Evidence map›Paper›PMID 19878581›Full record

ArticleBMC biotechnology2009

Affinity maturation generates greatly improved xyloglucan-specific carbohydrate binding modules.

Laura von Schantz, Fredrika Gullfot, Sebastian Scheer, Lada Filonova, Lavinia Cicortas Gunnarsson, James E Flint, Geoffrey Daniel, Eva Nordberg-Karlsson, Harry Brumer, Mats Ohlin

Open access · goldAbstract read
In one paragraph

Article in BMC biotechnology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 29% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
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  6. Article
  7. Immunological Approaches to Biomass Characterization and Utilization.Frontiers in bioengineering and biotechnology · 2015
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 5 institutions in 3 countries.

Laura von SchantzDept of Immunotechnology, Lund University, Lund, Sweden. laura.von_schantz@immun.lth.se
Fredrika Gullfot
Sebastian Scheer
Lada Filonova
Lavinia Cicortas Gunnarsson
James E Flint
Geoffrey Daniel
Eva Nordberg-Karlsson
Harry Brumer
Mats Ohlin
Lund University · SEKTH Royal Institute of Technology · SESwedish University of Agricultural Sciences · SEMax Planck Society · DENewcastle University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMolecular 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.

resultsTwo 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.

conclusionWe 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.

Indexed as

Mutagenesis, Site-DirectedPeptide LibraryAmino Acid SequenceGlucansMolecular Sequence DataProtein BindingReceptors, Cell SurfaceSeedsSubstrate SpecificityTamarindusXylansGlucansPeptide LibraryReceptors, Cell Surfacesaccharide-binding proteinsXylansxyloglucan

Identifiers

PMID19878581
PMCPMC2783032
OpenAlexW1992617534

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.