ArticlemAbs
Site-specific N- and O-glycosylation analysis of atacicept.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 30 citations in OpenAlex.
- Computational design of a glycosylated multi-epitope vaccine against HAsV-1 and HAsV-2 astrovirus for acute gastroenteritis.Scientific reports · 2025Article
- A chemoenzymatic method for simultaneous profiling N- and O-glycans on glycoproteins using one-pot format.Cell reports methods · 2024Article
- Immunoglobulin G glycosylation and its alterations in aging-related diseases.Acta biochimica et biophysica Sinica · 2024Review
- Comprehensive multi-attribute method workflow for biotherapeutic characterization and current good manufacturing practices testing.Nature protocols · 2023Review
- O-glycosylation and its role in therapeutic proteins.Bioscience reports · 2022Review
- An etanercept O-glycovariant with enhanced potency.Molecular therapy. Methods & clinical development · 2022Article
- Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021Review
- SerumJournal of clinical medicine · 2021Article
- Design and High Expression of Non-glycosylated Lysostaphins inFrontiers in microbiology · 2021Article
- Optimal Dissociation Methods Differ forJournal of proteome research · 2020Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Fc-fusion protein atacicept is currently under clinical investigation for its biotherapeutic application in autoimmune diseases owing to its ability to bind the two cytokines B-Lymphocyte Stimulator (BLyS) and A PRoliferation-Inducing Ligand (APRIL). Like typical recombinant IgG-based therapeutics, atacicept is a glycoprotein whose glycosylation-related heterogeneity arises from the glycosylation-site localization, site-specific occupation and structural diversity of the attached glycans. Here, we present a first comprehensive site-specific N- and O-glycosylation characterization of atacicept using mass spectrometry-based workflows. First, N- and O-glycosylation sites and their corresponding glycoforms were identified. Second, a relative quantitation of the N-glycosylation site microheterogeneity was achieved by glycopeptide analysis, which was further supported by analysis of the released N-glycans. We confirmed the presence of one N-glycosylation site, carrying 47 glycoforms covering 34 different compositions, next to two hinge region O-glycosylation sites with core 1-type glycans. The relative O-glycan distribution was analyzed based on the de-N-glycosylated intact protein species. Overall, N- and O-glycosylation were consistent between two individual production batches.
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Registered trials
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.