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Binding of Soluble Yeast ?-Glucan to Human Neutrophils and Monocytes is Complement-Dependent.


ABSTRACT: The immunomodulatory properties of yeast ?-1,3/1,6 glucans are mediated through their ability to be recognized by human innate immune cells. While several studies have investigated binding of opsonized and unopsonized particulate ?-glucans to human immune cells mainly via complement receptor 3 (CR3) or Dectin-1, few have focused on understanding the binding characteristics of soluble ?-glucans. Using a well-characterized, pharmaceutical-grade, soluble yeast ?-glucan, this study evaluated and characterized the binding of soluble ?-glucan to human neutrophils and monocytes. The results demonstrated that soluble ?-glucan bound to both human neutrophils and monocytes in a concentration-dependent and receptor-specific manner. Antibodies blocking the CD11b and CD18 chains of CR3 significantly inhibited binding to both cell types, establishing CR3 as the key receptor recognizing the soluble ?-glucan in these cells. Binding of soluble ?-glucan to human neutrophils and monocytes required serum and was also dependent on incubation time and temperature, strongly suggesting that binding was complement-mediated. Indeed, binding was reduced in heat-inactivated serum, or in serum treated with methylamine or in serum reacted with the C3-specific inhibitor compstatin. Opsonization of soluble ?-glucan was demonstrated by detection of iC3b, the complement opsonin on ?-glucan-bound cells, as well as by the direct binding of iC3b to ?-glucan in the absence of cells. Binding of ?-glucan to cells was partially inhibited by blockade of the alternative pathway of complement, suggesting that the C3 activation amplification step mediated by this pathway also contributed to binding.

SUBMITTER: Bose N 

PROVIDER: S-EPMC3740326 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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The immunomodulatory properties of yeast β-1,3/1,6 glucans are mediated through their ability to be recognized by human innate immune cells. While several studies have investigated binding of opsonized and unopsonized particulate β-glucans to human immune cells mainly via complement receptor 3 (CR3) or Dectin-1, few have focused on understanding the binding characteristics of soluble β-glucans. Using a well-characterized, pharmaceutical-grade, soluble yeast β-glucan, this study evaluated and cha  ...[more]

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