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RIII (CD16)1
*
Department of Immunology and
Medarex Europe, University Hospital Utrecht, Utrecht, The Netherlands;
Department of Clinical Immunology, Medical School Hannover, Hannover, Germany; and
§
Department of Cell Biology and Immunology, Free University, Amsterdam, The Netherlands
Previously, we have demonstrated that phagocytosis of IgG1-coated
particles by macrophages in vitro is impaired by deletion of Fc
RIII
in mice, suggesting that IgG1 may interact preferentially with
FcRIII. In the present study, the biologic relevance of this
observation was addressed by triggering various effector functions of
the immune system in FcRIII-/- mice, using panels of
mAbs of different IgG subclasses. Both binding and phagocytosis of
IgG1-coated sheep or human erythrocytes by FcRIII-/-
macrophages in vitro were strongly impaired, indicating that the
impaired ingestion of complexed IgG1 by FcRIII-/-macrophages is due to a defect in binding. An in vivo
consequence of the defective phagocytosis was observed by resistance of
FcRIII-deficient mice to experimental autoimmune hemolytic anemia,
as shown by a lack of IgG1-mediated erythrophagocytosis in vivo by
liver macrophages. Furthermore, trapping of soluble IgG1-containing
immune complexes by follicular dendritic cells in mesenteric lymph
nodes from FcRIII-/- mice was abolished. Whole blood
from FcRIII-/- mice was unable to induce lysis of
tumor cells in the presence of IgG1 antitumor Abs. Finally, IgG1 mAbs
proved unable to mount a passive cutaneous anaphylaxis in
FcRIII-/- mice. Together, these results demonstrate
that IgG1 complexes, either in particulate or in soluble form, trigger
in vitro and in vivo immune effector functions in mice predominantly
via FcRIII.
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