ReviewFrontiers in immunology2026
Immunoglobulin G N-glycosylation remodeling in viral infections: immunomodulatory roles and potential biomarker implications.
Review in Frontiers in immunology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Counteracting Influenza Virus Evolution Through the Full Spectrum of Broadly Protective Antibodies.Immunological reviews · 2026Review
- Fc effector functions in RNA viral infections: mechanisms of antiviral immunity and implications for vaccine design.Frontiers in immunology · 2026Review
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glycosylation of Immunoglobulin G (IgG), a complex post-translational modification, is essential for the structure and function of IgG. The varying affinities of different IgG N-glycans for Fcγ receptors can influence inflammatory responses, including antibody-dependent cell-mediated cytotoxicity (ADCC), complement-dependent cytotoxicity (CDC), and antibody-dependent cell phagocytosis (ADCP). Existing research indicates a correlation between IgG N-glycosylation and a range of diseases, such as autoimmune disorders, neurologic diseases, and cancer. Persistent and emerging viral infections pose a significant risk to public health, and the elicitation of innate and adaptive immune responses in the host following viral infection is intricately linked to inflammatory mediators, yet the relationship between viral infections and IgG N-glycosylation has not been systematically explored. In this review, we delineate the typical immune response to viral infection, expound on the structure and functionality of IgG N-glycans, and summarize the alterations in IgG N-glycans in human serum/plasma post-viral infection, along with the underlying inducements for these modifications. These alterations could serve as biomarkers for viral infectious diseases, thereby facilitating early detection and prognostic assessment of such conditions. Furthermore, exploring these modifications may elucidate the molecular mechanisms underlying the diseases and identify novel therapeutic targets.
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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.