Afucosylated IgG responses in humans – structural clues to the regulation of humoral immunity

Janita J. Oosterhoff, Mads Delbo Larsen, C. Ellen van der Schoot, Gestur Vidarsson*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review


Healthy immune responses require efficient protection without excessive inflammation. Recent discoveries on the degree of fucosylation of a human N-linked glycan at a conserved site in the immunoglobulin IgG-Fc domain might add an additional regulatory layer to adaptive humoral immunity. Specifically, afucosylation of IgG-Fc enhances the interaction of IgG with FcγRIII and thereby its activity. Although plasma IgG is generally fucosylated, afucosylated IgG is raised in responses to enveloped viruses and Plasmodium falciparum proteins expressed on infected erythrocytes, as well as during alloimmune responses. Moreover, while afucosylation can exacerbate some infectious diseases (e.g., COVID-19), it also correlates with traits of protective immunity against malaria and HIV-1. Herein we discuss the implications of IgG afucosylation for health and disease, as well as for vaccination.

Original languageEnglish
Pages (from-to)800-814
Number of pages15
JournalTrends in Immunology
Issue number10
Publication statusPublished - Oct 2022


  • complement
  • Fc-receptors
  • fucosylation
  • galactosylation
  • glycosylation
  • humoral immunity
  • IgG antibodies


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