ArticleImmunity, inflammation and disease2014
A pilot study showing differences in glycosylation patterns of IgG subclasses induced by pneumococcal, meningococcal, and two types of influenza vaccines.
Article in Immunity, inflammation and disease, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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Who cites it
23 citing papers in PubMed, 37 citations in OpenAlex.
- Trial
- Endothelial cells sialylate IgG within the FcRn-mediated recycling pathway.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Multivariate analysis of glycogenes reveals coordinated regulation of immunoglobulin glycosylation in an immortalized human B cell system.bioRxiv : the preprint server for biology · 2025Article
- Nanolipoprotein particle (NLP) vaccine confers protection againstFrontiers in immunology · 2025Article
- Regulators of placental antibody transfer through a modeling lens.Nature immunology · 2024Review
- Review
- Unveiling the multifaceted landscape of N-glycosylation in antibody variable domains: Insights and implications.International journal of biological macromolecules · 2024Article
- Quantitative mechanistic model reveals key determinants of placental IgG transfer and informs prenatal immunization strategies.PLoS computational biology · 2023Article
- Comparative analysis of spike-specific IgG Fc glycoprofiles elicited by adenoviral, mRNA, and protein-based SARS-CoV-2 vaccines.iScience · 2023Article
- Afucosylated IgG responses in humans - structural clues to the regulation of humoral immunity.Trends in immunology · 2022Review
- A functional spleen contributes to afucosylated IgG in humans.Scientific reports · 2021Article
- Afucosylated Plasmodium falciparum-specific IgG is induced by infection but not by subunit vaccination.Nature communications · 2021Article
- Proatherogenic Sialidases and Desialylated Lipoproteins: 35 Years of Research and Current State from Bench to Bedside.Biomedicines · 2021Review
- Glycosylation of Antigen-Specific Antibodies: Perspectives on Immunoglobulin G Glycosylation in Vaccination and Immunotherapy.Experientia supplementum (2012) · 2021Article
- Sialylated Immunoglobulins for the Treatment of Immuno-Inflammatory Diseases.International journal of molecular sciences · 2020Review
- Understanding the role of antibody glycosylation through the lens of severe viral and bacterial diseases.Glycobiology · 2020Review
- Maternal Immunization: Nature Meets Nurture.Frontiers in microbiology · 2020Review
- Article
- Antibody glycosylation in inflammation, disease and vaccination.Seminars in immunology · 2018Review
- Differences in IgG Fc Glycosylation Are Associated with Outcome of Pediatric Meningococcal Sepsis.mBio · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The presence of a carbohydrate moiety on asparagine 297 in the Fc part of an IgG molecule is essential for its effector functions and thus influences its vaccine protective effect. Detailed structural carbohydrate analysis of vaccine induced IgGs is therefore of interest as this knowledge can prove valuable in vaccine research and design and when optimizing vaccine schedules. In order to better understand and exploit the protective potential of IgG antibodies, we carried out a pilot study; collecting serum or plasma from volunteers receiving different vaccines and determining the IgG subclass glycosylation patterns against specific vaccine antigens at different time points using LC-ESI-MS analysis. The four vaccines included a pneumococcal capsule polysaccharide vaccine, a meningococcal outer membrane vesicle vaccine, a seasonal influenza vaccine, and a pandemic influenza vaccine. The number of volunteers was limited, but the results following immunization indicated that the IgG subclass which dominated the response showed increased galactose and the level of sialic acid increased with time for most vaccinees. Fucose levels increased for some vaccinees but in general stayed relatively unaltered. The total background IgG glycosylation analyzed in parallel varied little with time and hence the changes seen were likely to be caused by vaccination. The presence of an adjuvant in the pandemic influenza vaccine seemed to produce simpler and less varied glycoforms compared to the adjuvant-free seasonal influenza vaccine. This pilot study demonstrates that detailed IgG glycosylation pattern analysis might be a necessary step in addition to biological testing for optimizing vaccine development and strategies.
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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.