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Lymphocytes utilize CD11b/CD18 for adhesion to Candida albicans
1Department of Microbiology and Immunology, Stritch School of Medicine, University of Chicago, Maywood, Illinois 60153, USA.
Cellular Immunology
|May 25, 1996
Summary
Large granular lymphocytes use Mac-1 (CD11b/CD18) to adhere to Candida albicans hyphae, inhibiting fungal growth. This interaction is mediated by Mac-1 binding to microbial ligands and extracellular matrix proteins.
Area of Science:
- Immunology
- Microbiology
- Cell Biology
Background:
- Large granular lymphocytes (LGLs) play a role in fungal immunity.
- Adherence of LGLs to Candida albicans hyphae is crucial for inhibiting fungal growth.
Purpose of the Study:
- To identify the specific lymphocyte surface molecules responsible for adhesion to Candida albicans hyphae.
- To elucidate the molecular mechanisms underlying LGL-fungal interactions.
Main Methods:
- Utilized monoclonal antibodies targeting CD11b and CD18 subunits of Mac-1.
- Tested inhibition of lymphocyte adhesion using known Mac-1 protein ligands (vitronectin, laminin, fibrinogen) and RGD-containing peptides.
- Assessed the effect of carbohydrate N-acetyl-D-glucosamine on lymphocyte adhesion.
Main Results:
- Monoclonal antibodies against Mac-1 (CD11b/CD18) significantly inhibited LGL adhesion to C. albicans hyphae.
- Protein ligands of Mac-1, including extracellular matrix proteins and RGD peptides, also blocked this adhesion.
- N-acetyl-D-glucosamine, a known inhibitor of Mac-1-mediated yeast adhesion, similarly inhibited hyphal adhesion.
Conclusions:
- Mac-1 (CD11b/CD18) is the primary lymphocyte surface molecule mediating adhesion to Candida albicans hyphae.
- Microbial ligands and extracellular matrix proteins can activate lymphocyte Mac-1 for fungal adhesion.
- A model for Mac-1 activation by microbial ligands in LGL-fungal interactions is proposed.