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Immediately following MOLECULAR DISPLAY: THE CHEMISTRY SET FOR PROTEINS AND SMALL MOLECULES
Corporate Sponsor:
Sponsoring Publications:
Drug Discovery and Development
Expert Opinion on Biological Therapy
Genomics and Proteomics
Human Antibodies
Journal of Molecular Biology
Pharmacogenomics
PharmaVOICE
CHI's Prospects for Commercialization of Human Monoclonal Antibodies
CHI's Proteomics Survey 2003Web Partner:
GenomicsProteomics.com
The Antibody Resource PageThe pipeline of therapeutic antibodies has been growing steadily, building on successful clinical trials, particularly in cancer. This growth will certainly accelerate, as genomic companies with many novel targets seek to employ antibodies to modulate these targets. In addition, studies employing antibodies, or antibody mimics, are being ramped up as part of the explosive growth of proteomics. All of these trends place a tremendous emphasis on the development of new approaches for faster antibody development, improved methods of selection and optimization, alternatives for production, and evaluation for novel applications. This conference will provide you with key updates on important developments in each of these areas.
Scientific Advisors
Dr. Andrew Bradbury, Los Alamos National Laboratories
Dr. Hennie R. Hoogenboom, BioQuest BV and University of Liège (Belgium)
Dr. Peter J. Hudson, CSIRO Health Sciences and Nutrition (Australia)Speakers
Dr. Yevgenya Akselband, One Cell Systems, Inc.
Dr. Michael Bardroff, MorphoSys AG (Germany)
Dr. Itai Benhar, Tel-Aviv University (Israel)
Dr. Laird Bloom, Phylos, Inc.
Dr. Andrew Bradbury, Los Alamos National Laboratories
Dr. Frank Carr, Biovation (UK)
Dr. Mark de Souza, Director of Corporate Development, Dyax Corp.
Dr. Chaitanya Divgi, Weill Medical College of Cornell University and Memorial Sloan-Kettering Cancer Center
Dr. Dominik Escher, CEO ESBATech AG (Switzerland)
Dr. Michael Feldhaus, Pacific Northwest National Laboratories
Dr. Robert Hayes, Xencor
Dr. Peter J. Hudson, CSIRO Health Science and Nutrition (Australia)
Dr. Laurent Jespers, MRC-Laboratory of Molecular Biology (UK)
Dr. Angray Kang, Avanir Pharmaceuticals
Dr. Robert J. Kreitman, National Cancer Institute, National Institutes of Health
Dr. James D. Marks, University of California, San Francisco
Dr. Ralph Minter, Cambridge Antibody Technology (UK)
Dr. Michael C. Mullenix, Molecular Staging Inc.
Dr. Corinne Olesen, Applied Biosystems
Dr. John W. Park, University of California, San Francisco
Dr. Franck Perez, Institut Curie (France)
Dr. Emanuel F. Petricoin III, U.S. Food and Drug Administration
Dr. Herald Reiersen, Affitech AS (Norway)
Dr. Yoram Reiter, Technion-Israel Institute of Technology
Dr. Peter Senter, Seattle Genetics
Dr. Jackie Sharon, Boston University School of Medicine
Preconference Tutorial
Comparison of Display Technologies for Making
Therapeutic Antibodies
Tuesday, May, 15 - 5:30 pm - 8:30 pmTechnologies for Antibody Selection
An Array-Based System for High-Throughput Binding Kinetics Analysis by Surface Plasmon Resonance: Application to Hybridoma Screening
Covalent Antibody Display by a P2 Phage Replication Protein
Generation of Antibody Therapeutics by Phage and Ribosome Display
Human Fab Antibody Isolation and Rapid Affinity Maturation Using an Integrated Phage and Yeast Display Platform
Naïve Yeast Display Libraries
Rapid Cell Line Enrichment for High Secretors and Rare CellsAntibody Engineering and Optimization
Predicting and Overcoming Immunogenicity via T Cell Epitopes
Rational Engineering of Monoclonal Antibodies
A General Solution for Stable Cytoplasmic Intrabodies
Recombinant Polyclonal Antibody Libraries to Human Colorectal Cancer
Human Recombinant Antibodies with MHC-Restricted T Cell Receptor-like Specificity
The Biophysical Properties of Fully Human Domain AntibodiesBeyond Antibodies
