ReviewFrontiers in chemistry2022
Advances in IgA glycosylation and its correlation with diseases.
Review in Frontiers in chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.
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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.
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Who cites it
39 citing papers in PubMed, 1 synthesis or guideline pooled it, 61 citations in OpenAlex.
- S100 proteins in IgA vasculitis and other systemic vasculitides - from pathogenic mechanisms to clinical biomarkers: a systematic review.Frontiers in immunology · 2026Pooled it
- Label-Free Profiling of Immunoglobulin Isotypes Using Solid-State Nanopores.Small methods · 2026Article
- Structural promiscuity in the human circulatory IgA1 clonal repertoire.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Multiplex Detection of Immunoglobulins Uncovers Intrathecal IgA Elevation in Multiple Sclerosis.Cells · 2026Article
- The hidden language of gut-derived lipopolysaccharides: fine chemistry, huge immunological consequences.Chemical science · 2026Review
- Fc Profiling of Polyclonal IgG, IgA and IgM by Light Chain Capturing Coupled with NanoRP-LC-MS.JACS Au · 2026Article
- FUT2-mediated intestinal fucosylation: a master regulator of host-microbiota symbiosis in health and disease.Frontiers in microbiology · 2026Review
- Article
- N-Glycosylation of Antibodies: Biological Effects During Infections and Therapeutic Applications.Antibodies (Basel, Switzerland) · 2025Review
- Anti-SARS-CoV-2 Spike IgA2 Induces Inflammation by Human Macrophages.European journal of immunology · 2025Article
- In-depth analysis of the tear fluid glycoproteome reveals diverse lacritin glycosylation and spliceoforms.The Journal of biological chemistry · 2025Article
- The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025Review
- In-depth analysis of the tear fluid glycoproteome reveals diverse lacritin glycosylation and spliceoforms.bioRxiv : the preprint server for biology · 2025Article
- Nasal delivery of secretory IgA confers enhanced neutralizing activity against Omicron variants compared to its IgG counterpart.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Article
- Antibody Aggregation: A Problem Within the Biopharmaceutical Industry and Its Role in AL Amyloidosis Disease.The protein journal · 2025Review
- The role ofFrontiers in immunology · 2025Article
- Aberrant glycosylation patterns as potential biomarkers for diagnosis and disease progression in bullous pemphigoid.Frontiers in immunology · 2025Article
- Targeting mucosal immunity in malaria control: the underexplored role of IgA.Frontiers in malaria · 2025Article
- AsymmetricJournal of the American Chemical Society · 2024Article
- The role of antibody glycosylation in autoimmune and alloimmune kidney diseases.Nature reviews. Nephrology · 2024Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Immunoglobulin A (IgA) is the most abundant immunoglobulin synthesized in the human body. It has the highest concentration in the mucosa and is second only to IgG in serum. IgA plays an important role in mucosal immunity, and is the predominant antibody used to protect the mucosal surface from pathogens invasion and to maintain the homeostasis of intestinal flora. Moreover, The binding IgA to the FcαRI (Fc alpha Receptor I) in soluble or aggregated form can mediate anti- or pro- inflammatory responses, respectively. IgA is also known as one of the most heavily glycosylated antibodies among human immunoglobulins. The glycosylation of IgA has been shown to have a significant effect on its immune function. Variation in the glycoform of IgA is often the main characteration of autoimmune diseases such as IgA nephropathy (IgAN), IgA vasculitis (IgAV), systemic lupus erythematosus (SLE), and rheumatoid arthritis (RA). However, compared with the confirmed glycosylation function of IgG, the pathogenic mechanism of IgA glycosylation involved in related diseases is still unclear. This paper mainly summarizes the recent reports on IgA's glycan structure, its function, its relationship with the occurrence and development of diseases, and the potential application of glycoengineered IgA in clinical antibody therapeutics, in order to provide a potential reference for future research in this field.
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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.