Archived Content

DISCOVERY STREAM  

14th Annual  

Phage and Yeast Display of Antibodies
and Proteins April 30 - May 1


The methods for using phage and yeast display are constantly being improved and modified for the purpose of isolating high affinity protein ligands against nearly any receptor through directed evolution.   The use of display techniques generate high quality antibody libraries to screen against disease targets.  This meeting will look at the use of high throughput gene sequencing for improving library diversity and depth.  It will also look at using criteria early in selections for developability.  The use of available crystal structures is now guiding engineering approaches for biologics.  Plan to take in the latest developments in this important sector of protein engineering to see where the field is headed.

Meet the Scientific Advisory Board 

Andrew M. Bradbury, M.B. B.S., Ph.D., Staff Scientist, Biosciences, Los Alamos National Laboratory - Biography 

David Lowe, Ph.D., Fellow, R&D, MedImmune, UK 

Aaron K. Sato, Ph.D., Senior Director, OncoMed Pharmaceuticals, Inc. - Biography  

Gregory A. Weiss, Ph.D., Professor, Departments of Chemistry, Molecular Biology & Biochemistry, University of California, Irvine - Biography  

K. Dane Wittrup, Ph.D., J.R. Mares Professor, Chemical Engineering & Bioengineering, Massachusetts Institute of Technology - Biography   

 

Day 1 | Day 2 | Download Brochure 

SUNDAY, APRIL 29

4:00 - 6:00 pm Main Conference Registration

 

MONDAY, APRIL 30

7:00 am Registration and Morning Coffee


» KEYNOTE SESSION 

8:30 Chairperson’s Opening Remarks

Aaron K. Sato, Ph.D., Senior Director, OncoMed Pharmaceuticals, Inc.

8:40 Display Antibodies against Interesting Targets: Partnerships with Academia

Anthony J. CoyleAnthony J. Coyle, Ph.D., Vice President & CSO, Centers for Therapeutic Innovation, Pfizer, Inc. (biography)

Centers for Therapeutic Innovation (CTI) is the industry leading model in R&D in innovation.  CTI’s have been established in four US-based sites, signing 19 academic partners and is poised to be a transformational force, employing an entrepreneurial R&D model that accesses the best science in the world to deliver mechanistically-relevant clinical studies that can translate into differentiated, clinically-validated candidates in order to deliver important medicines to patients.  This presentation will highlight some of the innovative science and technology science in the Oncology and Autoimmune disease fields.

9:10 Generation of Receptor-Blocking Human Antibodies by Phage Display

John McCaffertyJohn McCafferty, Ph.D., Research Director, Biochemistry, University of Cambridge (biography)

Recombinant antibodies provide a means to control receptor activation with potential utility in the treatment of cancer or the control of stem cell differentiation. Using phage display in conjunction with cell based screening assays we have generated and affinity matured human antibodies which affect cell signalling by a number of different modalities including ligand neutralisation, receptor blocking and stabilisation of closed conformations. The different approaches used will be discussed.


B CELL CLONING 

9:40 B Cell Display: Screening the Native Human B Cell Repertoire for Broadly Crossreactive Antibodies against the Influenza A Virus

Minha-ParkMinha Park, Ph.D., Scientist, Antibody Discovery & B Cell Immunology, Trellis Bioscience (biography)

The human B cell repertoire represents a rich library of antibodies that have been naturally selected for high affinity, stability, and lack of off-target reactivity against human antigens, and therefore, less likely to cause immunogenicity when used as therapeutic agents.  However, the low frequency of B cells expressing high quality antigen-specific antibodies has posed a barrier to discovery.  Here, we show successful application of the Trellis Cellspot platform of single cell phenotyping to recover rare human B cells expressing high affinity and broadly crossreactive antibodies against the influenza A virus.
 

10:10 Grand Opening Coffee Break in the Exhibit Hall with Poster Viewing

 

IN VIVO HALF-LIFE EXTENSION 

11:10 Engineering Super Albumin for Improving Serum Half-Life

G. Jonah A. Rainey, Ph.D., Scientist II, Antibody Discovery & Protein Engineering, MedImmune LLC

FcRn binds both IgG and albumin and diverts them from the lysosomal degredation pathway thus enhancing their lifespan. While FcRn mediated half-life extension through Fc has been engineered extensively, pH dependent affinity maturation of albumin to improve serum half-life remains laregely unexplored. We have engineered human albumin to improve its affinity for FcRn while retaining the pH dependence of binding through off rate engineering to extend lifespan of non-antibody therapeutics.

11:40 Use of pH Dependent Binding of Engineered Antibodies with Improved in vivo Half-Life Extension

Sally-WardE. Sally Ward, Ph.D., Paul and Betty Meek-FINA Professorship, Molecular Immunology, Cancer Immunobiology Center, University of Texas Southwestern (biography)

FcRn plays a central role in regulating the transport and distribution of IgG in the body. The presentation will cover recent developments in understanding FcRn function, combined with engineering FcRn-Fc interactions to generate therapies for autoimmune disease.

