Human and mouse macrophage-inducible C-type lectin (Mincle) bind Candida albicans
Candida 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...
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| Veröffentlicht in: | Glycobiology (Oxford) 2008-09, Vol.18 (9), p.679-685 |
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| creator | Bugarcic, Andrea Hitchens, Kelly Beckhouse, Anthony G Wells, Christine A Ashman, Robert B Blanchard, Helen |
| description | Candida 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 macrophage. |
| doi_str_mv | 10.1093/glycob/cwn046 |
| format | Article |
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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 macrophage.</description><identifier>ISSN: 0959-6658</identifier><identifier>EISSN: 1460-2423</identifier><identifier>DOI: 10.1093/glycob/cwn046</identifier><identifier>PMID: 18509109</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Animals ; C-type lectin ; Candida albicans ; Candida albicans - metabolism ; Cell Extracts - pharmacology ; Cells, Cultured ; Dimerization ; Humans ; Lectins, C-Type - metabolism ; Lectins, C-Type - physiology ; Macrophages - metabolism ; Male ; Membrane Proteins - metabolism ; Membrane Proteins - physiology ; Mice ; Mincle ; Protein Binding ; receptor-binding assay ; Solubility</subject><ispartof>Glycobiology (Oxford), 2008-09, Vol.18 (9), p.679-685</ispartof><rights>Oxford University Press © The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org 2008</rights><rights>The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c549t-8d701715ba80eae9748326623085fa1c3a32aa9ec8689d908dc53f1d6474fd453</citedby><cites>FETCH-LOGICAL-c549t-8d701715ba80eae9748326623085fa1c3a32aa9ec8689d908dc53f1d6474fd453</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,782,786,1586,27931,27932</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18509109$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bugarcic, Andrea</creatorcontrib><creatorcontrib>Hitchens, Kelly</creatorcontrib><creatorcontrib>Beckhouse, Anthony G</creatorcontrib><creatorcontrib>Wells, Christine A</creatorcontrib><creatorcontrib>Ashman, Robert B</creatorcontrib><creatorcontrib>Blanchard, Helen</creatorcontrib><title>Human and mouse macrophage-inducible C-type lectin (Mincle) bind Candida albicans</title><title>Glycobiology (Oxford)</title><addtitle>Glycobiology</addtitle><description>Candida 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 macrophage.</description><subject>Animals</subject><subject>C-type lectin</subject><subject>Candida albicans</subject><subject>Candida albicans - metabolism</subject><subject>Cell Extracts - pharmacology</subject><subject>Cells, Cultured</subject><subject>Dimerization</subject><subject>Humans</subject><subject>Lectins, C-Type - metabolism</subject><subject>Lectins, C-Type - physiology</subject><subject>Macrophages - metabolism</subject><subject>Male</subject><subject>Membrane Proteins - metabolism</subject><subject>Membrane Proteins - physiology</subject><subject>Mice</subject><subject>Mincle</subject><subject>Protein Binding</subject><subject>receptor-binding assay</subject><subject>Solubility</subject><issn>0959-6658</issn><issn>1460-2423</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0U1v1DAQBmALgehSOHKFiANqD6FjO3bsI6ygW6l8rKAS6sWaOM7ikjghTgT773GVVZG49GJfnnmt8UvIcwpvKGh-tmv3tq_O7O8AhXxAVrSQkLOC8YdkBVroXEqhjsiTGG8AqKRKPCZH6QSdxldku5k7DBmGOuv6ObqsQzv2ww_cudyHera-al22zqf94LLW2cmH7OSjD7Z1p1mVRLZOs77GDNvKWwzxKXnUYBvds8N9TK4-vP-23uSXn88v1m8vcysKPeWqLoGWVFSowKHTZaE4k5JxUKJBajlyhqidVVLpWoOqreANrWVRFk1dCH5MXi-5w9j_ml2cTOejdW2LwaVNjNQF10rCvZAB5xQkT_DVf_Cmn8eQljCMAqeiFLdp-YLSN8U4usYMo-9w3BsK5rYRszRilkaSf3EInavO1f_0oYIEThbQz8O9WYe3fZzcnzuM408jS14Ks_l-bb58umbvSrU12-RfLr7B3uBu9NFcfWVAOYBmijHG_wJoRKza</recordid><startdate>20080901</startdate><enddate>20080901</enddate><creator>Bugarcic, Andrea</creator><creator>Hitchens, Kelly</creator><creator>Beckhouse, Anthony G</creator><creator>Wells, Christine A</creator><creator>Ashman, Robert B</creator><creator>Blanchard, Helen</creator><general>Oxford University Press</general><general>Oxford Publishing Limited (England)</general><scope>FBQ</scope><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7TK</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7T5</scope><scope>7X8</scope></search><sort><creationdate>20080901</creationdate><title>Human and mouse macrophage-inducible C-type lectin (Mincle) bind Candida albicans</title><author>Bugarcic, Andrea ; 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| subjects | Animals C-type lectin Candida albicans Candida albicans - metabolism Cell Extracts - pharmacology Cells, Cultured Dimerization Humans Lectins, C-Type - metabolism Lectins, C-Type - physiology Macrophages - metabolism Male Membrane Proteins - metabolism Membrane Proteins - physiology Mice Mincle Protein Binding receptor-binding assay Solubility |
| title | Human and mouse macrophage-inducible C-type lectin (Mincle) bind Candida albicans |
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