Evidence map›Paper›PMID 34157283›Full record

ReviewThe Journal of biological chemistry2021

Sialic acid O-acetylation: From biosynthesis to roles in health and disease.

Eline A Visser, Sam J Moons, Suzanne B P E Timmermans, Heleen de Jong, Thomas J Boltje, Christian Büll

Open access · goldAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

60 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Forgotten Gangliosides:International journal of molecular sciences · 2026
    Review
  9. Article
  10. Glycan-related genes and genetic disorders.Journal of human genetics · 2026
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Loss of sialic acid side-chainProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Article
  19. Article
  20. Expression of 9-Life (Basel, Switzerland) · 2025
    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

6 authors at 2 institutions in 2 countries.

Eline A VisserInstitute for Molecules and Materials, Department of Synthetic Organic Chemistry, Radboud University Nijmegen, Nijmegen, the Netherlands.
Sam J MoonsInstitute for Molecules and Materials, Department of Synthetic Organic Chemistry, Radboud University Nijmegen, Nijmegen, the Netherlands.
Suzanne B P E TimmermansInstitute for Molecules and Materials, Department of Synthetic Organic Chemistry, Radboud University Nijmegen, Nijmegen, the Netherlands.
Heleen de JongInstitute for Molecules and Materials, Department of Synthetic Organic Chemistry, Radboud University Nijmegen, Nijmegen, the Netherlands.
Thomas J BoltjeInstitute for Molecules and Materials, Department of Synthetic Organic Chemistry, Radboud University Nijmegen, Nijmegen, the Netherlands. Electronic address: t.boltje@ru.nl.
Christian BüllCopenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark; Hubrecht Institute, Utrecht, the Netherlands. Electronic address: c.bull@sund.ku.dk.
Radboud University Nijmegen · NLUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sialic acids are nine-carbon sugars that frequently cap glycans at the cell surface in cells of vertebrates as well as cells of certain types of invertebrates and bacteria. The nine-carbon backbone of sialic acids can undergo extensive enzymatic modification in nature and O-acetylation at the C-4/7/8/9 position in particular is widely observed. In recent years, the detection and analysis of O-acetylated sialic acids have advanced, and sialic acid-specific O-acetyltransferases (SOATs) and O-acetylesterases (SIAEs) that add and remove O-acetyl groups, respectively, have been identified and characterized in mammalian cells, invertebrates, bacteria, and viruses. These advances now allow us to draw a more complete picture of the biosynthetic pathway of the diverse O-acetylated sialic acids to drive the generation of genetically and biochemically engineered model cell lines and organisms with altered expression of O-acetylated sialic acids for dissection of their roles in glycoprotein stability, development, and immune recognition, as well as discovery of novel functions. Furthermore, a growing number of studies associate sialic acid O-acetylation with cancer, autoimmunity, and infection, providing rationale for the development of selective probes and inhibitors of SOATs and SIAEs. Here, we discuss the current insights into the biosynthesis and biological functions of O-acetylated sialic acids and review the evidence linking this modification to disease. Furthermore, we discuss emerging strategies for the design, synthesis, and potential application of unnatural O-acetylated sialic acids and inhibitors of SOATs and SIAEs that may enable therapeutic targeting of this versatile sialic acid modification.

Indexed as

AcetylationAcetyltransferasesAnimalsBiosynthetic PathwaysCarboxylic Ester HydrolasesDiseaseGlycoproteinsHumansN-Acetylneuraminic AcidPolysaccharidesAcetyltransferasesCarboxylic Ester HydrolasesGlycoproteinsN-Acetylneuraminic AcidPolysaccharidessialic acid O-acetyltransferaseglycan modificationsglycobiologyinfluenza C/D virusO-acetylationsialic acid O-acetyl esterases (SIAEs)sialic acid O-acetyl transferases (SOATs)sialic acids

Identifiers

PMID34157283
PMCPMC8319020
OpenAlexW3174385860

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.