The Emerging Importance of IgG Fab Glycosylation in Immunity | Zendy

Fleur S. van de Bovenkamp | Zendy; Lise Hafkenscheid | Zendy; Theo Rispens | Zendy; Yoann Rombouts | Zendy

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The Emerging Importance of IgG Fab Glycosylation in Immunity

Author(s) -

Fleur S. van de Bovenkamp,

Lise Hafkenscheid,

Theo Rispens,

Yoann Rombouts

Publication year - 2016

Publication title -

the journal of immunology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.737

H-Index - 372

eISSN - 1550-6606

pISSN - 0022-1767

DOI - 10.4049/jimmunol.1502136

Subject(s) - somatic hypermutation , glycosylation , glycan , n linked glycosylation , fragment crystallizable region , glycoprotein , antibody , immunology , immunoglobulin g , immunoglobulin d , glycoproteomics , immunity , biology , chemistry , immune system , b cell , microbiology and biotechnology , biochemistry

Human IgG is the most abundant glycoprotein in serum and is crucial for protective immunity. In addition to conserved IgG Fc glycans, ∼15-25% of serum IgG contains glycans within the variable domains. These so-called "Fab glycans" are primarily highly processed complex-type biantennary N-glycans linked to N-glycosylation sites that emerge during somatic hypermutation. Specific patterns of Fab glycosylation are concurrent with physiological and pathological conditions, such as pregnancy and rheumatoid arthritis. With respect to function, Fab glycosylation can significantly affect stability, half-life, and binding characteristics of Abs and BCRs. Moreover, Fab glycans are associated with the anti-inflammatory activity of IVIgs. Consequently, IgG Fab glycosylation appears to be an important, yet poorly understood, process that modulates immunity.

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