APR 04, 2016 08:00 AM PDT

Phage Antibody Selection on the Reichert SR7500DC SPR System

Speakers
  • Research Assistant Professor, Department of Microbiology and Immunology and Director, Biomolecular Interaction Laboratory, University of Rochester
    Biography
      The ability to rapidly isolate human antibodies using phage display has opened up new approaches to understanding protein function. Research in my laboratory is focused on the manipulation of immunoglobulin molecules to develop novel reagents for characterization of protein expression and structure. We are using phage antibody technology in several areas of proteomics research to develop improved reagents for protein characterization as well as novel inhibitors of protein function that will aid in defining the roles of the many new proteins discovered through genomic sequencing. Major efforts are aimed at dissecting the saliva proteome and developing panels of antibodies for incorporation into new diagnostic platforms using protein microarrays.

      A second initiative is to derive antibodies useful for solving the structure of proteins by X-ray crystallography. Additional studies focus on the therapeutic potential of single-chain antibodies to reduce protein aggregation and misfolding, a process that characterizes a variety of neurodegenerative diseases.

    Abstract:
    DATE: April 4, 2016
    TIME:  8:00am Pacific time, 11:00am Eastern time


    The use of surface plasmon resonance to characterize protein:protein interactions is well established and has been the method of choice for determination of antibody affinity for the last 20 years. Developments such as phage display have led to rapid production of numerous antibodies in a high-throughput environment that typically requires affinity analysis to select the proper candidates for further development. Moreover, since most display libraries are limited in terms of the number of sequences in the libraries (typically 1x109 to 1x1010), a frequent result is that initial candidates for development are not of sufficiently high affinity, necessitating affinity improvement strategies.  In this presentation, we will describe our studies to demonstrate that the Reichert SPR System can be used to improve the efficiency of phage antibody isolation and characterization and to evaluate the potential for optimizing selection of high affinity variants. The idea of using an SPR instrument to function as both a lab-on a chip to permit semi-automated manipulation of phage preparations as well as providing the SPR signal as a window on the binding and enrichment of high affinity variants of scFvs or Fabs (or other scaffolds like camelid VHH and fibronectin domains) is appealing, and could lead to a significant competitive advantage in the expanding market for therapeutic antibodies.

    Learning Objectives
    • Gain an appreciation for how SPR could be utilized to dramatically improve the phage display and enrichment process
    • Understanding parameters important for optimizing phage enrichment processes
    • Understanding of the flexibility of the Reichert SPR system for phage applications


     

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