Evidence map›Paper›PMID 36304448›Full record

ArticleFrontiers in immunology2022

Specific location of galactosylation in an afucosylated antiviral monoclonal antibody affects its FcγRIIIA binding affinity.

Grayson Hatfield, Lioudmila Tepliakova, Genevieve Gingras, Andrew Stalker, Xuguang Li, Yves Aubin, Roger Y Tam

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

14 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Selective fluorination of Fc glycans enhances antibody-mediated effector functions.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Exploring glycoform-dependent dynamic modulations in human immunoglobulin G via computational and experimental approaches.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Review
  12. Review
  13. Review
  14. 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

7 authors at 1 institution in 1 country.

Grayson HatfieldCentre for Oncology, Radiopharmaceuticals and Research, Biologics and Radiopharmaceutical Drugs Directorate, Health Canada, Ottawa, ON, Canada.
Lioudmila TepliakovaCentre for Oncology, Radiopharmaceuticals and Research, Biologics and Radiopharmaceutical Drugs Directorate, Health Canada, Ottawa, ON, Canada.
Genevieve GingrasCentre for Oncology, Radiopharmaceuticals and Research, Biologics and Radiopharmaceutical Drugs Directorate, Health Canada, Ottawa, ON, Canada.
Andrew StalkerCentre for Oncology, Radiopharmaceuticals and Research, Biologics and Radiopharmaceutical Drugs Directorate, Health Canada, Ottawa, ON, Canada.
Xuguang LiCentre for Oncology, Radiopharmaceuticals and Research, Biologics and Radiopharmaceutical Drugs Directorate, Health Canada, Ottawa, ON, Canada.
Yves AubinCentre for Oncology, Radiopharmaceuticals and Research, Biologics and Radiopharmaceutical Drugs Directorate, Health Canada, Ottawa, ON, Canada.
Roger Y TamCentre for Oncology, Radiopharmaceuticals and Research, Biologics and Radiopharmaceutical Drugs Directorate, Health Canada, Ottawa, ON, Canada.
Health Canada · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Monoclonal antibodies (mAbs) comprise an essential type of biologic therapeutics and are used to treat diseases because of their anti-cancer and anti-inflammatory properties, and their ability to protect against respiratory infections. Its production involves post-translational glycosylation, a biosynthetic process that conjugates glycans to proteins, which plays crucial roles in mAb bioactivities including effector functions and pharmacokinetics. These glycans are heterogeneous and have diverse chemical structures whose composition is sensitive to manufacturing conditions, rendering the understanding of how specific glycan structures affect mAb bioactivity challenging. There is a need to delineate the effects of specific glycans on mAb bioactivity to determine whether changes in certain glycosylation profiles (that can occur during manufacturing) will significantly affect product quality. Using enzymatic transglycosylation with chemically-defined

Indexed as

Antibodies, MonoclonalGalactoseAntibodies, ViralAntibody-Dependent Cell CytotoxicityAntiviral AgentsPolysaccharidesAntibodies, MonoclonalAntibodies, ViralAntiviral AgentsGalactosePolysaccharides2D NMReffector activityglycosylationmonoclonal antibodystructure-function activity

Identifiers

PMID36304448
PMCPMC9596277
OpenAlexW4304606589

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.