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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0006837,
umls-concept:C0021701,
umls-concept:C0064830,
umls-concept:C0079785,
umls-concept:C0443264,
umls-concept:C0450254,
umls-concept:C0521033,
umls-concept:C0524637,
umls-concept:C1514562,
umls-concept:C1704675,
umls-concept:C1711351,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
11
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pubmed:dateCreated |
1998-12-21
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pubmed:abstractText |
Interactions of microorganisms with integrins are central to the host defense mechanisms. The leukocyte integrin CD11b/CD18 is the principal adhesion receptor on leukocytes for Candida albicans, a major opportunistic pathogen. In this study we have investigated the roles of three regions within the receptor, the inserted (I) and lectin-like domains within the CD11b subunit, and the CD18 subunit, in CD11b/CD18-C. albicans interactions. We report four major findings. 1) A mutation in CD18 exerts a dominant negative effect on the function of the CD11b/CD18 complex. This interpretation is based on the observation that in the absence of CD18, the CD11b subunit alone binds C. albicans well, but a single point mutation at Ser138 of CD18 abolishes CD11b/CD18 binding of the fungus. 2) The lectin-like domain is not sufficient for CD11b/CD18-C. albicans interactions. Rather, the lectin-like domain appears to influence CD11b/CD18 binding activity by modulating the function of the I domain. 3) The I domain is the primary binding site for C. albicans in the receptor and is sufficient to support an efficient interaction. 4) We have identified specific amino acid sequences within the I domain that engage the microorganism. Compared with other ligands of CD11b/CD18, C. albicans has some unique as well as common contact sites within the I domain of the receptor. Such unique contact sites may underlie the ability of C. albicans to modulate CD11b/CD18 function and raise the possibility for selective interference of the microorganism-host leukocyte interactions.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD18,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Macrophage-1 Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
161
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6198-205
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9834106-Antigens, CD18,
pubmed-meshheading:9834106-Candida albicans,
pubmed-meshheading:9834106-Cell Adhesion,
pubmed-meshheading:9834106-Cell Line,
pubmed-meshheading:9834106-Humans,
pubmed-meshheading:9834106-Interleukin-2,
pubmed-meshheading:9834106-Kidney,
pubmed-meshheading:9834106-Lectins,
pubmed-meshheading:9834106-Lymphocyte Activation,
pubmed-meshheading:9834106-Lymphocytes,
pubmed-meshheading:9834106-Macrophage-1 Antigen,
pubmed-meshheading:9834106-Models, Molecular,
pubmed-meshheading:9834106-Peptide Fragments,
pubmed-meshheading:9834106-Peptide Mapping,
pubmed-meshheading:9834106-Protein Binding,
pubmed-meshheading:9834106-Protein Structure, Tertiary,
pubmed-meshheading:9834106-Transfection
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pubmed:year |
1998
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pubmed:articleTitle |
Interaction of the fungal pathogen Candida albicans with integrin CD11b/CD18: recognition by the I domain is modulated by the lectin-like domain and the CD18 subunit.
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pubmed:affiliation |
The Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Department of Molecular Cardiology, The Cleveland Clinic Foundation, OH 44195, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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