Fluorobodies: Binding Ligands with Intrinsic Fluorescence
Structural Design of High-Affinity Antibody-like Domains
TRINECTIN™ Antibody MimicsAntibodies in Proteomics and Target Discovery
Use of Reverse-Phase Protein Arrays for Signal Pathway Profiling
Rolling Circle Amplification in Proteomic Applications with Ultrasensitive Multiplex Immunoassays
"Immunization" with Subcellular Compartments and Use of Scfvs as Protein Conformation Sensors in Living CellsTherapeutic Applications of Antibodies and Antibody Fragments
Radioimmunotherapy (RIT): Current Status and Future Prospects
Recombinant Immunotoxins for the Treatment of Hematologic Malignancies
Immunoliposomes Targeted Using scFvs
Development of Potent and Highly Effective Monoclonal Antibody-Auristatin Conjugates for Cancer Therapy
HuCAL® Antibodies: Designed as Therapeutics
Tuesday, May 13
5:00-6:30pm Early Registration and Poster and Exhibit Setup
5:30-8:30 Preconference Tutorial (includes light dinner)
Comparison of Display Technologies for Making Therapeutic Antibodies
Dr. James D. Marks, University of California, San Francisco
A number of competing display technologies have been developed for generating and evolving therapeutic antibodies. Using antibodies to the bioterror agent botulinum neurotoxin, we have studied and compared phage vs. yeast display for both generations of lead antibodies from immune libraries as well as for evolution of antibody affinity. Here we describe the differences we have observed with respect to (1) expression host bias, (2) antibody diversity, (3) antibody affinity, (4) expression levels, and (5) ease of manipulation. Conclusions will be presented as to when each system is best employed.
7:00am Registration, Poster and Exhibit Viewing, and Light Continental Breakfast
Technologies for Antibody Selection
8:00 Welcome by Session Chairperson
Dr. Andrew Bradbury, Staff Scientist, Life Sciences Division, Los Alamos National Laboratories8:15 Selection of Highly Stable Human scFvs for Library Construction and Screening
Dr. Dominik Escher, CEO ESBATech AG (Switzerland)
We have employed the stringent intracellular conditions, under which no disulfide bridges are formed, to select for the most stable human scFv frameworks. Through an initial antigen-independent selection procedure, we have selected from the whole pool of more than 1.5 million possible human scFv VH and VL fragments, those, which have a very high intracellular stability and solubility. These selected human scFv frameworks are functional under reducing intracellular conditions. Furthermore, we observe that these selected human VH and VL fragments show increased stability and better expression properties compared to conventional scFvs also under natural, oxidizing conditions. In addition, due to the analysis of our selected, stable human scFvs, a targeted rational approach for optimizing stability and expression of an existing scFv is possible. A detailed characterization and comparison to the consensus sequences of the different VH and VL families of our selected human scFvs will be presented.8:45 A High Throughput System for Binding Kinetics Analysis by Surface Plasmon Resonance: Application to Monoclonal Antibody Characterization
Dr. Corinne Olesen, Sr. Manager, Scientists, Cell Biology & Functional Proteomics, Applied Biosystems
