Engineered xyloglucan specificity in a carbohydrate-binding module
2006 (English)In: Glycobiology, ISSN 0959-6658, E-ISSN 1460-2423, Vol. 16, no 12, 1171-1180 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2006. Vol. 16, no 12, 1171-1180 p.
binding specificity, carbohydrate-binding module, molecular engineering, phage display, xyloglucan, plant-cell walls, rhodothermus-marinus xylanase, antibody fab fragments, monoclonal-antibodies, pichia-pastoris, cellulose, oligosaccharides, polysaccharides, affinity, probes
IdentifiersURN: urn:nbn:se:kth:diva-16145DOI: 10.1093/glycob/cwl038ISI: 000242270800002ScopusID: 2-s2.0-33751368319OAI: oai:DiVA.org:kth-16145DiVA: diva2:334187
QC 201005252010-08-052010-08-05Bibliographically approved