Evidence map›Paper›PMID 26067753›Full record

ArticlemAbs2015

Processing of complex N-glycans in IgG Fc-region is affected by core fucosylation.

Alexandra Castilho, Clemens Gruber, Andreas Thader, Chris Oostenbrink, Maria Pechlaner, Herta Steinkellner, Friedrich Altmann

Open access · goldAbstract read
In one paragraph

Article in mAbs, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
6.2field-weighted citation impact, top 4% 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

33 citing papers in PubMed, 61 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Improving theFrontiers in plant science · 2024
    Article
  7. Article
  8. Introduction of a human- and keyboard-friendly N-glycan nomenclature.Beilstein journal of organic chemistry · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. An oligosaccharyltransferase fromFrontiers in plant science · 2023
    Article
  14. The role ofFrontiers in immunology · 2023
    Review
  15. Article
  16. Review
  17. 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

7 authors at 1 institution in 1 country.

Alexandra Castilhoa Department of Applied Genetics and Cell Biology ; University of Natural Resources and Life Sciences ; Vienna , Austria.
Clemens Gruber
Andreas Thader
Chris Oostenbrink
Maria Pechlaner
Herta Steinkellner
Friedrich Altmann
BOKU University · AT

Funding

Austrian Science Fund FWF L 575
6 · The paper itself

Abstract

We investigated N-glycan processing of immunoglobulin G1 using the monoclonal antibody cetuximab (CxMab), which has a glycosite in the Fab domain in addition to the conserved Fc glycosylation, as a reporter. Three GlcNAc (Gn) terminating bi-antennary glycoforms of CxMab differing in core fucosylation (α1,3- and α1,6-linkage) were generated in a plant-based expression platform. These GnGn, GnGnF(3), and GnGnF(6) CxMab variants were subjected in vivo to further processing toward sialylation and GlcNAc diversification (bisected and branching structures). Mass spectrometry-based glycan analyses revealed efficient processing of Fab glycans toward envisaged structures. By contrast, Fc glycan processing largely depend on the presence of core fucose. A particularly strong support of glycan processing in the presence of plant-specific core α1,3-fucose was observed. Consistently, molecular modeling suggests changes in the interactions of the Fc carbohydrate chain depending on the presence of core fucose, possibly changing the accessibility. Here, we provide data that reveal molecular mechanisms of glycan processing of IgG antibodies, which may have implications for the generation of glycan-engineered therapeutic antibodies with improved efficacies.

Indexed as

Amino Acid SequenceAnimalsCetuximabCrystallography, X-RayFucoseGlycosylationHumansImmunoglobulin Fc FragmentsImmunoglobulin GMiceModels, MolecularMolecular Sequence DataPolysaccharidesProtein ConformationCetuximabFucoseImmunoglobulin Fc FragmentsImmunoglobulin GPolysaccharidesbisected glycanscetuximabcore fucosylationglycan modellingIgGNicotiana benthamianasialylation

Identifiers

PMID26067753
PMCPMC4622071
OpenAlexW1675027666

What OpenQuestion holds

Textmetadata
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.