Evidence map›Paper›PMID 27038031›Full record

ArticleJournal of the American Society for Mass Spectrometry2016

Site-Specific N-Glycosylation of Recombinant Pentameric and Hexameric Human IgM.

Edward S X Moh, Chi-Hung Lin, Morten Thaysen-Andersen, Nicolle H Packer

Abstract read
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In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Article
  2. Defining the Features of Complement-Active IgM.Journal of molecular biology · 2025
    Article
  3. Understanding IgM Structure and Biology to Engineer New Antibody Therapeutics.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Bacterial lectin BambL acts as a B cell superantigen.Cellular and molecular life sciences : CMLS · 2021
    Article
  11. 3D Structures of IgA, IgM, and Components.International journal of molecular sciences · 2021
    Review
  12. Glycosylation of Plant-Produced Immunoglobulins.Experientia supplementum (2012) · 2021
    Article
  13. Review
  14. Secreted IgM: New tricks for an old molecule.Journal of leukocyte biology · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  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

4 authors.

Edward S X MohDepartment of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, NSW, 2109, Australia.
Chi-Hung LinDepartment of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, NSW, 2109, Australia.
Morten Thaysen-AndersenDepartment of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, NSW, 2109, Australia.
Nicolle H PackerDepartment of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, NSW, 2109, Australia. nicki.packer@mq.edu.au.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation is known to play an important role in IgG antibody structure and function. Polymeric IgM, the largest known antibody in humans, displays five potential N-glycosylation sites on each heavy chain monomer. IgM can exist as a pentamer with a connecting singly N-glycosylated J-chain (with a total of 51 glycosylation sites) or as a hexamer (60 glycosylation sites). In this study, the N-glycosylation of recombinant pentameric and hexameric IgM produced by the same human cell type and culture conditions was site-specifically profiled by RP-LC-CID/ETD-MS/MS using HILIC-enriched tryptic and GluC glycopeptides. The occupancy of all putative N-glycosylation sites on the pentameric and hexameric IgM were able to be determined. Distinct glycosylation differences were observed between each of the five N-linked sites on the IgM heavy chains. While Asn171, Asn332, and Asn395 all had predominantly complex type glycans, differences in glycan branching and sialylation were observed between the sites. Asn563, a high mannose-rich glycosylation site that locates in the center of the IgM polymer, was only approximately 60% occupied in both the pentameric and hexameric IgM forms, with a difference in relative abundance of the glycan structures between the pentamer and hexamer. This study highlights the information obtained by characterization of the site-heterogeneity of a highly glycosylated protein of high molecular mass with quaternary structure, revealing differences that would not be seen by global glycan or deglycosylated peptide profiling. Graphical Abstract ᅟ.

Indexed as

Amino Acid SequenceChromatography, LiquidGlycopeptidesGlycosylationHumansImmunoglobulin GImmunoglobulin MPolysaccharidesTandem Mass SpectrometryGlycopeptidesImmunoglobulin GImmunoglobulin MPolysaccharidesGlycopeptideHexamerIgMPentamerSite-specific glycosylation

Identifiers

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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.