Applied Biosystems has developed a new platform that uses Grating-Coupled Surface Plasmon Resonance technology (GC-SPR) for measurement of real-time binding kinetics between unlabeled analytes and biomolecules immobilized on a biosensor chip. In contrast to other SPR detection platforms, GC-SPR provides an optical design that allows simultaneous real-time kinetic analysis of multiple samples spotted on a gold chip. We describe the application of GC-SPR for the simultaneous characterization of monoclonal antibodies immobilized on a gold biosensor chip. This approach enables measurement of the binding constants of hundreds of monoclonals in a single experiment. In a similar manner, various surface immobilization chemistries are used for applications such as protein-protein interactions, nucleic acid-protein interactions, and epitope mapping. By combining parallel screening with binding kinetics, this system can improve the workflow and productivity of laboratories performing affinity screening and high throughput binding characterization studies.9:15 Covalent Antibody Display by a P2 Phage Replication Protein
Dr. Herald Reiersen, Senior Scientist, Affitech AS
We have demonstrated a new in vitro display tool for antibody fragments. Fusion proteins of the P2 phage DNA replication protein P2A with scFv antibodies have been made, and linear DNA of the scFv-P2A constructs were processed in an in vitro coupled transcription-translation mix of E. coli S30 lysate. Complexes of scFv-P2A covalently bound its own DNA were isolated after panning on antigen-coated solid phase, and the enriched DNA were amplified by PCR and applied in the next cycles of panning.9:45 Generation of Antibody Therapeutics by Phage and Ribosome Display
Dr. Ralph Minter, Senior Research Scientist, Cambridge Antibody Technology
Both phage display and ribosome display systems can be used effectively to isolate large numbers of sequence-diverse antibodies from naïve libraries. Once leads have been identified the same display technologies can be used to optimize the drug candidates to the in vitro characteristics leading to the desired efficacy in vivo. Using case studies we will demonstrate the integration of display-based selections, high-throughput screening, and secondary cell-based assays to generate therapeutic antibodies. We will also use examples to highlight the advantages specific to the different types of display system for both antibody isolation and optimization. Finally, examples of antibodies generated to "difficult" targets will be presented.10:15 Poster and Exhibit Viewing, Refreshment Break
10:45 Human Fab Antibody Isolation and Rapid Affinity Maturation Using an Integrated Phage and Yeast Display Platform
Dr. Mark de Souza, Director of Corporate Development, Dyax Corp.
Dyax uses an integrated antibody discovery platform for the rapid selection, screening, affinity maturation, and IgG reformatting of target-specific human Fab antibodies. This antibody discovery pipeline is complemented by yeast display technology whereby lead Fab antibodies can be rapidly and efficiently affinity matured. The modular design of our phage-displayed human Fab libraries facilitates affinity maturation by novel yeast display procedures based on the combinatorial shuffling of antibody gene fragments. Examples will be given of the utility of this platform.11:15 Naïve Yeast Display Libraries
Dr. Michael Feldhaus, Pacific Northwest National Laboratories
A nonimmune library of 109 human antibody scFv fragments has been cloned and expressed on the surface of yeast, and nanomolar-affinity scFvs routinely obtained by magnetic bead screening and flow cytometric sorting. The yeast library can be amplified 1010-fold without measurable loss of clonal diversity, enabling effectively indefinite expansion of the library. The expression, stability, and antigen binding properties of more than 50 isolated scFv clones were assessed directly on the yeast cell surface by immunofluorescent labeling and flow cytometry, obviating separate subcloning, expression, and purification steps and thereby expediting the isolation of novel affinity reagents. The ability to use multiplex library screening demonstrates the utility of this approach for high throughput antibody isolation for proteomics applications.11:45 Rapid Cell Line Enrichment for High Secretors and Rare Cells
Dr. Yevgenya Akselband, Senior Scientist, One Cell Systems, Inc.
