Evidence map›Paper›PMID 42890387›Full record

ArticleAAPS open2026

Second-generation lectin microarray for high throughput glycan profiling of therapeutic antibodies.

Kayla Hess, Helena Yun, Shen Luo, Uriel Ortega-Rodriguez, Grace Henry Lunde, Sarah Rogstad, Lai-Xi Wang, Baolin Zhang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in AAPS open, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Kayla HessOffice of Pharmaceutical Quality Research, Office of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20993, United States.
Helena YunDepartment of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742.
Shen LuoOffice of Pharmaceutical Quality Research, Office of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20993, United States.
Uriel Ortega-RodriguezOffice of Pharmaceutical Quality Research, Office of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20993, United States.
Grace Henry LundeDepartment of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742.
Sarah RogstadOffice of Pharmaceutical Quality Research, Office of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20993, United States.
Lai-Xi WangDepartment of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742.
Baolin ZhangOffice of Pharmaceutical Quality Research, Office of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20993, United States.

Funding

Glycoengineering of antibodies to modulate immune functionsR01AI155716 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI LAI-XI WANG · 2020 to 2026
$3.6M
Intramural FDA HHS FD999999NIAID NIH HHS R01 AI155716
6 · The paper itself

Abstract

N-linked glycosylation is a critical quality attribute of therapeutic monoclonal antibodies (mAbs), influencing efficacy, safety, and pharmacokinetics. Accurate and high-throughput glycan profiling is therefore critical for product quality and manufacturing consistency. Here, we evaluated a novel lectin microarray platform for the detection of glycan epitopes commonly present in therapeutic antibodies. To assess specificity and performance, a panel of anti-HER2 mAbs with uniform glycan structures was generated via chemoenzymatic glycoengineering. These antibodies were analyzed in parallel by lectin microarray profiling of intact antibodies and mass spectrometry-based characterization of released glycans. Results from both approaches were highly concordant, demonstrating the lectin microarray's semi-quantitative capability for accurate glycan profiling. Further studies confirmed the platform's dynamic range and intermediate precision. Evaluation with the adalimumab reference product and eight biosimilars further confirmed its utility as a complementary tool for therapeutic antibody characterization. Collectively, these findings established the lectin microarray as a robust, high-throughput method for glycan analysis in therapeutic antibody development.

Indexed as

biosimilar assessmentglycan analysisglycan profilehigh throughputlectin microarraymass spectrometrymethod verificationmonoclonal antibody

Identifiers

PMID42890387
PMCPMC13671424

What OpenQuestion holds

Textmetadata
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.