Evidence map›Paper›PMID 24821760›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Specificity of O-glycosylation in enhancing the stability and cellulose binding affinity of Family 1 carbohydrate-binding modules.

Liqun Chen, Matthew R Drake, Michael G Resch, Eric R Greene, Michael E Himmel, Patrick K Chaffey, Gregg T Beckham, Zhongping Tan

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Loosenin-Like Proteins fromApplied and environmental microbiology · 2023
    Article
  6. Engineering cellulases for conversion of lignocellulosic biomass.Protein engineering, design & selection : PEDS · 2023
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Carbohydrate-binding moduleChemical science · 2020
    Article
  12. Article
  13. Article
  14. Review
  15. UniqueJournal of biological engineering · 2019
    Article
  16. Article
  17. The impact ofChemical science · 2018
    Article
  18. Article
  19. Article
  20. Article
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

8 authors.

Liqun ChenDepartment of Chemistry and Biochemistry and BioFrontiers Institute, University of Colorado, Boulder, CO 80303; and.
Matthew R DrakeDepartment of Chemistry and Biochemistry and BioFrontiers Institute, University of Colorado, Boulder, CO 80303; and.
Michael G ReschBiosciences Center and.
Eric R GreeneDepartment of Chemistry and Biochemistry and BioFrontiers Institute, University of Colorado, Boulder, CO 80303; and.
Michael E HimmelBiosciences Center and.
Patrick K ChaffeyDepartment of Chemistry and Biochemistry and BioFrontiers Institute, University of Colorado, Boulder, CO 80303; and.
Gregg T BeckhamNational Bioenergy Center, National Renewable Energy Laboratory, Golden, CO 80401 gregg.beckham@nrel.gov zhongping.tan@colorado.edu.
Zhongping TanDepartment of Chemistry and Biochemistry and BioFrontiers Institute, University of Colorado, Boulder, CO 80303; and gregg.beckham@nrel.gov zhongping.tan@colorado.edu.ORCID http://orcid.org/0000-0002-9302-150X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The majority of biological turnover of lignocellulosic biomass in nature is conducted by fungi, which commonly use Family 1 carbohydrate-binding modules (CBMs) for targeting enzymes to cellulose. Family 1 CBMs are glycosylated, but the effects of glycosylation on CBM function remain unknown. Here, the effects of O-mannosylation are examined on the Family 1 CBM from the Trichoderma reesei Family 7 cellobiohydrolase at three glycosylation sites. To enable this work, a procedure to synthesize glycosylated Family 1 CBMs was developed. Subsequently, a library of 20 CBMs was synthesized with mono-, di-, or trisaccharides at each site for comparison of binding affinity, proteolytic stability, and thermostability. The results show that, although CBM mannosylation does not induce major conformational changes, it can increase the thermolysin cleavage resistance up to 50-fold depending on the number of mannose units on the CBM and the attachment site. O-Mannosylation also increases the thermostability of CBM glycoforms up to 16 °C, and a mannose disaccharide at Ser3 seems to have the largest themostabilizing effect. Interestingly, the glycoforms with small glycans at each site displayed higher binding affinities for crystalline cellulose, and the glycoform with a single mannose at each of three positions conferred the highest affinity enhancement of 7.4-fold. Overall, by combining chemical glycoprotein synthesis and functional studies, we show that specific glycosylation events confer multiple beneficial properties on Family 1 CBMs.

Indexed as

BiofuelsModels, MolecularCellulasesGlycosylationLigninMolecular StructureProtein EngineeringReceptors, Cell SurfaceTrichodermaBiofuelsCellulasesLigninlignocelluloseReceptors, Cell Surfacesaccharide-binding proteinsbiofuelscellulasechemical synthesisprotein engineering

Identifiers

PMID24821760
PMCPMC4040550

What OpenQuestion holds

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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.