|
Overview | Short
Courses | Day 1 (Joint Session) |
Day 2 | Day 3 | Download Brochure
7:30 am - 3:00 pm Conference Registration
7:30 Morning Coffee
THE NEXT GENERATION OF ANTIBODIES
8:15 Chairperson’s Remarks
Gregory P. Adams, Ph.D., Member, Fox Chase Cancer Center
|
Keynote Presentation
8:25 Novel Targets for Autoimmunity and Inflammatory Diseases Identified Using Viral Virulence Factors
Paul J. Carter, Ph.D., Chief Scientific Officer, Senior Vice
President, Research & Development, VLST, Inc.
Many viruses have evolved proteins known as “virulence factors” that down regulate the host immune response. Identification of the cellular targets of these virulence factors provides a way to streamline the development of novel therapeutics, including for autoimmunity and inflammatory diseases. A combined bioinformatic and proteomic platform has been developed and used to identify >130 putative virulence factors. The human cellular targets have been identified for >30 virulence factors including viral CD47 found in multiple pox viruses. The virulence factor therapeutic concept will be illustrated using preclinical data for a human CD47-Fc fusion protein. |
9:05 Chemical Expansion of Antibodies
Vaughn Smider, M.D., Ph.D., Assistant Professor, Molecular Biology, The Scripps Research Institute
Recently it has become possible to genetically engineer unnatural amino acids into protein sequences. We have developed antibody combinatorial libraries that contain 21 amino acids. These unnatural amino acids have unique chemical characteristics, which endows them with novel antigen binding properties. We have selected antibodies from the combinatorial libraries where the 21st amino acid is absolutely required for its antigen binding properties. These techniques allow for the creation of next generation antibodies with unique chemical properties and reactivity.
9:35 Beyond Edman Degradation: Automated de novo Protein Sequencing of Monoclonal Antibodies
Nuno Bandeira, Ph.D., Executive Director, Center for Computational Mass Spectrometry, University of California, San Diego
The characterization and engineering of monoclonal antibodies is usually preceded by time-consuming Edman/cDNA sequencing steps for determination of the heavy and light chain sequences – a low-throughput pipeline that does not address post-translational modifications. In a departure from these platforms, we have developed the Comparative Shotgun Protein Sequencing (CSPS) suite of algorithms – a mass spectrometry based protein sequencing approach resulting in over 95% sequence coverage and automatic discovery of unexpected post-translational modifications. In contrast with the current multiple-week duration of typical sequencing projects, CSPS delivers additional functionality while reducing the time required to sequence an antibody to under 72 hours, a dramatic reduction as compared to the average 2-4 months for classical Edman sequencing of an entire antibody. While we demonstrate CSPS on monoclonal antibodies, the underlying techniques are not antibody-specific and the results indicate that CSPS has the potential to be a disruptive technology for all protein sequencing applications.
10:05 Coffee Break in the Exhibit Hall
11:00 Highly Diversified Human Antibody Libraries and Innovative Tools for Antibody Optimization and Selection
Philippe Mondon, Ph.D., Director, Antibody Engineering and Directed Molecular Evolution, MilleGen SA
Random introduction of variability in the entire variable domains of antibodies has been used to optimize selected antibodies from human libraries. However, the mutagenesis processes used were unnatural and induced modifications able to change the nature of the antibody and increase the risk of immunogenicity. To overcome this drawback, we have generated a library from in vivo rearranged V-genes from non-immunized donors and also from a naturally oriented population of antibodies against several pathologies. Furthermore, we further increased the complexity through a random mutation technology (MutaGen) mimicking the in vivo process responsible for the antibody maturation. We used the natural human polymerases known as mutases in vitro, due to their low fidelity, to replicate the entire variable domain of large V-genes repertoires. Thus we made hyperdiversified human antibody fragment libraries and set up a platform to engineer the selected antibodies.
11:30 rPEG-Fusion to Improve Half-life and Safety of Protein Therapeutics
Volker Schellenberger, Ph.D., Vice President, Drug Discovery, Amunix
rPEGs are recombinant protein chains with PEG-like properties. rPEGs can be fused to protein therapeutics, which eliminates the need for chemical PEG conjugation. Similar to PEG, rPEGs result in improved biological half-life and reduced immunogenicity. Due to their protein nature rPEGs are fully biodegradable, which eliminates safety risks associated with non-degradable PEG. The hydrophilic nature of rPEG improves folding of most fusion partners, which simplifies production, purification, and drug formulation.
