Evidence map›Paper›PMID 19425533›Full record

ArticleBioconjugate chemistry2009

Site specific conjugation of fluoroprobes to the remodeled Fc N-glycans of monoclonal antibodies using mutant glycosyltransferases: application for cell surface antigen detection.

Elizabeth Boeggeman, Boopathy Ramakrishnan, Marta Pasek, Maria Manzoni, Anu Puri, Kristin H Loomis, Timothy J Waybright, Pradman K Qasba

Abstract read
In one paragraph

Article in Bioconjugate chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

44 citing papers in PubMed, 109 citations in OpenAlex.

  1. Article
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  6. Single Photon Emission Computed Tomography Tracer.Recent results in cancer research. Fortschritte der Krebsforschung. Progres dans les recherches sur le cancer · 2026
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  8. Review
  9. Site-Specific Modification of Native IgGs with Flexible Drug-Load.Chembiochem : a European journal of chemical biology · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. The Chemistry Behind ADCs.Pharmaceuticals (Basel, Switzerland) · 2021
    Review
  14. Recent Advances in the Chemical Biology ofMolecules (Basel, Switzerland) · 2021
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  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

8 authors at 1 institution in 1 country.

Elizabeth BoeggemanStructural Glycobiology Section, CCR-Nanobiology Program, SAIC-Frederick, Inc., Frederick, Maryland 21702, USA.
Boopathy Ramakrishnan
Marta Pasek
Maria Manzoni
Anu Puri
Kristin H Loomis
Timothy J Waybright
Pradman K Qasba
Science Applications International Corporation (United States) · US

Funding

Utilizing Glycosyltransferases for BioconjugationZIABC010742 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI QASBA, PRADMAN K · 2009 to 2013
$1.1M
Using Glycosyltransferases for Conjugation of Single-Chain Antibodies and LipidsZIABC010805 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI QASBA, PRADMAN K · 2009 to 2010
$509k
Intramural NIH HHS ZIA BC010742NCI NIH HHS N01 CO012400NCI NIH HHS N01-CO-12400
6 · The paper itself

Abstract

The Fc N-glycan chains of four therapeutic monoclonal antibodies (mAbs), namely, Avastin, Rituxan, Remicade, and Herceptin, released by PNGase F, show by MALDI analysis that these biantennary N-glycans are a mixture of G0, G1, and G2 glycoforms. The G0 glycoform has no galactose on the terminal GlcNAc residues, and the G1 and G2 glycoforms have one or two terminal galactose residues, respectively, while no N-glycan with terminal sialic acid residue is observed. We show here that under native conditions we can convert the N-glycans of these mAbs to a homogeneous population of G0 glycoform using beta1,4 galactosidase from Streptococcus pneumoniae. The G0 glycoforms of mAbs can be galactosylated with a modified galactose having a chemical handle at the C2 position, such as ketone or azide, using a mutant beta1,4-galactosyltransferase (beta1,4Gal-T1-Y289L). The addition of the modified galactose at a specific glycan residue of a mAb permits the coupling of a biomolecule that carries an orthogonal reactive group. The linking of a biotinylated or a fluorescent dye carrying derivatives selectively occurs with the modified galactose, C2-keto-Gal, at the heavy chain of these mAbs, without altering their antigen binding activities, as shown by indirect enzyme linked immunosorbent assay (ELISA) and fluorescence activated cell sorting (FACS) methods. Our results demonstrate that the linking of cargo molecules to mAbs via glycans could prove to be an invaluable tool for potential drug targeting by immunotherapeutic methods.

Indexed as

AnimalsAntibodies, MonoclonalAntigens, SurfaceBinding SitesBiotinylationCell Line, TumorEnzyme-Linked Immunosorbent AssayErb-b2 Receptor Tyrosine KinasesFluorescent DyesGalactoseGlucosamineGlycosylationGlycosyltransferasesHumansImmunoglobulin GMutant ProteinsAntibodies, MonoclonalAntigens, SurfaceErb-b2 Receptor Tyrosine KinasesFluorescent DyesGalactoseGlucosamineGlycosyltransferasesImmunoglobulin GMutant ProteinsOligosaccharidesPolysaccharidesVascular Endothelial Growth Factor A

Identifiers

PMID19425533
PMCPMC3464487
OpenAlexW2008652440

What OpenQuestion holds

Textmetadata
LicenceTDM
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.