GENETIC ENGINEERING NEWS WEBINAR
Wednesday April 29, 2009 1:00pm EDT - 2:30pm EDT

Epitope Mapping in Antibody Patenting

by Timothy J. Shea, Jr.,  Director,

Sterne, Kessler, Goldstein & Fox P.L.L.C.

 

A Comprehensive Epitope Mapping Strategy for Drug Development

by Jennifer F. Nemeth, PhD, Principal Research Scientist,

Discovery Mass Spectrometry,

Centocor Research and Discovery

 

Epitope Mapping of CAT-2200, A Fully Human Inhibitory Antibody to IL-17

by Mark Abbott, PhD, Principal Scientist,

AstraZeneca, Alderley Park, UK

 

Epitope Mapping by Amide Hydrogen/Deuterium Exchange Mass Spectrometry

by Yoshitomo Hamuro, PhD, Sr. Director of Technology Development,

ExSAR Corporation

 

1. How important is it to have the antibody paratope characterized,  that is, the residues on the antibody that bind the antigen for patent purposes?  (Shea)
2. What are the IP implications of having incorrect epitope information in your patent claims? (Shea)
3. Can epitope mapping data that is not in the patent application be brought into litigation at a later date? (Shea)
4. In the case of an antibody whose epitope sequence has been previously characterized, would further demonstrating a dependence on sequence modification, for example phosphorylation, provide sufficient grounds for a patent application? (Shea)
5. What is the limit of the epitope's size for a patent application? (Shea)
6. At what point in your development path do you seek epitope mapping information?(Nemeth & Abbott)
7. What is the benefit of multiple tests if crystallography has the highest resolution? (Nemeth)
8. How can you distinguish regions of epitope binding from regions of rapid conformational change that may be induced upon binding? (Nemeth)
9. What was the time-length to do these epitope mapping studies, and what bottlenecks did you experience during the process, and how does pharma address those bottlenecks when doing these studies? (Nemeth)
10. How can epitopes of dimers, for example receptors, be mapped? (Abbott)
11. How to distinguish epitope versus alosteric sites? What are the best practices? (Abbott)
12. Which methods are misleading in determining epitopes? Can you give one specific example and explain why? (Abbott)
13. What are the controls for the antibody pull down experiment? Are those peptides pulled down by a non specific mechanism? (Abbott)
14. What is the resolution of H/D Exchange epitope mapping? (Hamuro)
15. What is the applicability of H/D-Exchange mapping for difficult proteins such as glycosylated proteins, disulphide-bonded proteins and large proteins? (Hamuro)
16. What program or methodology did you use for docking? (Hamuro)

 

Sep 15 2006 (Vol. 26, No. 16)


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