12:00 pm Close of Morning Session
12:15 Luncheon Workshop (Sponsorship Available)
or Lunch on your Own
APPLYING ANTIBODIES TO NOVEL PROBLEMS
1:45 Chairperson’s Remarks
Volker Schellenberger, Ph.D., Vice President, Drug Discovery, Amunix
1:50 Bispecific Antibody Engineering for Oncology and Automimmunity
Robert Mabry, Ph.D., Senior Scientist, Antibody Discovery and Assay Technology, ZymoGenetics, Inc.
While engineered bispecific antibodies (bsAbs) have been reported for over a decade, difficulties with manufacturing have reduced the momentum of such constructs and remain a significant obstacle in the use of bsAbs as potential therapeutics. Several challenges for bsAb engineering include: retention of affinity and stability comparable to the parent mAb/antibody fragment, ability to bind both targets simultaneously, host expression, and serum persistence. Here, we present stable antibody fragments assembled in several Fc fusion formats for bispecificity that potentially overcome these obstacles and exhibit stability and pharmacokinetics similar to therapeutic mAbs.
2:20 Broadly Neutralizing Antibodies to Highly Variable Viruses
Mansun Law, Ph.D., Department of Immunology and Microbial Science, The Scripps Research Institute
An important consideration in the development of anti-viral antibodies is that the antibodies should be active against different circulating virus strains. Broadly neutralizing antibodies are favorable candidates in antibody development because they target relatively conserved epitopes and cross-neutralize multiple viral strains. The strategies of the discovery and characterization of these uncommon antibodies will be discussed.
2:50 Developing Anti-Mullerian Inhibiting Substance Type II Receptor Antibodies for Ovarian Cancer Therapy
Gregory P. Adams, Ph.D., Member, Department of Medical Oncology, Fox Chase Cancer Center
The Mullerian Inhibiting Substance Type II Receptor (MISIIR) presents a promising new target for the immunotherapy of ovarian cancer. In adult females MISIIR expression is limited to a few tissues including the ovarian surface epithelium and MISIIR is expressed in a large percentage of ovarian tumors. Our work in the development and characterization of anti-MISIIR antibodies will be presented.
|
3:20 Sponsored by |
|
|
|
3:35 Refreshment Break in the Exhibit Hall
4:30 Epitope Specific Effects of AMG 479 and Other IGF-1R Antibodies
Frank Calzone, Ph.D., Executive Scientific Director, Oncology Research, Amgen
AMG 479 is a fully human antibody under clinical evaluation as an IGF-1R targeted inhibitor for cancer. The preclinical analysis of AMG 479 and other IGF-1R antibodies has revealed epitope specific differences in the mechanisms of receptor inhibition that will be discussed.
5:00 Phylomer Libraries: A Rich Source of Bioactive Peptides for Blocking Targets Inside and
Outside of Cell
Paul Watt, Ph.D., Vice President, Drug Discovery, Phylogica Ltd., Adjunct Associate Professor, University of Western Australia
Phylomers are a new class of peptides derived from highly biodiverse genomic fragments of bacterial genomes. Typically Phylomers range between 15 and 40 amino acids in size, sufficient to encode super-secondary structures and/or folds. Synthetic Phylomers fused to a protein transduction domain, have been shown to have biological activity against intracellular targets in ex vivo and in vivo assays. Screening against CD40 ligand, an extracellular target with a key role in inflammation, has yielded functional Phylomer peptides, which have been subjected to a variety of affinity maturation approaches to further improve specificity and potency. Phylomer libraries in parallel formats are also being explored as a source of rapid leads for diagnostics as well as target discovery/validation.
5:30 T Cell Engaging BiTE Antibodies: Clinical PoC and Recent Developments
Tobias Raum, Ph.D., Senior Director Lead Discovery, Immunotherapy, Micromet AG
BiTE antibody technology is based on single chain bispecific antibody molecules, binding to CD3 on cytotoxic T cells and a surface antigen on a target cell, such as a cancer cell. This close cell contact leads to the efficient killing of the target cell. The first BiTE antibody directed against CD19 on NHL cancer cells has proven efficacy in a clinical phase I trial. Results will be discussed. An advanced new BiTE platform was recently developed and will be presented.
6:00 Reception in the Exhibit Hall
7:00 Close of Day
Overview | Short
Courses | Day 1 (Joint Session) |
Day 2 | Day 3 | Download Brochure
For more information, please contact:
Mary Ann Brown, Sr. Conference Director
Phone: 781-972-5497
E-mail: mabrown@healthtech.com
For exhibit and sponsorship information, please contact:
Suzanne Carroll, Manager-Business
Development
Phone: 781-972-5452
E-mail: scarroll@healthtech.com
|
