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7:30am Morning Coffee

Useful Methods and Technology to Support Your Expression System

8:25 Chairperson’s Remarks 

8:30 Processing, Maturation and Activation of Recombinant Zymogens by a Novel Insect Cell Line Stably Transfected with a Human Pro-Protein Convertase
Carettoni Daniele, Ph.D., Head, Biochemistry, Axxam
Site-specific proteolytic processing is a key event in physiological and recombinant expression of a large number of enzymes and bioactive peptides, including proteases, hormones and neuropeptides. To achieve their functional state, the pro-domain of these proteins needs to be precisely cleaved at the proper activation site in the proper cell compartment. In eukaryotic cells, the conserved family of pro-protein convertases accomplish this role for the vast majority of the pro-proteins targeted to the secretory pathway. However, the endogenous set of pro-protein convertases usually fails to support the complete activation of heterologous pro-proteins produced at high levels in insect cells. To address this problem, we have engineered an insect cell line to stably express a human pro-protein convertase. This novel insect cell line was selected by using a functional assay based on the ability to promote the activation of an inactive protease precursor. The final clone displayed the ability to process almost to completion a wide range of physiological substrates, including recombinantly expressed human serine proteases, metalloproteases and lipases. The increased processing of the secreted proteins directly correlated with the increased catalytic activity of the enzymes. The stably transfected cells have been successfully cultured under different conditions, ranging from miniaturized plate format to mid production scale. 

9:00 Technology Spotlight 
(Sponsorship Available – Please contact Suzanne Carroll, or 781-972-5452) 

9:15 Process Development and Scale-up Biomanufacturing of the Recombinant Parvovirus B19 Virus-Like-Particle Vaccine in BEVS for Phase I/II Clinical Trials
Victor Van Cleave, Ph.D., Vice President, Research & Development, Meridian Life Science, Inc.
Meridian Life Science, Inc. recently completed manufacture of a clinical grade recombinant human Parvovirus B19 (HPVB19) Vaccine using BEVS for the National Institutes of Health (NIH) for use in a recently initiated Phase I safety study. The vaccine consists of two viral proteins (VP1 and VP2) in separate baculovirus vectors that are co-infected at the correct MOIs into Spodoptera frugiperda (Sf9) cells and that, upon expression, self assemble in the appropriate ratio into immunogenic virus-like particles. Future clinical studies will require a more economical production process, thus this presentation will review our previous experiences and address the additional process development studies that are required to improve yields, optimize culture conditions, and scale-up biomanufacturing. Results of the recently initiated phase I clinical study will also be presented if available at the time of the presentation.

9:45 Rapid Baculovirus Titre by Capillary Electrophoresis and Label Free Intrinsic Imaging 
Stuart Hassard, Ph.D., Head Biologist, deltaDOT Ltd.
Viral Titre is an essential part of Baculovirus expression and yet has seen few technological advances since its inception in the early 1980’s. Standard techniques of plaque forming unit assays are benchmark virological practice and have inherent time and cost penalties. Immunological techniques and PCR-based assays have ameliorated the time issue to some extent, but exacerbated the assay costs, particularly of consumables. The Peregrine benchtop HPCE analyzer provides fast, high quality, label-free separations of proteins, glycoproteins, peptides, nucleic acids, bacteria, virus and small molecules. Based on a single-channel capillary system, the Peregrine provides superior resolution, sensitivity and reproducibility compared to existing HPCE systems. deltaDOT’s proprietary Label Free Intrinsic Imaging™ (LFII™) technology is a novel and powerful technique that enables the detection of molecules without the use of labels, dyes, stains or radioactivity. The same instrument can be used throughout the expression procedure, analysing viral titre, protein expression in culture, protein purification and final QA/QC of post translationally modified product.

10:15 Networking Coffee Break

Vaccines & Immunotherapies

10:55 Chairperson’s Remarks

11:00 Utility of the Insect Cell Culture System for the Development of an Active Immunotherapeutic; A Case Study 
Daniel P. Gold, Ph.D., Chief Scientific Officer, Favrille, Inc.
Pioneering academic studies utilizing patient specific idiotype immunotherapy to treat B-cell non-Hodgkin’s lymphoma offers a potential new treatment paradigm for patients with this disease. However, time and cost constraints for producing this therapy have prevented its commercial development. Our presentation will focus on the features of baculovirus and insect cell culture that make this manufacturing method optimal from a product quality and cost perspective for the timely delivery of these personalized therapies.

11:30 Production of a Novel Influenza Vaccine Using Insect Cells 
Penny L. Post, Ph.D., Director, Quality Control, Protein Sciences Corporation
Approximately 5 – 20% of the US population is infected with influenza annually, where > 200,000 are hospitalized from complications and 36,000 die from flu each year. Influenza is the 6th leading cause of death among US adults. Licensed vaccines can be as little as 30% effective in preventing hospitalizations in the elderly and immunocompromised and as little as 70% effective in preventing the flu in healthy adults < 65.1 All influenza vaccines licensed in the United States are made in embryonated eggs. Protein Sciences Corporation has used the baculovirus expression vector system (BEVS) to produce a novel influenza vaccine using insect cells. The BEVS technology provides advantages of speed, cost, and safety. When used to produce an influenza vaccine, the composition of which changes annually, additional advantages include: rapid response to emerging strains, elimination of the need to handle live viruses (especially for pandemic influenza), and production of authentic antigen that does not require egg-adaptation. A recent field trial showed the PSC vaccine to be at least as effective as the licensed vaccine. This talk will describe the technology used to produce this vaccine, the clinical trial data obtained, and regulatory considerations, including our path to product licensure. 1Source: CDC web site and

12:00pm Development of a Low-Cost, Insect Larvae-Derived Recombinant Subunit Vaccine Against RHDV
Silvia Gómez-Sebastián, Ph.D., I+D+I, Algenex S.L- INIA
Vaccine antigens against rabbit hemorrhagic disease virus (RHDV) are currently derived from inactivated RHDV obtained from livers of experimentally infected rabbits. Several RHDV-derived recombinant immunogens have been reported. However, their application in vaccines has been restricted due to their high production costs. In this talk we describe the development of an inexpensive, safe, stable vaccine antigen for RHDV. The potential costs of an RHDV vaccine made using this technology would be reduced ~477 times vs. the same protein produced in insect cells maintained by fermentation. In conclusion, the larva expression system may provide a broad-based strategy for production of recombinant subunit antigens (insectigens) for human or animal medicines, especially when production costs constrain their use.

12:30 End of the Baculovirus Technology Conference


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