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Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries
Published on: January 17, 2015
Structure of a VHH isolated from a naïve phage display library
Brandy White1, Ian Huh1, Cory L Brooks2
1Department of Chemistry, California State University Fresno, 2555 E San Ramon Ave, Fresno, CA, 93740, USA.
Objective:
To determine the X-ray structure and biophysical properties of a Camelid VHH isolated from a naïve phage display library.
Results:
Single domain antibodies (VHH) derived from the unique immune system of the Camelidae family have gained traction as useful tools for biotechnology as well as a source of potentially novel therapeutics. Here we report the structure and biophysical characterization of a VHH originally isolated from a naïve camelid phage display library. VHH R419 has a melting temperate of 66 °C and was found to be a monomer in solution. The protein crystallized in space group P6522 and the structure was solved by molecular replacement to a resolution of 1.5 Å. The structure revealed a flat paratope with CDR loops that could be classified into existing canonical loop structures. A combination of high expression yield, stability and rapid crystallization might make R419 into a candidate scaffold for CDR grafting and homology modeling.
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