2). Results obtained with MD-2 suggest that baculoviral systems may provide the best expression system for the expression and structural and functional characterization of heat sensitive, hydrophobic proteins.

12:15pm Lunch Technology Workshop (Sponsorship Available) or Lunch on Your Own 
(Contact Suzanne Carroll, scarroll@healthtech.com or 781-972-5452)

Protein Production

1:45 Chairperson’s Remarks

1:50 Baculovirus Mediated Protein Production: Overcoming the Challenges to Accelerate Drug Discovery
Ian Hunt, Ph.D., Associate Director, Protein Structure Group, Discovery Technologies, Novartis Institutes for BioMedical Research
For most biotech and pharmaceutical companies, protein production groups play a crucial role in the drug discovery process. Specifically, the recombinant proteins they generate contribute to several key stages of the drug discovery pathway. These include exploratory research, target validation, high-throughput screening (HTS), selectivity screens and structural biology studies. Therefore the quick and rapid production of high quality recombinant protein is a crucial component of many drug discovery campaigns. In this regard, baculovirus mediated insect cell expression has increasingly become one of the most popular vehicles for the production of large quantities of recombinant protein for structural and functional studies of therapeutically relevant bio-molecules. Moreover, in an effort to enhance the speed and throughput of the system and thus align it to the demands of the modern drug discovery environment, significant efforts have been made by many groups to streamline the process and enable faster delivery of protein. This presentation will therefore use a series of case studies from a number of different drug targets to illustrate the utility of BEVS (in the context of supplying proteins for structure based drug design) and also highlight some of the technologies Novartis has developed to expedite the throughput and efficiency of baculovirus directed protein expression. The presentation will also include discussion on some of the current bottlenecks within the process and potential new and enabling technologies that may assuage them.

2:25 From Automated Screening to Production: Streamlining Protein Production in the Baculovirus Expression System
Alycia Shoultz, Scientist IV, Head of Baculovirus Production, Department of Biologics and Biomolecular Sciences, Boehringer Ingelheim Pharma, Inc.
We have developed a two-pronged approach to protein production in the baculovirus expression system to address the challenges of both expression screening and biomass production. Initially, a reproducible and scaleable process was developed to minimize the time between plasmid delivery and biomass production. With this process, a construct can be screened for expression, a plaque purified viral stock can be created, and 5 to 10L’s of biomass can be generated within 3 weeks. Approximately 100L’s of biomass can be generated using the initial viral stock at a greater than 95% success rate in qualitatively predicting protein production levels. Recently, an automated and highly parallel screening method was developed to expand our capacity to screen large numbers of constructs for productivity. This presentation will describe both the methods, the results of these methods, and outlining the automation that was developed to streamline the baculovirus expression screening process.

2:55 Technology Spotlights (Sponsorship Available – Please contact Suzanne Carroll, scarroll@healthtech.com or 781-972-5452) 

3:25 Networking Refreshment Break in the Exhibit Hall

Protein Expression

4:00 Structure and Function of Vaccinia-Derived Proteins Expressed in Insect Larvae: Mouse Efficacy Studies and Covalent Analysis
George W. Buchman, Ph.D., Chief Scientific Officer, Protein Expression and Recovery Labs, Chesapeake PERL
Chesapeake PERL expresses proteins using recombinant baculoviral infection of insect larvae from the cabbage looper moth (Thermoplusia ni). The system represents a cost-effective and highly-scaleable alternative to insect cell culture, and possesses inherent advantages. We are developing a subunit vaccine for smallpox using the insect system in collaboration with grant partners at the University of Pennsylvania, and have previously reported on protein yield and immunogenicity. In the current work, we extend routine immunogenic analyses to include study of covalent structure, including patterns of subunit glycosylation. Additionally, a comprehensive study for protection afforded by the subunit vaccine against a vaccinia challenge in mice, and summary plans for a subsequent NHP protection study, are presented. Lastly, we will survey progress for other protein projects in process utilizing our novel platform.

4:30 A Fast and Multi-Parallel Approach for Small-Scale Expression Screening Using the BEVS System
Aline Tirat-Boeuf, Scientist, CPC / LFP / BCS, Novartis Institutes for BioMedical Research
A systematic screening of various expression conditions at a small-scale range will help to increase the chances of successful expression of proteins in insect cells with the BEVS system. We have therefore established a procedure allowing the cultivation of insect cells in a multi-well plate, lysis of the cells and purification of the recombinant protein on small-columns and analysis of the samples with gel electrophoresis. This set-up allows us to test in parallel different parameters such as cell type, multiplicity of infection, time of infection, etc., very rapidly and allows us to identify the optimal combination of parameters for an expression of recombinant protein at elevated levels. In this talk, we will present the procedure itself as well as some real examples underlining its usefulness.

5:00 Novel SUMO System to Enhance Expression of Proteins in Insect Cells
Li Liu, Ph.D., Senior Scientist, R&D, LifeSensors, Inc.
SUMO (small ubiquitin-related modifier) system was developed about five years ago and continues to gain prominence for difficult-to-express proteins in E. coli. However, no comparable system has been developed for eukaryotes, especially insect cells. Endogenous de-SUMOylases are abundant in insect and mammalian cells that remove the fusion tag and the ability of enhanced expression and affinity purification of protein is lost. A novel SUMO tag for insect cell system has been developed that is not cleavable in insect cells. We have selected diverse families of difficult-to-express proteins as examples to test the enhanced expression by the new tag called “SUMO Star.” The results indicated that SUMO Star tag enhanced protein expression levels 5-80 fold compared to wild type SUMO tag or non-tagged native protein. Biologically active protein production is dramatically enhanced with the attachment of SUMO Star tag. SUMO Star tag makes significant impact on quality and quantity of difficult-to-express proteins and especially those proteins that require native N-terminal for function and cannot be generated by other expression systems.

5:30 Reception in the Exhibit Hall

7:00 End of Day One 

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