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2017 ; 29
(7
): 303-310
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Diversification of IgG effector functions
#MMPMID28472280
Bournazos S
; Ravetch JV
Int Immunol
2017[Jul]; 29
(7
): 303-310
PMID28472280
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IgG is the major immunoglobulin class produced during an immune response against
foreign antigens and efficiently provides protection through its bifunctional
nature. While the Fab domains confer highly specific recognition of the antigen,
the Fc domain mediates a wide range of effector functions that modulate several
aspects of innate and adaptive immunity. Engagement of the various types of Fc?
receptors (Fc?Rs) by an IgG Fc domain can activate distinct immunomodulatory
pathways with pleiotropic functional consequences for several leukocyte types. Fc
effector functions are not limited to phagocytosis and cytotoxicity of
IgG-opsonized targets but exhibit remarkable diversity and include modulation of
leukocyte activity and survival, cytokine and chemokine expression, maturation of
antigen-presenting cells, antigen processing and presentation, B-cell selection
and IgG affinity maturation, as well as regulation of IgG production. These
functions are initiated upon specific interactions of the Fc domain with the
various types of Fc?Rs-a process that is largely determined by the structural
heterogeneity of the IgG Fc domain. Modulation of the Fc-associated glycan
structure and composition along with differences in the primary amino acid
sequence among the IgG subclasses represent the two main diversification
mechanisms of the Fc domain that generate a spectrum of Fc domain phenotypes with
distinct affinity for the various Fc?R types and differential capacity to
activate immunomodulatory pathways.
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