Evidence map›Paper›PMID 31544815›Full record

ArticleAntibodies (Basel, Switzerland)2019

Impact of Acetylated and Non-Acetylated Fucose Analogues on IgG Glycosylation.

Martina Zimmermann, Janike Ehret, Harald Kolmar, Aline Zimmer

Abstract read
In one paragraph

Article in Antibodies (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. A metabolic inhibitor blocks cellular fucosylation and enables production of afucosylated antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. 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

4 authors.

Martina ZimmermannMerck Life Sciences, Upstream R&D, Frankfurter Strasse 250, 64293 Darmstadt, Germany. martina.zimmermann@external.merckgroup.com.ORCID 0000-0001-5896-6084
Janike EhretMerck Life Sciences, Upstream R&D, Frankfurter Strasse 250, 64293 Darmstadt, Germany. Janike.ehret@merckgroup.com.ORCID 0000-0003-2215-0168
Harald KolmarInstitute for Organic Chemistry and Biochemistry, Technische Universität Darmstadt, Alarich-Weiss-Strasse 4, 64287 Darmstadt, Germany. Kolmar@Biochemie-TUD.de.ORCID 0000-0002-8210-1993
Aline ZimmerMerck Life Sciences, Upstream R&D, Frankfurter Strasse 250, 64293 Darmstadt, Germany. Aline.zimmer@merckgroup.com.ORCID 0000-0003-0279-4863

Funding

Merck KGaA N/A
6 · The paper itself

Abstract

The biological activity of therapeutic antibodies is highly influenced by their glycosylation profile. A valuable method for increasing the cytotoxic efficacy of antibodies, which are used, for example, in cancer treatment, is the reduction of core fucosylation, as this enhances the elimination of target cells through antibody-dependent cell-mediated cytotoxicity. Development of fucose analogues is currently the most promising strategy to reduce core fucosylation without cell line engineering. Since peracetylated sugars display enhanced cell permeability over the highly polar free hydroxy sugars, this work sought to compare the efficacy of peracetylated sugars to their unprotected forms. Two potent fucose analogues, 2-deoxy-2-fluorofucose and 5-alkynylfucose, and their acetylated forms were compared for their effects on fucosylation. 5-alkynylfucose proved to be more potent than 2-deoxy-2-fluorofucose at reducing core fucosylation but was associated with a significant higher incorporation of the alkynylated fucose analogue. Acetylation of the sugar yielded only slightly lower fucosylation levels suggesting that acetylation has a minor impact on cellular entry. Even though the efficacy of all tested components was confirmed, results presented in this study also show a significant incorporation of unnatural fucose analogues into the glycosylation pattern of the produced IgG, with unknown effect on safety and potency of the monoclonal antibody.

Indexed as

acetylationCHO cell culturefucose analoguesIgG fucosylationincorporation

Identifiers

PMID31544815
PMCPMC6640710

What OpenQuestion holds

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Registered trials

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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.