title: A mannose-binding receptor is expressed on human keratinocytes and mediates killing of Candida albicans.
abstract: Human keratinocytes are known to kill Candida albicans in vitro, but the mechanism of killing is not yet understood. Here, we demonstrate that spontaneous, ultraviolet-B-light-induced, alpha-melanocyte-stimulating-hormone-induced, and interleukin-8-induced Candida killing by keratinocytes can be inhibited with mannan and mannosylated bovine serum albumin (Man-BSA). A polyclonal goat serum raised against the human macrophage mannose receptor stained suprabasal keratinocytes, but no staining was observed on keratinocytes with a monoclonal antibody (mAb15) specific for the human macrophage mannose receptor. Mannose-affinity chromatography of keratinocyte extract isolated a 200 kDa protein, and on the Western blot the goat antiserum reacted with a 200 kDa protein. In radioligand binding studies, the binding of 125I-Man-BSA to human keratinocytes was inhibited by mannan in a concentration-dependent manner. Analysis of the binding revealed a single class keratinocyte mannose receptor with a KD of 1.4 x 10(-8) M and a Bmax of 1 x 10(4) binding sites per cell. The binding of 125I-Man- BSA to keratinocytes proved to be time-dependent, acid-precipitable, and Ca2+- and trypsin-sensitive. After trypsinization the receptors underwent a rapid recovery at 37 degrees C. These results demonstrate the presence of mannose receptor on human keratinocytes, and its active involvement in the killing of Candida albicans.
authors.affiliation: Department of Dermatology, Albert Szent-Györgyi Medical Center, University of Szeged, Szeged, Hungary. szolnoky@derma.u-szeged.hu
authors.forename: G
authors.initials: G
authors.lastname: Szolnoky
authors.forename: Z
authors.initials: Z
authors.lastname: Bata-Csörgö
authors.forename: A S
authors.initials: AS
authors.lastname: Kenderessy
authors.forename: M
authors.initials: M
authors.lastname: Kiss
authors.forename: A
authors.initials: A
authors.lastname: Pivarcsi
authors.forename: Z
authors.initials: Z
authors.lastname: Novák
authors.forename: K
authors.initials: K
authors.lastname: Nagy Newman
authors.forename: G
authors.initials: G
authors.lastname: Michel
authors.forename: T
authors.initials: T
authors.lastname: Ruzicka
authors.forename: L
authors.initials: L
authors.lastname: Maródi
authors.forename: A
authors.initials: A
authors.lastname: Dobozy
authors.forename: L
authors.initials: L
authors.lastname: Kemény
mesh_terms: D000911:Antibodies, Monoclonal; D015153:Blotting, Western; D002118:Calcium / Q000378:metabolism; D002176:Candida albicans / Q000276:immunology*; D002177:Candidiasis / Q000276:immunology* / Q000378:metabolism; D002448:Cell Adhesion; D002614:Chelating Agents / Q000494:pharmacology; D003429:Cross Reactions; D004533:Egtazic Acid / Q000494:pharmacology; D005434:Flow Cytometry; D006801:Humans; D007150:Immunohistochemistry; D066298:In Vitro Techniques; D007457:Iodine Radioisotopes; D015603:Keratinocytes / Q000166:cytology / Q000378:metabolism* / Q000382:microbiology*; D037181:Lectins, C-Type; D007962:Leukocytes / Q000276:immunology / Q000378:metabolism / Q000382:microbiology; D008351:Mannans / Q000494:pharmacology; D008358:Mannose / Q000493:pharmacokinetics; D000090323:Mannose Receptor; D037241:Mannose-Binding Lectins; D011869:Radioligand Assay; D011956:Receptors, Cell Surface / Q000032:analysis / Q000096:biosynthesis* / Q000276:immunology; D012709:Serum Albumin / Q000493:pharmacokinetics; D012867:Skin / Q000166:cytology / Q000382:microbiology
chemical_list: D000911:Antibodies, Monoclonal; D002614:Chelating Agents; D007457:Iodine Radioisotopes; D037181:Lectins, C-Type; D008351:Mannans; D000090323:Mannose Receptor; D037241:Mannose-Binding Lectins; D011956:Receptors, Cell Surface; D012709:Serum Albumin; C023840:mannose-bovine serum albumin conjugate; D004533:Egtazic Acid; D008358:Mannose; D002118:Calcium