Table 2.

Summary of FcR effector responses elicited by IgG binding. IgG N-glycosylation of the Fc domain is directly linked to changes in affinity for FcRs that either produce more pro-inflammatory responses (ADCC) or anti-inflammatory responses (immune modulation). Anti-inflammatory activity is said to be dominant.

Effector Response	Immune Cells	Inflammation	Relation to IgG	Ref (1st Author)
Cytokines - Molecules with hormone-like function	All	Both	Altered IgG glycosylation may be linked to changes in cytokine expression	Lin (1995) [64]
Degranulation - Release of antimicrobial cytotoxic agents	Mast Cells, Basophils, Neutrophils, Eosinophils, Cytotoxic T Cells, NK Cells	Pro	↑ Fcγ-RI binding = ↑ degranulation, thus ↑ localised inflammation	Woolhiser (2001) [56]
Phagocytosis - Recognising & engulfing large particles or cells opsonised by C3b or IC, or amassed IC	Mast Cells, Basophils, Neutrophils, Eosinophils, Macrophages	Pro	↑ Fc binding can lead to ↑ localised inflammation	Quast (2014) [6], Russell (2009) [65]
ADCC - Cell lysis mediated by cytotoxic granules containing perforin & granzymes	NK Cells, Macrophages, Monocytes, Neutrophils, Eosinophils	Pro	↓ core fucosylated/sialylated IgG = ↑ Fcγ-RIIIa binding = ↑ ADCC Overall, this leads to ↑ localised inflammation/cell apoptosis	Nimmerjahn (2005) [38], Quast (2014) [6]
Immune Modulation - Upregulation of Fcγ-RIIb, which dominantly inhibits activating FcR	All	Anti	↑ sialylated IgG = ↑ Fcγ-RIIb binding Overall, this leads to ↑ anti-inflammatory activity	Pincetic (2014) [15], Schwab (2013) [4], Sondermann (2013) [52]

=, “leads to” or equal to; ↑, increased; ↓, decreased.