Evidence map›Paper›PMID 26514686›Full record

ArticlemAbs2016

Evaluation of a glycoengineered monoclonal antibody via LC-MS analysis in combination with multiple enzymatic digestion.

Renpeng Liu, John Giddens, Colleen M McClung, Paula E Magnelli, Lai-Xi Wang, Ellen P Guthrie

Open access · goldAbstract read
In one paragraph

Article in mAbs, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

10 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Glycosylation of Therapeutic Proteins: A Critical Quality Attribute.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  4. Chemoenzymatic Synthesis of HIV-1 Glycopeptide Antigens.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Implementation of Glycan Remodeling to Plant-Made Therapeutic Antibodies.International journal of molecular sciences · 2018
    Article
  10. 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 1 country.

Renpeng Liua New England Biolabs Inc. , Ipswich , MA 01938.
John Giddensb Department of Chemistry & Biochemistry ; University of Maryland , College Park , MD 20742.
Colleen M McClunga New England Biolabs Inc. , Ipswich , MA 01938.
Paula E Magnellia New England Biolabs Inc. , Ipswich , MA 01938.
Lai-Xi Wangb Department of Chemistry & Biochemistry ; University of Maryland , College Park , MD 20742.
Ellen P Guthriea New England Biolabs Inc. , Ipswich , MA 01938.
New England Biolabs (United States) · USUniversity of Maryland, College Park · US

Funding

Synthesis and Function of Antibody Fc Domain GlycoformsR01GM096973 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI WANG, LAI-XI · 2011 to 2020
$2.4M
NIGMS NIH HHS R01 GM096973
6 · The paper itself

Abstract

Glycosylation affects the efficacy, safety and pharmacokinetics/pharmacodynamics properties of therapeutic monoclonal antibodies (mAbs), and glycoengineering is now being used to produce mAbs with improved efficacy. In this work, a glycoengineered version of rituximab was produced by chemoenzymatic modification to generate human-like N-glycosylation with α 2,6 linked sialic acid. This modified rituximab was comprehensively characterized by liquid chromatography-mass spectrometry and compared to commercially available rituximab. As anticipated, the majority of N-glycans were converted to α 2,6 linked sialic acid, in contrast to CHO-produced rituximab, which only contains α 2,3 linked sialic acid. Typical posttranslational modifications, such as pyro-glutamic acid formation at the N-terminus, oxidation at methionine, deamidation at asparagine, and disulfide linkages were also characterized in both the commercial and glycoengineered mAbs using multiple enzymatic digestion and mass spectrometric analysis. The comparative study reveals that the glycoengineering approach does not cause any additional posttranslational modifications in the antibody except the specific transformation of the glycoforms, demonstrating the mildness and efficiency of the chemoenzymatic approach for glycoengineering of therapeutic antibodies.

Indexed as

Mass SpectrometryAnimalsCHO CellsCricetinaeCricetulusGlycosylationHumansN-Acetylneuraminic AcidRituximabN-Acetylneuraminic AcidRituximabantibody characterizationglycoengineeringglycosylation analysisLC-MSprocainamide

Identifiers

PMID26514686
PMCPMC4966608
OpenAlexW1844979451

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.