IgG Subclasses and Allotypes: From Structure to Effector Functions
Open accessAbstract
Of the five immunoglobulin isotypes, immunoglobulin G (IgG) is most abundant in human serum. The four subclasses, IgG1, IgG2, IgG3, and IgG4, which are highly conserved, differ in their constant region, particularly in their hinges and upper CH2 domains. These regions are involved in binding to both IgG-Fc receptors (FcγR) and C1q. As a result, the different subclasses have different effector functions, both in terms of triggering FcγR-expressing cells, resulting in phagocytosis or antibody-dependent cell-mediated cytotoxicity, and activating complement. The Fc-regions also contain a binding epitope for the neonatal Fc receptor (FcRn), responsible for the extended half-life, placental transport, and bidirectional transport of IgG to mucosal surfaces. However, FcRn is also expressed in myeloid cells, where it participates in both phagocytosis and antigen presentation together with classical FcγR and complement. How these properties, IgG-polymorphisms and post-translational modification of the antibodies in the form of glycosylation, affect IgG-function will be the focus of the current review.
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In one of the first studies, a shift of the peak levels of systemic IL-6 and TNF from nighttime to daytime was observed in 11 individuals with insomnia without concomitant mental disorders, compared with healthy age- and body-mass index-matched control participants.
“a shift of the peak levels of systemic IL-6 and TNF from nighttime to daytime was observed in 11 individuals with insomnia without concomitant mental disorders, compared with healthy age- and body-mass index-matched control participants”
From The Sleep-Immune Crosstalk in Health and Disease (2019) · cites this paper as [565]
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- Authors
- Vidarsson, G., Dekkers, G., & Rispens, T.
- Affiliations
- Amsterdam UMC Location University of Amsterdam (NL)
- Corresponding author
- Vidarsson, Gestur
- Venue
- Frontiers in Immunology
- Publisher
- Frontiers Media SA
- Published
- 2014-10-20
- Volume
- 5
- Pages
- 520-520
- ISSN
- 1664-3224 (ISSN-L)
- PMC
- PMC4202688
- OpenAlex
- W2169656611
- Cited by
- 2,667
- References
- 219
- Citations by year
- 2026: 228 · 2025: 261 · 2024: 288 · 2023: 315 · 2022: 309 · 2021: 289 · 2020: 270 · 2019: 219 · 2018: 176 · 2017: 148 · 2016: 118 · 2015: 41
- FWCI
- 15.92
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Frontiers in Immunology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Pure Amsterdam UMC (submittedVersion)
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Life Sciences › Immunology and Microbiology › Immunology › Immunodeficiency and Autoimmune Disorders
- Keywords
- IgG subclasses, IgG allotypes, hinge region, CH2 domain, Fc gamma receptor, C1q, antibody-dependent cellular cytotoxicity, phagocytosis, complement activation, neonatal Fc receptor, antibody half-life, placental transport, antibody glycosylation, antigen presentation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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