The process of selecting and expanding transfected cells and hybridomas using limited dilution cloning is time consuming and labor intensive. We have developed a method for rapidly enriching a cell population for high secretors or rare cells. The Gel Microdrop Secretion Assay permits isolation of individual cells based on level of secreted protein, antigen specificity, isotype, surface marker, or multiple parameters simultaneously. Using FACS, large cell libraries can be screened and recovered for cloning in days instead of weeks or months. Typically, 3 x 106 cells can be screened in less than one hour and subpopulations as small as 0.1% can be recovered for scale-up or gene cloning.12:15 Interactive Panel Discussion with Questions from Audience for Morning Speakers
Antibody Engineering and Optimization
1:45 Comments by Session Chairperson
Dr. Andrew Bradbury2:00 Predicting and Overcoming Immunogenicity via
T Cell Epitopes
Dr. Frank Carr, President and Chief Scientific Officer, Biovation
In the world of protein/peptide vaccination, the importance of helper T cell epitopes in mounting a sustainable immune response to a protein has been recognized. The "DeImmunisation™" approach presented in this talk is the converse of vaccination whereby helper T cell epitopes are removed from proteins to reduce immunogenicity. Such reduction of immunogenicity can be demonstrated both in mouse and human systems. The presentation will address prediction of immunogenicity in antibodies and overcoming of such immunogenicity via T cell epitope removal. Several examples will be considered including a phase I/II clinical stage DeImmunisation™-modified antibody for prostate cancer.2:30 Rational Engineering of Monoclonal Antibodies
Dr. Robert Hayes, Director of Antibody Engineering, Xencor
We have designed and implemented a platform to reengineer biochemical and cell biological characteristics of monoclonal antibodies using PDA™, a set of computational and experimental tools that allows the rational manipulation of protein sequences to incorporate desired characteristics without altering the overall structure. In silico library generation finds protein sequences that are completely novel by screening the full diversity of protein sequence space, while selecting for those variants that are likely to be folded and active, a task not possible for purely experimental protein libraries developed using random mutagenesis or molecular evolution. This platform allows us to efficiently engineer new characteristics of antibodies including improvement of immunoglobulin structural stability, modulation of relative affinity for Fc receptors, enhancement of affinity and specificity, and improvement of pharmacodynamic properties.3:00 A General Solution for Stable Cytoplasmic Intrabodies
Dr. Itai Benhar, Department of Molecular Microbiology and Biotechnology, The George S. Wise Faculty of Life Sciences, Tel-Aviv University
We present an approach that allows the expression of any scFv as a cytoplasmic intrabody. Our approach is based on fusion technology, where the scFvs are expressed as C-terminal fusions with the Escherichia coli maltose binding protein (MBP). MBP was recently shown to act as a "chaperone in context of a fusion protein." We show that as a production system MBP-scFvs are produced at efficiency that probably exceeds all known scFv production systems. We further demonstrate that MBP-scFvs are more stable than the corresponding unfused scFvs and that they perform more efficiently as cytoplasmic intrabodies in both bacteria and transfected mammalian cells.3:30 Poster and Exhibit Viewing, Refreshment Break
4:00 Recombinant Polyclonal Antibody Libraries to Human Colorectal Cancer
Dr. Jackie Sharon, Professor of Pathology and Laboratory Medicine, Boston University School of Medicine
We have developed a system for PCAL generation and have selected diverse Fab phage display libraries with a high percentage of clones reactive to human colorectal cancer cell lines. Analysis of library clones showed that more than 80% of clones express IgG-and of those about 80% are reactive with colorectal cancer cells-and that the libraries are still polyclonal. The efficacy of the polyclonal IgG antibody libraries is being evaluated in a nude mouse-human colorectal cancer xenograft model, by comparison to the clinically used anti-colorectal cancer monoclonal antibody 17-1A.4:30 Human Recombinant Antibodies with MHC-Restricted T Cell Receptor-like Specificity: Recognition of Distinct T Cell Epitopes Derived from a Variety of Tumor Associated Antigens
Dr. Yoram Reiter, Faculty of Biology, Technion-Israel Institute of Technology
