Human anti-peptidoglycan-IgG-mediated opsonophagocytosis is controlled by calcium mobilization in phorbol myristate acetate-treated U937 cells
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Recently, we demonstrated that human serum amyloid Pcomponent (SAP) specifically recognizes exposed bacterialpeptidoglycan (PGN) of wall teichoic acid (WTA)-deficientStaphylococcus aureus ΔtagO mutant cells and then inducescomplement-independent phagocytosis. In our preliminaryexperiments, we found the existence of human serumimmunoglobulins that recognize S. aureus PGN (anti-PGNIgGs),which may be involved in complement-dependentopsonophagocytosis against infected S. aureus cells. Weassumed that purified serum anti-PGN-IgGs and S. aureusΔtagO mutant cells are good tools to study the molecularmechanism of anti-PGN-IgG-mediated phagocytosis. Therefore,we tried to identify the intracellular molecule(s) that is involvedin the anti-PGN-IgG-mediated phagocytosis using purifiedhuman serum anti-PGN-IgGs and different S. aureus mutantcells. Here, we show that anti-PGN-IgG-mediated phagocytosisin phorbol myristate acetate-treated U937 cells is mediated byCa2+ release from intracellular Ca2+ stores and anti-PGN-IgGdependentCa2+ mobilization is controlled via a phospholipaseCγ-2-mediated pathway.
Abstract
Recently, we demonstrated that human serum amyloid Pcomponent (SAP) specifically recognizes exposed bacterialpeptidoglycan (PGN) of wall teichoic acid (WTA)-deficientStaphylococcus aureus ΔtagO mutant cells and then inducescomplement-independent phagocytosis. In our preliminaryexperiments, we found the existence of human serumimmunoglobulins that recognize S. aureus PGN (anti-PGNIgGs),which may be involved in complement-dependentopsonophagocytosis against infected S. aureus cells. Weassumed that purified serum anti-PGN-IgGs and S. aureusΔtagO mutant cells are good tools to study the molecularmechanism of anti-PGN-IgG-mediated phagocytosis. Therefore,we tried to identify the intracellular molecule(s) that is involvedin the anti-PGN-IgG-mediated phagocytosis using purifiedhuman serum anti-PGN-IgGs and different S. aureus mutantcells. Here, we show that anti-PGN-IgG-mediated phagocytosisin phorbol myristate acetate-treated U937 cells is mediated byCa2+ release from intracellular Ca2+ stores and anti-PGN-IgGdependentCa2+ mobilization is controlled via a phospholipaseCγ-2-mediated pathway.
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