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J S Lorenz

Publications and source records attributed to J S Lorenz.

2 recordsLinked to original sources

The iC3b receptor on Candida albicans: subcellular localization and modulation of receptor expression by glucose.

Patient isolates of Candida albicans from blood, urine, or mucosal sites express a surface receptor for C3 fragment iC3b that is recognized by monoclonal antibodies (MAb) directed against alpha-chain epitopes of the neutrophil iC3b receptor, also known as the type 3 complement receptor (CR3) or CD11b/CD18. Because 60% of these patients were hyperglycemic, the effect of glucose on receptor expression was investigated. As assessed by flow cytometry, yeasts grown in 20 mM D-glucose exhibited a four- to six-fold increase in receptor expression compared with yeasts grown in 20 mM L-glutamate. Receptor expression increased as glucose concentration rose from 0 to 20 mM (equivalent to plasma glucose concentrations of 0-360 mg/dl). Augmentation of receptor expression by growth in glucose led to significant inhibition of phagocytosis compared with that of organisms grown in equimolar L-glutamate. SDS-PAGE, Western blotting, and immunodetection of extracts of yeast cell wall, membrane, and cytosol disclosed a protein of 165 kDa in membrane and cytosolic extracts, consistent with the published Mr of the alpha-chain of neutrophil CR3. These studies provide a mechanism to explain the predilection of C. albicans to infect the hyperglycemic host.

Adolescent↗

An iC3b receptor on Candida albicans: structure, function, and correlates for pathogenicity.

Heretofore, the existence of membrane receptors for biologically active fragments of mammalian complement proteins has been confined to mammalian cells, where these receptors serve to protect the host by triggering multiple aspects of the phagocytic response to microbial invasion. In this study, we show that surface receptors for the C3 fragment iC3b are present on the yeast Candida albicans, where they promote the pathogenicity of this organism by inhibiting phagocytosis. These receptors share homology with the alpha-chain, but not with the beta-chain, of neutrophil receptors for iC3b, as determined by the binding of monoclonal antibodies, and are induced by mycelial transformation of the yeast and by high concentrations of glucose. Blockade of these receptors by monoclonal antibodies significantly augments phagocytosis for those strains studied. By binding iC3b noncovalently, these receptors impair phagocytic uptake of C. albicans by human polymorphonuclear leukocytes.

Antibodies, Monoclonal↗