We demonstrate, for the first time, the ability to isolate high-affinity human recombinant antibodies with the antigen-specific, MHC-restricted specificity of T cells. The selected human TCR-like Fabs may prove to be very useful for monitoring and visualizing the expression of specific MHC-peptide complexes on the surface of tumor cells, antigen-presenting cells, and lymphoid tissues, as well as for developing a new family of targeting agents for immunotherapy.5:00 The Biophysical Properties of Fully Human Domain Antibodies
Dr. Laurent Jespers, Senior Scientist, MRC-Laboratory of Molecular Biology (UK)
The small size of domain antibodies (dAbs) offers a commercial alternative to monoclonal antibodies for tissue penetration, binding to target pockets, formatting, and manufacturing costs. Here, we report the construction of a large synthetic library of dAbs based on a single human VH scaffold. Detailed biophysical analysis of several clones reveals that these dAbs have stability and solubility characteristics that allow them to be expressed at high levels as recombinant proteins and purified to high concentrations as well-behaved monomeric molecules. These results offer the promise for nonimmunogenic therapy by fully human dAbs.5:30 Interactive Panel Discussion with Questions from Audience for Afternoon Speakers
6:00 Close of Conference Day One
Thursday, May 15
8:00am Poster and Exhibit Viewing and Light Continental Breakfast
Beyond Antibodies
8:30 Comments by Session Chairperson
Dr. Hennie R. Hoogenboom, BioQuest BV and University of Liège8:45 Fluorobodies: Binding Ligands with Intrinsic Fluorescence
Dr. Andrew Bradbury
We have created a library of intrinsically fluorescent binding ligands by inserting antibody-binding loops into a highly stable form of GFP. Binders against a number of different targets , with affinities comparable to those of antibodies, have been selected from this library. Fluorobodies are extremely stable and express very well. Recent results will be described.9:15 Structural Design of High-Affinity, Antibody-like Domains
Dr. Peter J. Hudson, Scientific Director, Biomolecular Engineering Division, CSIRO Health Science and Nutrition
We have constructed display libraries of novel V-like domains to complement the current range of natural and synthetic antibody repertoires. These V-domains form efficient scaffolds for the presentation and selection of constrained polypeptides displayed as long surface loop structures. Importantly, V-domains can penetrate clefts in the antigen (enzymes, viral capsids, and cell-surface receptors) and therefore target both refractory antigens and immunosilent cavities.9:45 TRINECTIN™ Antibody Mimics: High-Affinity Binding Proteins Generated through in Vitro Evolution Technology
Dr. Laird Bloom, Group Leader, Cell Biology, Phylos, Inc.
We have selected antibody mimics against targets of interest using RNA display, an in vitro method that uses the covalent fusion between a protein and the mRNA that encodes that protein. The TRINECTIN™ antibody mimic scaffold is based on the tenth human fibronectin type III domain, a highly stable 10 kDa protein in which we have randomized residues in three solvent-accessible loops. We will show examples of selected proteins that bind to targets with nano- to picomolar affinities and that inhibit ligand-receptor interactions.10:15 Poster and Exhibit Viewing, Refreshment Break
Antibodies in Proteomics and Target Discovery10:45 Comments by Session Chairperson
Dr. Hennie R. Hoogenboom10:50 Use of Reverse Phase Protein Arrays for Signal Pathway Profiling
Dr. Emanuel F. Petricoin III, Co-Director, Clinical Proteomics Program, Center for Biologics Evaluation and Research, U.S. Food and Drug Administration
Cellular signaling events drive and underpin all biologic processes. The deregulation of the circuitry of the cell is most often responsible for human disease. Past attempts at elucidating the signaling network relied on "inferentialomics" from gene array data. As protein modifications such as phosphorylation cannot be accurately assessed using gene transcription proofing, we have developed a new type of protein array that can employ laser capture microdissected cells for multiplexed phosphorylation fingerprinting. Now dozens and dozens of specific signaling events can be monitored simultaneously from only a few thousand cells procured from human biopsy specimens. We use these new types of arrays in NCI clinical trials employing molecular targeted therapeutics towards the goal of patient-tailored therapy.11:20 Use of Rolling Circle Amplification in Proteomic Applications with Ultrasensitive Multiplex Immunoassays
Dr. Michael C. Mullenix, Section Head, Immunodiagnostics, Molecular Staging Inc.
