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*
Divison of Infectious Diseases, University of Geneva, Switzerland;
Department for Medical Microbiology, University of Linköping, Sweden; and
European Molecular Biology Laboratory Mouse Biology Program, Monterotondo, Italy
Phagocytosis and the microbicidal functions of neutrophils require
dynamic changes of the actin cytoskeleton. We have investigated the
role of gelsolin, a calcium-dependent actin severing and capping
protein, in peripheral blood neutrophils from gelsolin-null
(Gsn-) mice. The phagocytosis of complement
opsonized yeast was only minimally affected. In contrast, phagocytosis
of IgG-opsonized yeast was reduced close to background level in
Gsn- neutrophils. Thus, gelsolin is
essential for efficient IgG- but not complement-mediated phagocytosis.
Furthermore, attachment of IgG-opsonized yeast to
Gsn- neutrophils was reduced (
50%) but
not to the same extent as ingestion (73%). This was not due to
reduced surface expression of the Fc
-receptor or its lateral
mobility. This suggests that attachment and ingestion of IgG-opsonized
yeast by murine neutrophils are actin-dependent and gelsolin is
important for both steps in phagocytosis. We also investigated granule
exocytosis and several steps in phagosome processing, namely the
formation of actin around the phagosome, translocation of granules, and
activation of the NADPH-oxidase. All these functions were normal in
Gsn- neutrophils. Thus, the role of
gelsolin is specific for IgG-mediated phagocytosis. Our data suggest
that gelsolin is part of the molecular machinery that distinguishes
complement and IgG-mediated phagocytosis. The latter requires a more
dynamic reorganization of the cytoskeleton.
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