Afucosylated IgG characterizes enveloped viral responses and correlates with COVID-19 severity.
Science
; 371(6532)2021 02 26.
Article
in English
| MEDLINE | ID: covidwho-1066801
ABSTRACT
Immunoglobulin G (IgG) antibodies are crucial for protection against invading pathogens. A highly conserved N-linked glycan within the IgG-Fc tail, which is essential for IgG function, shows variable composition in humans. Afucosylated IgG variants are already used in anticancer therapeutic antibodies for their increased activity through Fc receptors (FcγRIIIa). Here, we report that afucosylated IgG (approximately 6% of total IgG in humans) are specifically formed against enveloped viruses but generally not against other antigens. This mediates stronger FcγRIIIa responses but also amplifies brewing cytokine storms and immune-mediated pathologies. Critically ill COVID-19 patients, but not those with mild symptoms, had high concentrations of afucosylated IgG antibodies against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), amplifying proinflammatory cytokine release and acute phase responses. Thus, antibody glycosylation plays a critical role in immune responses to enveloped viruses, including COVID-19.
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Immunoglobulin G
/
SARS-CoV-2
/
COVID-19
/
Antibodies, Viral
Type of study:
Prognostic study
Topics:
Vaccines
/
Variants
Limits:
Adult
/
Aged
/
Female
/
Humans
/
Male
/
Middle aged
/
Young adult
Language:
English
Year:
2021
Document Type:
Article
Affiliation country:
Science.abc8378
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