Rolling circle amplification (RCA) enabled the development of a 180-feature microarray cytokine immunoassay. Thirty-seven percent of the features had a sensitivity of £ 10 pg/mL, 38% of the features had sensitivity of £ 100 pg/mL, 20% of the features had a sensitivity of £ 1000 pg/ml, and 5% of the features had a sensitivity of £ 1000 pg/mL. The sensitivity achieved is appropriate for measurement of biologically relevant changes in cytokine levels in serum, plasma, and culture supernatants. RCA also improved sensitivity in commercially available cytometric bead format immunoassays. The fold increase in sensitivity observed averaged ~30-fold and ranged from 2- to 100-fold while maintaining specificity in multiplex assays developed using Luminex xMAP™ technology.11:50 The Recombinant Antibody Approach in Cell Biology: "Immunization" with Subcellular Compartments and Use of Scfvs as Protein Conformation Sensors in Living Cells
Dr. Franck Perez, Institut Curie
We show that recombinant antibodies can be selected by antibody phage display using a complex mixture of proteins, corresponding to a subcellular compartment, as a target. We screened against microtubule-associated proteins and against intact Golgi complex and obtain specific antibodies in each case. We then expressed an anti-Golgi recombinant antibody as a GFP-tagged molecule in living. This allowed us to track in real time the behavior of the endogenous protein. Finally, we obtained recombinant antibodies specific for the GTP-bound conformation of a small GTPase. These antibodies can be used to detect the activated form of the small GTPase by immunofluorescence, by pull-down experiment or even in living cells after expression of the GFP-tagged antibody. In conclusion, our data suggest that recombinant antibodies can be used as conformation, and this would be particularly valuable to detect proteins locked in a pathological conformation.
Therapeutic Applications of Antibodies and Antibody Fragments
1:15 Comments by Session Chairperson
Dr. Peter J. Hudson1:20 Radioimmunotherapy (RIT): Current Status and Future Prospects
Dr. Chaitanya Divgi, Professor and Member, Weill Medical College of Cornell University; and Memorial Sloan-Kettering Cancer Center
The recent FDA approval of yttrium-90 labeled intact immunoglobulin against the CD20 antigen for the treatment of B-cell lymphoma underscores the potential of radiolabeled antigen-binding constructs in the treatment of cancer. This presentation will review the status and potential of cytotoxic radionuclides and antigen-binding constructs with potential in RIT and outline the directions of such therapy in solid and hematologic neoplasms. The clinical research being carried out at Memorial Sloan-Kettering Cancer Center will primarily be presented, along with the significant work carried out elsewhere.1:50 Recombinant Immunotoxins for the Treatment of Hematologic Malignancies
Dr. Robert J. Kreitman, Chief, Clinical Immunotherapy Section, Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health
Recombinant immunotoxins targeting CD25 and CD22 have been administered to patients with leukemia, and dramatic major responses have been achieved. These immunotoxins are 63 kDa in size and contain the Fv fragment of a monoclonal antibody genetically fused to a truncated form of Pseudomonas exotoxin. BL22-targeting CD22 is the first agent that produces complete remissions in the majority of patients with chemotherapy-resistant hairy cell leukemia and is being developed for other leukemias as well.2:20 Immunoliposomes Targeted Using scFvs
Dr. John W. Park, Comprehensive Cancer Center, University of California, San Francisco
Summary unavailable at time of printing.2:50 Refreshment Break
3:10 Development of Potent and Highly Effective Monoclonal Antibody-Auristatin Conjugates for Cancer Therapy
Dr. Peter Senter, Vice President, Seattle Genetics
