ArticleMolecular & cellular proteomics : MCP2010
Post-translational modifications differentially affect IgG1 conformation and receptor binding.
Article in Molecular & cellular proteomics : MCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 172 papers, 1 of them a synthesis that pooled it.
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Who cites it
172 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Biosimilarity and Interchangeability: Principles and Evidence: A Systematic Review.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2018Pooled it
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- Harnessing deep learning to accelerate the development of antibodies and aptamers.Acta pharmaceutica Sinica. B · 2026Review
- CNS-compartmentalized IgG aggregates and glycosylation in multiple sclerosis contribute to oligoclonal bands and neuronal cytotoxicity.Frontiers in immunology · 2026Article
- Glycosylated IgG antibodies contribute to the recovery of haemorrhagic fever with renal syndrome patients.eLife · 2025Article
- Multiscale Computational Studies of PEG Chain Length Effects on HER2 mAb Fc Structure and Binding Energetics.ACS omega · 2025Article
- Structural and epitope characterization of anti-DEFA5 monoclonal antibodies clones 1A8 and 4F5 for inflammatory bowel disease subtype diagnostics.International journal of biological macromolecules · 2025Article
- Neutralizing Antibodies vs. Viruses: Interacting Mechanisms and Escape Tactics.Microorganisms · 2025Review
- Accelerating Characterization of Therapeutic Antibodies: A Comparative Assessment of icIEF-UV/MS and the Traditional Fractionation Workflow.Journal of the American Society for Mass Spectrometry · 2025Article
- Immunopeptidomics for autoimmunity: unlocking the chamber of immune secrets.NPJ systems biology and applications · 2025Review
- Advances and challenges in plant N-glycoengineering: when fucosylation matters.Frontiers in plant science · 2025Review
- Systematic Preparation of a 66-IgG Library with Symmetric and Asymmetric Homogeneous Glycans and Their Functional Evaluation.Journal of the American Chemical Society · 2024Article
- Enhanced N-Glycan Profiling of Therapeutic Monoclonal Antibodies through the Application of Upper-Hinge Middle-Up Level LC-HRMS Analysis.Antibodies (Basel, Switzerland) · 2024Article
- Characterization of the Charge Heterogeneity of a Monoclonal Antibody That Binds to Both Cation Exchange and Anion Exchange Columns under the Same Binding Conditions.Antibodies (Basel, Switzerland) · 2024Article
- Nutrient inputs and social metabolic control of T cell fate.Cell metabolism · 2024Review
- Article
- Regulatory considerations in the design, development and quality of monoclonal antibodies and related products for the diagnosis and treatment of cancer.Frontiers in oncology · 2024Review
- Immunomodulation of Antibody Glycosylation through the Placental Transfer.International journal of molecular sciences · 2023Review
- Enhancing Selectivity of Protein Biopharmaceuticals in Ion Exchange Chromatography through Addition of Organic Modifiers.International journal of molecular sciences · 2023Article
112 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
Funding
Abstract
Post-translational modifications (PTMs) can have profound effects on protein structure and protein dynamics and thereby can influence protein function. To understand and connect PTM-induced functional differences with any resulting conformational changes, the conformational changes must be detected and localized to specific parts of the protein. We illustrate these principles here with a study of the functional and conformational changes that accompany modifications to a monoclonal immunoglobulin gamma1 (IgG1) antibody. IgG1s are large and heterogeneous proteins capable of incorporating a multiplicity of PTMs both in vivo and in vitro. For many IgG1s, these PTMs can play a critical role in affecting conformation, biological function, and the ability of the antibody to initiate a potential adverse biological response. We investigated the impact of differential galactosylation, methionine oxidation, and fucosylation on solution conformation using hydrogen/deuterium exchange mass spectrometry and probed the effects of IgG1 binding to the FcgammaRIIIa receptor. The results showed that methionine oxidation and galactosylation both impact IgG1 conformation, whereas fucosylation appears to have little or no impact to the conformation. FcgammaRIIIa binding was strongly influenced by both the glycan structure/composition (namely galactose and fucose) and conformational changes that were induced by some of the modifications.
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