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KMID : 0624620150480010036
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BMB Reports
2015 Volume.48 No. 1 p.36 ~ p.41
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Human anti-peptidoglycan-IgG-mediated opsonophagocytosis is controlled by calcium mobilization in phorbol myristate acetate-treated U937 cells
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Kim Min-Jung
Rah So-Young
An Jang-Hyun
Kurokawa Kenji
Kim Uh-Hyun
Lee Bok-Luel
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Abstract
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Recently, we demonstrated that human serum amyloid P component (SAP) specifically recognizes exposed bacterial peptidoglycan (PGN) of wall teichoic acid (WTA)-deficient Staphylococcus aureus ΔtagO mutant cells and then induces complement-independent phagocytosis. In our preliminary experiments, we found the existence of human serum immunoglobulins that recognize S. aureus PGN (anti-PGNIgGs), which may be involved in complement-dependent opsonophagocytosis against infected S. aureus cells. We assumed that purified serum anti-PGN-IgGs and S. aureus ΔtagO mutant cells are good tools to study the molecular mechanism of anti-PGN-IgG-mediated phagocytosis. Therefore, we tried to identify the intracellular molecule(s) that is involved in the anti-PGN-IgG-mediated phagocytosis using purified human serum anti-PGN-IgGs and different S. aureus mutant cells. Here, we show that anti-PGN-IgG-mediated phagocytosis in phorbol myristate acetate-treated U937 cells is mediated by Ca2+ release from intracellular Ca2+ stores and anti-PGN-IgGdependent Ca2+ mobilization is controlled via a phospholipase Cγ-2-mediated pathway.
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KEYWORD
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Anti-peptidoglycan-IgGs, Calcium signaling, Phagocytosis, Phospholiphase C, U937 cells
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