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- W4313351520 abstract "Abstract β-glucans are considered as fungal pathogen-associated molecular patterns that are recognized by innate human cells. Our previous studies demonstrated that Imprime PGG®, an analytically well-characterized form of yeast-derived soluble β−glucan, bound to human neutrophils and monocytes via complement receptor 3 (CR3) and B-cells via CR2, and that receptor binding was complement-dependent. The objective of this study was to further our understanding of the mechanism underlying the interaction of soluble β−glucan with immune cells, specifically, to investigate a role for complement receptor type 1 (CR1; CD35; C3b/C4b receptor) in the binding of Imprime PGG. Blocking of CR1 by anti-CR1 monoclonal antibody significantly abrogated binding of Imprime PGG on all three cell types. Cell-surface CR1, as opposed to soluble CR1, was shown to be more important in mediating Imprime PGG binding. The role of CR1 was further confirmed by demonstrating enhanced binding of Imprime PGG to HEK 293T cells transfected with a combination of CR1 and CR2 genes in comparison to either gene alone. These results suggest that CR1 receptor works in concert with CR3 on neutrophils and monocytes, and with CR2 on B cells in recognizing Imprime PGG. Modulation of Imprime PGG-mediated immune functions after blocking CR1 receptor will also be presented. These data demonstrate for the first time the interplay of several complement receptors in recognizing soluble β−glucan by human immune cells." @default.
- W4313351520 created "2023-01-06" @default.
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- W4313351520 date "2013-05-01" @default.
- W4313351520 modified "2023-09-28" @default.
- W4313351520 title "Recognition of soluble yeast β-1,3/1,6 glucan by complement receptor 1 is essential for it to bind complement receptor 3 on human neutrophils and monocytes, and complement receptor 2 on B cells (P3048)" @default.
- W4313351520 doi "https://doi.org/10.4049/jimmunol.190.supp.125.2" @default.
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