Table of Contents
Biotechnology Research International
Volume 2017 (2017), Article ID 8791359, 8 pages
https://doi.org/10.1155/2017/8791359
Research Article

Generation of Recombinant Antibodies against the beta-(1,6)-Branched beta-(1,3)-D-Glucan Schizophyllan from Immunized Mice via Phage Display

1Department for Biotechnology, Institute of Biochemistry, Biotechnology and Bioinformatics, Technische Universität Braunschweig, Spielmannstraße 17, 38106 Braunschweig, Germany
2Institute for Physical and Theoretical Chemistry, Technische Universität Braunschweig, Rebenring 56, 38106 Braunschweig, Germany
3YUMAB GmbH, Rebenring 33, 38106 Braunschweig, Germany

Correspondence should be addressed to Udo Rau; ed.sb-ut@uar.u

Received 28 February 2017; Accepted 2 May 2017; Published 23 May 2017

Academic Editor: Maxim Golovkin

Copyright © 2017 Jörn Josewski et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

beta-(1,6)-Branched beta-(1,3)-D-glucans like schizophyllan from the basidiomycete Schizophyllum commune excite various immunostimulatory effects and have been clinically tested as adjuvants. Some of the glucans are also applicable in food or petrol industry due to their viscosity and temperature stability in aqueous solution. Antibodies against these glucans could be used as tool for analysis of glucan preparations or for further research of its bioactivity. Therefore, an immune phage display library was constructed from mice immunized with schizophyllan. Three recombinant monoclonal antibodies were isolated from this library by affinity selection (panning) on schizophyllan. The half-maximal effective concentration (EC50) values for those antibodies varied between 16.4 ng mL−1 and 21.3 ng mL−1. The clones showed binding specificity not only for schizophyllan but also for other beta-(1,6)-branched beta-(1,3)-D-glucans of similar macromolecular structure. Denaturation of the secondary structure led to a reduced antibody binding, indicating an epitope requiring the correct conformation of the triple helical structure of the glucans.