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Published online before print May 22, 2003
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* Laboratoire dImmunologie et de Parasitologie EA 2413, Université Montpellier I, France;
UMR CNRS 5539, Université Montpellier II, France; and
Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri
Correspondence: Jean Giaimis, Faculté de Pharmacie, 15 av. Charles Flahault, BP 14 491, 34 093 Montpellier Cedex 5, France. E-mail: jgiaimis{at}iup.pharma.univ-montp1.fr
Mannoproteins, as the main constituents of the outer layer of yeast cell walls, are able to interact with phagocytic cells in an opsonin-independent manner through the mannose receptor (MR) and to induce yeast ingestion by the professional phagocytes. Moreover, the MR also mediates endocytosis of soluble ligands through clathrin-coated pits. Here, we studied some aspects of the interaction between the MR and Candida albicans using murine E-clone macrophages and the consequences on MR trafficking. Using a pull-down assay involving mixture E-clone macrophage detergent lysate with mannosylated Sepharose beads and glutaraldehyde-fixed, heat-killed (HK) C. albicans, we found that binding of solubilized MR to mannosylated particles occurred with characteristics similar to the receptors cell-surface mannose-binding activity. We then demonstrated that MR expressed on E-clone macrophages contributed to phagocytosis of unopsonized, HK C. albicans and that yeast phagocytosis induced a decrease in MR endocytic activity without concomitant degradation of the receptor in the time lapse studied.
Key Words: receptor-mediated endocytosis ß-glucan receptors mannan
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