 

Sponsored by
Novozymes (white)
12:10 pm Advances in Albumin Half-Life Extension Platform Translates to Positive Pharmacokinetic Studies

Mark Perkins, Ph.D., Technical Solution Specialist, Novozymes Biopharma

The ability to enhance the therapeutic half-life of drugs by conjugation or fusion to albumin is now well established. We have shown that albumin can be further enhanced for uses in drug delivery by manipulating its interaction with the neonatal Fc receptor (FcRn) via the introduction of specific amino acid changes in the albumin sequence. This talk will highlight a novel albumin platform and will include new pharmacokinetic data demonstrating the extended circulatory half-life of the albumin variants and protein drugs linked to such variants.

12:40 Luncheon Presentations (Sponsorship Opportunities Available) or Lunch on Your Own

 

EPITOPE MAPPING WITH CRYSTALLIZATION AND DISPLAY 

2:00 Chairperson’s Remarks

David Lowe, Ph.D., Fellow, R&D, MedImmune UK

2:05 Phage Selection of Bicyclic Peptides

Christian-HeinisChristian Heinis, Ph.D., Laboratory of Therapeutic Peptides and Proteins, Ecole Polytechnique Federal de Lausanne (EPFL) (biography)

My laboratory is generating bicyclic peptide ligands with high affinity and specificity for disease targets using a phage display-based approach that I had developed with Sir Greg Winter at the Laboratory of Molecular Biology (LMB) in Cambridge, UK (1). I will present the structure of a target-bound bicyclic peptide, new bicyclic peptide formats as well as first in vivo data.
 

2:35 Synthetic Antibodies: Structure and Function

Shane Miersch, Ph.D., Research Associate, Sidhu Lab, University of Toronto

Synthetic antibody libraries have simplified the discovery of antibodies for structural studies. Synthetic antibody libraries are highly versatile for generating antibodies against diverse antigens. Moreover, synthetic antibodies exhibit superior performance in crystallization studies due to their stable nature.

3:05 Optimizing Functional Modules of Bispecific Antibodies Using Yeast Display Platform

Lihui Xu, Ph.D., Principal Scientist & Group Leader, Antibody Technology, Merrimack Pharmaceuticals (biography)

We developed a yeast display platform that combines the features of surface display and soluble expression within the single system, in conjunction with small structure-guided antibody library and innovative screening strategy, we are able to discover optimal functional modules in single campaign for a bispecific antibody that targets two Growth Factor Receptors.

3:35 State of the Art Epitope Mapping and Insights Gained from mAb-Target Co-Crystal Structures

David Lowe, Ph.D., Fellow, R&D, MedImmune UK (biography)

Examples of co-crystal structures will be used to provide insight into the antibody mechanism of action, species cross reactivity and the characteristics of the antibody paratope. In addition, alternative methods of epitope mapping will be illustrated.

4:05 Refreshment Break in the Exhibit Hall with Poster Viewing


4:45 Problem Solving Breakout Discussions

Concurrent problem solving breakout discussions, open to all attendees, speakers, sponsors, and exhibitors, provide a forum for discussing key issues and meeting potential collaborators. Plan to take part and explore these topics in-depth. Please pick a topic of your choice, find your table and join in.

Exploiting Crystallization Methods with Phage

Moderator:  Christian Heinis, Ph.D., Laboratory of Therapeutic Peptides and Proteins, Ecole Polytechnique Federal de Lausanne (EPFL)

• Antibody fragments as tools in crystallography
• Crystallization properties of alternative scaffolds
• Success rates with crystallization chaperones
• Selection of antibody fragments to diverse epitopes

Breaking the Barrier: Selecting Antibodies to Penetrate the BBB

Moderator:  Eric V. Shusta, Ph.D., Associate Professor, Chemical & Biological Engineering, University of Wisconsin, Madison


Synthetic Antibody Library Generation Strategies

Moderator:  Shane Miersch, Ph.D., Research Associate, Sidhu Lab, University of Toronto

• Framework choice
• Structure-based versus random design
• Choice of randomization sites
• Choice of chemical diversity

When Phage Falls Short: Alternate Display Methods

Moderator:  Eric T. Boder, Ph.D., Career Development Associate Professor, Chemical & Biomolecular Engineering, University of Tennessee

Techniques to Improve Half-Life Extension

Moderator: Chaity Chaudhury, Ph.D., Scientist, Antibody Discovery & Protein Engineering, MedImmune LLC

5:45-6:45 Welcome Reception in the Exhibit Hall with Poster Viewing
Emerald BioStructuresPoster Awards Sponsored by



Day 1 | Day 2 | Download Brochure