Journal article

Selection and affinity maturation of IgNAR variable domains targeting Plasmodium falciparum AMA1

SD Nuttall, KS Humberstone, UV Krishnan, JA Carmichael, L Doughty, M Hattarki, AM Coley, JL Casey, RF Anders, M Foley, RA Irving, PJ Hudson

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | WILEY | Published : 2004

Abstract

The new antigen receptor (IgNAR) is an antibody unique to sharks and consists of a disulphide-bonded dimer of two protein chains, each containing a single variable and five constant domains. The individual variable (V(NAR)) domains bind antigen independently, and are candidates for the smallest antibody-based immune recognition units. We have previously produced a library of V(NAR) domains with extensive variability in the CDR1 and CDR3 loops displayed on the surface of bacteriophage. Now, to test the efficacy of this library, and further explore the dynamics of V(NAR) antigen binding we have performed selection experiments against an infectious disease target, the malarial Apical Membrane A..

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