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• W2154820152 abstract "Abstract 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 receptor’s 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." @default.
• W2154820152 created "2016-06-24" @default.
• W2154820152 creator A5007089743 @default.
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• W2154820152 creator A5064162089 @default.
• W2154820152 creator A5087000318 @default.
• W2154820152 date "2003-05-22" @default.
• W2154820152 modified "2023-09-25" @default.
• W2154820152 title "Mannose receptor contribution to <i>Candida albicans</i> phagocytosis by murine E-clone J774 macrophages" @default.
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• W2154820152 doi "https://doi.org/10.1189/jlb.1202608" @default.
• W2154820152 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12885937" @default.
• W2154820152 hasPublicationYear "2003" @default.
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