ArticlemAbs
The impact of glycosylation on monoclonal antibody conformation and stability.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 141 papers.
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Who cites it
141 citing papers in PubMed.
- Article
- 2D NMR assessment of structural consistency and functional relationships in monoclonal antibodies.mAbs · 2026Article
- Human monoclonal antibodies targeting α-Gal restrict IgE engagement of α-Gal syndrome allergens.The Journal of clinical investigation · 2026Article
- Development and preliminary physicochemical characterization of a Ramucirumab biosimilar candidate in CHO cells using shake-flask fed-batch culture.Bioprocess and biosystems engineering · 2026Article
- Orthogonal Conjugation via Endoglycosidase and Microbial Transglutaminase Enables Efficient Synthesis of Dual-Payload Antibody-Drug Conjugates.ACS chemical biology · 2026Article
- Recommendations and considerations for hydroxyl radical protein footprinting-mass spectrometry.Nature methods · 2026Review
- Effect of ADCC-enhancing mutations on N-glycan profiles of human IgG1 antibodies.The Biochemical journal · 2026Article
- Online Deglycosylation of Monomeric Intact Proteins Using the PNGase Rc Immobilized-Enzyme Reactor.ACS omega · 2026Article
- Directional conjugation of monoclonal antibodies to nanoparticles using metal-free click chemistry.Nature protocols · 2026Review
- Biophysical trade-offs in antibody evolution are resolved by conformation-mediated epistasis.bioRxiv : the preprint server for biology · 2026Article
- Review
- Robustness Evaluation of a Legacy N-Glycan Profiling Method for a Therapeutic Antibody Under ICH Q14 Lifecycle Principles.Antibodies (Basel, Switzerland) · 2026Article
- Antibody display technologies from phages to cells: translational bottlenecks and AI-enabled opportunities.Frontiers in bioengineering and biotechnology · 2026Review
- Architects of folding, editors of immunity: the strategic use ofFrontiers in immunology · 2026Article
- Comparative Analysis of Glycan Composition in Therapeutic Antibodies via Glycan Profiling and Intact Mass Analysis.Molecules (Basel, Switzerland) · 2025Article
- Review
- Article
- Establishment of reference intervals for serum immunoglobulin GThe EPMA journal · 2025Article
- The impact of Fc glycosylation on IgG susceptibility to hinge region chemical reduction: implications for the development of immunoassays.Biochemistry and biophysics reports · 2025Article
- Highly variable aggregation and glycosylation profiles and their roles in immunogenicity to protein-based therapeutics.Journal of pharmaceutical sciences · 2025Review
81 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antibody glycosylation is a common post-translational modification and has a critical role in antibody effector function. The use of glycoengineering to produce antibodies with specific glycoforms may be required to achieve the desired therapeutic efficacy. However, the modified molecule could have unusual behavior during development due to the alteration of its intrinsic properties and stability. In this study, we focused on the differences between glycosylated and deglycosylated antibodies, as aglycosyl antibodies are often chosen when effector function is not desired or unimportant. We selected three human IgG1 antibodies and used PNGase F to remove their oligosaccharide chains. Although there were no detected secondary or tertiary structural changes after deglycosylation, other intrinsic properties of the antibody were altered with the removal of oligosaccharide chains in the Fc region. The apparent molecular hydrodynamic radius increased after deglycosylation based on size-exclusion chromatography analysis. Deglycosylated antibodies exhibited less thermal stability for the CH2 domain and less resistance to GdnHCl induced unfolding. Susceptibility to proteolytic cleavage demonstrated that the deglycosylated version was more susceptible to papain. An accelerated stability study revealed that deglycosylated antibodies had higher aggregation rates. These changes may impact the development of aglycosyl antibody biotherapeutics.
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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.