A series of novel antimitotic drugs in the auristatin E (AE) family were synthesized for targeted delivery to tumors using monoclonal antibodies (mAbs) against membrane antigens preferentially expressed on tumor cells. AE was linked to chimeric mAbs forming acid-labile and protease-sensitive conjugates that could be cleaved under conditions found within the lysosomes of target cells. In vitro cytotoxicity assays and plasma stability studies indicated that the protease-sensitive conjugates were highly active, stable, and immunologically specific. The peptide-linked conjugates were less toxic in vivo than the hydrazones. The mAb-peptide-AE conjugates induced cures and regressions of established anaplastic large-cell lymphoma and breast carcinoma xenografts at 1/30 to 1/10 the MTD, respectively. These new conjugates illustrate the importance of linker technology, drug potency, and conjugation methodology in developing safe and efficacious mAb-drug conjugates for cancer therapy.3:40 HuCAL® Antibodies: Designed as Therapeutics
Dr. Michael Bardroff, Senior Scientist, Antibody Research Department, MorphoSys AG
MorphoSys's Human Combinatorial Antibody Library, HuCAL® GOLD, combines the advantage of a high-quality library based on the proprietary CysDisplay™ screening technology with a high diversity in the CDR regions. In collaboration with GPC Biotech AG, Martinsried, Germany, MorphoSys was able to generate HLA-DR specific antibodies that induce death of DR+ lymphoma/leukemia cells and show in vivo efficacy in murine xenograft models of non-Hodgkin's lymphoma. In addition, MorphoSys is developing therapeutic antibodies against the inflammation target ICAM-1.4:10 Xenerex™ Technology – A Powerful Platform for Accessing Human Monoclonal Antibodies Against Recall Antigens: Generation of AVP-8C1, A Potent Protective Human Monoclonal Antibody Against Anthrax PA Toxin
Dr. Angray S. Kang, Associate Director, Antibody Technology, Xenerex Biosciences-Avanir Pharmaceuticals
Avanir Pharmaceuticals Inc (XenerexÔ Biosciences.technology), has developed a powerful platform for the rapid generation of high affinity human monoclonal anti-bodies against recall antigens. The essence of the Xenerexä technology platform is three fold: First that it permits judicious selection of donors that have in the past been exposed to pathogens, attenuated pathogens or vaccines (creating many oppor-tunities):Secondly from these donor cells we can recall specific B-cells with defined antigen(s), and finally we can rescue and immortalize the cells producing the desired human antibodies. We will present an example of the Xenerex technology using Anthrax (AVA) vaccinated donors. We will demonstrate in vivo stimulation of spe-cific B-cells with PA as recall antigen. We will demonstrate the generation of a diverse a panel of high affinity antibodies that neutralize anthrax protective antigen (PA) exotoxin. From this panel we will discuss promising antibody candidates including AVP-8C1 against B. anthracis PA toxin. Our lead antibody AVP-8C1 that has a high affinity for PA (Kd 1.2.x10-12M, KinExA, 3.x10-11M, BiaCore) and neu-tralizes anthrax toxin PA in vitro, is also very effective in vivo. Data to support in vivo efficacy will be presented. Other examples of recall selection will also be pre-sented to demonstrate the versatility of this platform technology. Co-Authors: Ivy Jiang, Shu Man Sun, Rebecca Nedellec, Ritsuko Sawada, Paul Ruther, Fei Wang, Diane Millis, Alejandro Alvarez, John Abrams, & Phillip R. Morrow
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HOTEL INFORMATION
Hyatt Regency Cambridge
575 Memorial Drive
Cambridge, MA 02139
T: 617-492-1234
F: 617-491-6906
Room Rate: $189 S/D
Cut-off Date: April 21, 2003Please call the hotel directly to make your room reservation. Identify yourself as a Cambridge Healthtech Institute conference attendee to receive the reduced room rate. Reservations made after the cut-off date or after the group room block has been filled (whichever comes first) will be accepted on a space-and-rate-availability basis. Rooms are limited, so please book early.
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