Join the free sicentifc Biologics seminar. The seminar is free of charge and will take place at Bestuursgebouw at University of Utrecht
- Universiteit Utrecht, Bestuursgebouw – Room 0.33G Address: Heidelberglaan 8 3584 CS Utrecht.
- Date: Monday, October 2, 2017
- Time: 9:30 AM–11:30 AM (CEST: Amsterdam, Berlin, Stockholm)
Contact: Lindsay Mesure email@example.com
Join the complimentary scientific seminar at University of Utrecht on Monday 2 October 2017
The program will be presented by both a scientist from Promega Corporation and from Jannsen Vaccines & Prevention BV
Title: Assessing Fc-mediated effector function in infectious diseases.
Speaker: Dr. Börries Brandenburg, Associate Director, Janssen Vaccines & Prevention B.V., Archimedesweg 4-6, 2333 CN Leiden
Click here for Speaker’s bio
Interactions with receptors for the Fc region of IgG (FcγRs) have been shown to contribute to the in vivo protection against influenza A viruses provided by broadly neutralizing antibodies (bnAbs) that bind to the viral hemagglutinin (HA) stem. In particular, Fc-mediated antibody-dependent cellular cytotoxicity (ADCC) has been shown to contribute to protection by stem-binding bnAbs. Fc-mediated effector functions appear not to contribute to protection provided by strain-specific HA head-binding antibodies. We used a panel of anti-stem and anti-head influenza A and B monoclonal antibodies with identical human IgG1 Fc domains and investigated their ability to mediate ADCC-associated FcγRIIIa activation. Antibodies which do not interfere with sialic acid binding of HA can mediate FcγRIIIa activation. However, the FcγRIIIa activation was inhibited when a mutant HA, unable to bind sialic acids, was used. Antibodies which block sialic acid receptor interactions of HA interfered with FcγRIIIa activation. The inhibition of FcγRIIIa activation by HA head-binding and sialic acid receptor-blocking antibodies was confirmed in plasma samples of H5N1 vaccinated human subjects. Together, these results suggest that in addition to Fc-FcγR binding, interactions between HA and sialic acids on immune cells are required for optimal Fc-mediated effector functions by anti-HA antibodies.
Title: Bioluminescent bioassays power single or combination immunotherapy targeting two immune checkpoint receptors.
Speaker: Dr. Mei Cong, R&D Director, Promega Corporation, Madison, USA
Mei is a R&D Director at Promega Research leading a team of scientists in products and custom assay development. It includes Bioassays for biologics and Target Engagement for small molecules. In the last seven years Mei has been focusing on leading the development of reporter Bioassays useful for measuring activities of biologic drugs in immunotherapy. Dr. Mei Cong received her Ph.D. in Biochemistry from the University of Arizona. She completed her post-doctoral training on GPCR signal transduction pathway regulation with Dr. Robert Lefkowitz, 2012 Nobel Laureate in Chemistry at Duke University Medical Center. Prior to joining Promega, Mei spent over 20 years in pharma and biotech developing and delivering robust cell-based assays.
Therapeutic antibodies designed to target immune checkpoint receptors function by modulating a patient’s own immune system and are promising strategies to treat cancer. This can be achieved by directly stimulating T cell receptors or by engaging distinctive immune checkpoint pathways through signaling via immune co-stimulatory receptors (GITR, CD40, OX40, 4-1BB and HVEM) and inhibitory receptors (PD-1, CTLA-4, TIGIT, LAG3, Tim-3). Here I will describe a portfolio of cell-based bioassays for biologic development in immunotherapy Programs targeting co-stimulatory immune checkpoint receptors, inhibitory receptors (PD-1, CTLA-4, TIGIT, LAG3, Tim-3), or combination immunotherapy targeting two checkpoint receptors. These bioluminescent bioassays reflect the mechanism of action for each antibody drug candidate, and exhibit assay specificity, precision, accuracy, linearity and robustness required for drug potency and stability determination. They will empower current and future immunotherapy drug development.