Journal
BMB REPORTS
Volume 48, Issue 1, Pages 36-41Publisher
KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
DOI: 10.5483/BMBRep.2015.48.1.080
Keywords
Anti-peptidoglycan-IgGs; Calcium signaling; Phagocytosis; Phospholiphase C; U937 cells
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Funding
- Pusan National University Research Grant
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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 Delta tagO 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-PGN-IgGs), which may be involved in complement-dependent opsonophagocytosis against infected S. aureus cells. We assumed that purified serum anti-PGN-IgGs and S. aureus Delta tagO 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-IgG-dependent Ca2+ mobilization is controlled via a phospholipase C gamma-2-mediated pathway.
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