oru.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Affinity maturation generates greatly improved xyloglucan-specific carbohydrate binding modules
Dept of Immunotechnology, Lund University, Lund, Sweden.
School of Biotechnology, Royal Institute of Technology (KTH), Stockholm, Sweden.
Dept of Immunotechnology, Lund University, Lund, Sweden; The International Max Plank Research School for Molecular and Cellular Biology, Max-Planck-Institute of Immunobiology, Freiburg, Germany.
Dept of Wood Science, Swedish University of Agricultural Science, Uppsala, Sweden; WURC, Swedish University of Agricultural Science, Uppsala, Sweden.
Show others and affiliations
2009 (English)In: BMC Biotechnology, ISSN 1472-6750, E-ISSN 1472-6750, Vol. 9, article id 92Article in journal (Refereed) Published
Abstract [en]

BACKGROUND: Molecular evolution of carbohydrate binding modules (CBM) is a new approach for the generation of glycan-specific molecular probes. To date, the possibility of performing affinity maturation on CBM has not been investigated. In this study we show that binding characteristics such as affinity can be improved for CBM generated from the CBM4-2 scaffold by using random mutagenesis in combination with phage display technology.

RESULTS: Two modified proteins with greatly improved affinity for xyloglucan, a key polysaccharide abundant in the plant kingdom crucial for providing plant support, were generated. Both improved modules differ from other existing xyloglucan probes by binding to galactose-decorated subunits of xyloglucan. The usefulness of the evolved binders was verified by staining of plant sections, where they performed better than the xyloglucan-binding module from which they had been derived. They discriminated non-fucosylated from fucosylated xyloglucan as shown by their ability to stain only the endosperm, rich in non-fucosylated xyloglucan, but not the integument rich in fucosylated xyloglucan, on tamarind seed sections.

CONCLUSION: We conclude that affinity maturation of CBM selected from molecular libraries based on the CBM4-2 scaffold is possible and has the potential to generate new analytical tools for detection of plant carbohydrates.

Place, publisher, year, edition, pages
BioMed Central, 2009. Vol. 9, article id 92
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:oru:diva-64486DOI: 10.1186/1472-6750-9-92ISI: 000272337000001PubMedID: 19878581Scopus ID: 2-s2.0-71049184894OAI: oai:DiVA.org:oru-64486DiVA, id: diva2:1177098
Funder
Swedish Research CouncilMarianne and Marcus Wallenberg Foundation
Note

Funding Agencies:

Formas Funcfiber Centre

NSF  RCN-0090281

Available from: 2018-01-24 Created: 2018-01-24 Last updated: 2018-01-26Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMedScopus

Authority records BETA

Gunnarsson, Lavinia Cicortas

Search in DiVA

By author/editor
Gunnarsson, Lavinia Cicortas
In the same journal
BMC Biotechnology
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 45 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf