Afucosylated IgG responses in humans - structural clues to the regulation of humoral immunity.
Trends Immunol
; 43(10): 800-814, 2022 10.
Article
in English
| MEDLINE | ID: covidwho-1996295
ABSTRACT
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.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Immunity, Humoral
/
COVID-19
Topics:
Vaccines
Limits:
Humans
Language:
English
Journal:
Trends Immunol
Journal subject:
Allergy and Immunology
Year:
2022
Document Type:
Article
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