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Engineered xyloglucan specificity in a carbohydrate-binding module

TitleEngineered xyloglucan specificity in a carbohydrate-binding module
Publication TypeJournal Article
Year of Publication2006
AuthorsGunnarsson, LCicortas, Zhou, Q, Montanier, C, Karlsson, ENordberg, Brumer, H, Ohlin, M
JournalGLYCOBIOLOGY
Volume16
Pagination1171-1180
Date PublishedDEC
Type of ArticleArticle
ISSN0959-6658
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 exist in both fucosylated and non-fucosylated variants. Presently, the only xyloglucan marker available is the monoclonal antibody CCRC-M1 that is specific to 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, 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 is described. Using phage display technology in combination with a chemoenzymatic 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.

DOI10.1093/glycob/cwl038