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Engineered xyloglucan specificity in a carbohydrate-binding module.

Cicortas Gunnarsson, Lavinia LU ; Zhou, Q ; Montanier, C ; Nordberg Karlsson, Eva LU orcid ; Brumer, H III and Ohlin, Mats LU orcid (2006) In Glycobiology 16(12). p.1171-1180
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 -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... (More)
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 -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 ß-glucan-binding ability was achieved. (Less)
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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
binding specificity, molecular engineering, xyloglucan, phage display, carbohydrate-binding module
in
Glycobiology
volume
16
issue
12
pages
1171 - 1180
publisher
Oxford University Press
external identifiers
  • wos:000242270800002
  • scopus:33751368319
ISSN
1460-2423
DOI
10.1093/glycob/cwl038
project
Designed carbohydrate binding modules and molecular probes
language
English
LU publication?
yes
id
36595e57-0147-4540-8db0-beb43a82489a (old id 594483)
date added to LUP
2016-04-01 15:31:25
date last changed
2021-08-04 01:29:24
@article{36595e57-0147-4540-8db0-beb43a82489a,
  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 -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 ß-glucan-binding ability was achieved.},
  author       = {Cicortas Gunnarsson, Lavinia and Zhou, Q and Montanier, C and Nordberg Karlsson, Eva and Brumer, H III and Ohlin, Mats},
  issn         = {1460-2423},
  language     = {eng},
  number       = {12},
  pages        = {1171--1180},
  publisher    = {Oxford University Press},
  series       = {Glycobiology},
  title        = {Engineered xyloglucan specificity in a carbohydrate-binding module.},
  url          = {http://dx.doi.org/10.1093/glycob/cwl038},
  doi          = {10.1093/glycob/cwl038},
  volume       = {16},
  year         = {2006},
}