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Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Science 2021 ; 371 (6532): ä Nephropedia Template TP
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Afucosylated IgG characterizes enveloped viral responses and correlates with COVID-19 severity #MMPMID33361116
Larsen MD; de Graaf EL; Sonneveld ME; Plomp HR; Nouta J; Hoepel W; Chen HJ; Linty F; Visser R; Brinkhaus M; Sustic T; de Taeye SW; Bentlage AEH; Toivonen S; Koeleman CAM; Sainio S; Kootstra NA; Brouwer PJM; Geyer CE; Derksen NIL; Wolbink G; de Winther M; Sanders RW; van Gils MJ; de Bruin S; Vlaar APJ; Rispens T; den Dunnen J; Zaaijer HL; Wuhrer M; Ellen van der Schoot C; Vidarsson G
Science 2021[Feb]; 371 (6532): ä PMID33361116show ga
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 (FcgammaRIIIa). 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 FcgammaRIIIa 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.