Evidence map›Paper›PMID 29436927›Full record

ArticlemAbs2018

Quantitative analysis of glycation and its impact on antigen binding.

Jingjie Mo, Renzhe Jin, Qingrong Yan, Izabela Sokolowska, Michael J Lewis, Ping Hu

Open access · goldAbstract read
In one paragraph

Article in mAbs, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
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  5. Article
  6. Article
  7. Article
  8. Comparative Structure Activity Relationship Characterization of the Biosimilar BAT1806/BIIB800 to Reference Tocilizumab.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2025
    Article
  9. Article
  10. Protein Haptenation and Its Role in Allergy.Chemical research in toxicology · 2024
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Micro-Heterogeneity of Antibody Molecules.Experientia supplementum (2012) · 2021
    Review
  19. Review
  20. Review
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 1 institution in 1 country.

Jingjie Moa Large Molecules Analytical Development, Pharmaceutical Development & Manufacturing Sciences , Janssen Research & Development, LLC , Malvern , Pennsylvania , United States.
Renzhe Jina Large Molecules Analytical Development, Pharmaceutical Development & Manufacturing Sciences , Janssen Research & Development, LLC , Malvern , Pennsylvania , United States.ORCID 0000-0002-9519-4957
Qingrong Yana Large Molecules Analytical Development, Pharmaceutical Development & Manufacturing Sciences , Janssen Research & Development, LLC , Malvern , Pennsylvania , United States.
Izabela Sokolowskaa Large Molecules Analytical Development, Pharmaceutical Development & Manufacturing Sciences , Janssen Research & Development, LLC , Malvern , Pennsylvania , United States.
Michael J Lewisa Large Molecules Analytical Development, Pharmaceutical Development & Manufacturing Sciences , Janssen Research & Development, LLC , Malvern , Pennsylvania , United States.
Ping Hua Large Molecules Analytical Development, Pharmaceutical Development & Manufacturing Sciences , Janssen Research & Development, LLC , Malvern , Pennsylvania , United States.
Pharmaceutical Product Development (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycation has been observed in antibody therapeutics manufactured by the fed-batch fermentation process. It not only increases the heterogeneity of antibodies, but also potentially affects product safety and efficacy. In this study, non-glycated and glycated fractions enriched from a monoclonal antibody (mAb1) as well as glucose-stressed mAb1 were characterized using a variety of biochemical, biophysical and biological assays to determine the effects of glycation on the structure and function of mAb1. Glycation was detected at multiple lysine residues and reduced the antigen binding activity of mAb1. Heavy chain Lys100, which is located in the complementary-determining region of mAb1, had the highest levels of glycation in both stressed and unstressed samples, and glycation of this residue was likely responsible for the loss of antigen binding based on hydrogen/deuterium exchange mass spectrometry analysis. Peptide mapping and intact liquid chromatography-mass spectrometry (LC-MS) can both be used to monitor the glycation levels. Peptide mapping provides site specific glycation results, while intact LC-MS is a quicker and simpler method to quantitate the total glycation levels and is more useful for routine testing. Capillary isoelectric focusing (cIEF) can also be used to monitor glycation because glycation induces an acidic shift in the cIEF profile. As expected, total glycation measured by intact LC-MS correlated very well with the percentage of total acidic peaks or main peak measured by cIEF. In summary, we demonstrated that glycation can affect the function of a representative IgG1 mAb. The analytical characterization, as described here, should be generally applicable for other therapeutic mAbs.

Indexed as

AnimalsAntibodies, MonoclonalCHO CellsCricetulusDeuterium Exchange MeasurementGlycosylationHumansImmunoglobulin Heavy ChainsStructure-Activity RelationshipAntibodies, MonoclonalImmunoglobulin Heavy Chainsantigen bindingcIEFglycationHDX MSintact LC-MSMonoclonal antibodypeptide mappingstructural and function

Identifiers

PMID29436927
PMCPMC5916557
OpenAlexW2791547188

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.