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Glycobiology Advance Access published online on August 10, 2006
Glycobiology, doi:10.1093/glycob/cwl038
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received November 24, 2005
Revised August 7, 2006
Accepted August 8, 2006

Article

Engineered xyloglucan specificity in a carbohydrate-binding module

Lavinia Cicortas Gunnarsson 1, Qi Zhou 2, Cedric Montanier 3, Eva Nordberg Karlsson 4, Harry Brumer III 2, and Mats Ohlin 1 *

1 Department of Immunotechnology, Lund University, BMC D13, SE-221 84 Lund, Sweden
2 School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Center, SE-106 91 Stockholm, Sweden
3 Institute for Cell and Molecular Biosciences, University of Newcastle upon Tyne, Framlington Place, Newcastle upon Tyne NE2 4HH, United Kingdom
4 Department of Biotechnology, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden

* To whom correspondence should be addressed.
Mats Ohlin, E-mail: mats.ohlin{at}immun.lth.se


  Abstract

The field of plant cell wall biology is constantly growing and consequently so is the need for more sensitive and specific probes for individual wall components. Xyloglucan is a key polysaccharide widely distributed in the plant kingdom in both structural and storage tissues that exists in both fucosylated and non-fucosylated variants. Presently, the only xyloglucan marker available is the monoclonal antibody CCRC-M1 that is specific for terminal {alpha}-1,2-linked fucosyl residues on xyloglucan oligo- and polysaccharides. As a viable alternative to searches for natural binding proteins or creation of new monoclonal antibodies, we describe an approach to select xyloglucan-specific binding proteins from a combinatorial library of the carbohydrate binding module, CBM4-2, from xylanase Xyn10A of Rhodothermus marinus. Using phage-display technology in combination with a chemo-enzymatic method to anchor xyloglucan to solid supports, the selection of xyloglucan binding modules with no detectable residual wild-type xylan and {beta}-glucan binding ability was achieved.

Keywords: binding specificity /carbohydrate-binding module/molecular engineering/phage-display/xyloglucan.
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