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Engineered xyloglucan specificity in a carbohydrate-binding module
KTH, Skolan för bioteknologi (BIO), Glykovetenskap.ORCID-id: 0000-0001-9832-027X
Vise andre og tillknytning
2006 (engelsk)Inngår i: Glycobiology, ISSN 0959-6658, E-ISSN 1460-2423, Vol. 16, nr 12, s. 1171-1180Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

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.

sted, utgiver, år, opplag, sider
2006. Vol. 16, nr 12, s. 1171-1180
Emneord [en]
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
Identifikatorer
URN: urn:nbn:se:kth:diva-16145DOI: 10.1093/glycob/cwl038ISI: 000242270800002Scopus ID: 2-s2.0-33751368319OAI: oai:DiVA.org:kth-16145DiVA, id: diva2:334187
Merknad
QC 20100525Tilgjengelig fra: 2010-08-05 Laget: 2010-08-05 Sist oppdatert: 2017-12-12bibliografisk kontrollert

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