PubMed:18509109 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/18509109","sourcedb":"PubMed","sourceid":"18509109","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/18509109","text":"Human and mouse macrophage-inducible C-type lectin (Mincle) bind Candida albicans.\nCandida albicans is a causative agent in mycoses of the skin, oral cavity, and gastrointestinal tract. Identification of receptors, and their respective ligands, that are engaged by immune cells when in contact with C. albicans is crucial for understanding inflammatory responses leading to invasive candidiasis. Mincle is a recently identified macrophage-expressed receptor that is important for host responses to C. albicans. The carbohydrate-recognition domain of human and mouse Mincle were expressed, purified under denaturing conditions, and successfully refolded. In addition to oligomers, there are isolatable monomeric and dimeric forms of the protein that occur under two different buffer solutions. The human and mouse homologues bound yeast extract, and the isolated dimeric and monomeric species also demonstrated the recognition of whole C. albicans yeast cells. The data are indicative of several functional states mediating the interaction of Mincle and yeast at the surface of the 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