Engineered xyloglucan specificity in a carbohydrate-binding module.
Cicortas Gunnarsson, Lavinia LU ; Zhou, Q ; Montanier, C ; Nordberg Karlsson, Eva LU
; Brumer, H III
and Ohlin, Mats
LU
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/594483
- author
- Cicortas Gunnarsson, Lavinia
LU
; Zhou, Q
; Montanier, C
; Nordberg Karlsson, Eva
LU
; Brumer, H III
and Ohlin, Mats
LU
- organization
- publishing date
- 2006
- 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
- 2022-01-28 05:43:41
@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}},
keywords = {{binding specificity; molecular engineering; xyloglucan; phage display; carbohydrate-binding module}},
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}},
}