Abstracts

Biological sciences

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Adhesion of Candida albicans to oral streptococci is promoted by selective adsorption of salivary proteins to the streptococcal cell surface

Article Abstract:

Results show that oral colonization by Candida albicans cells is brought about by their recognizing surface-bound basic proline-rich proteins adhering to oral cavity enamel or streptococcal cell surfaces.

New Zealand, Statistical Data Included, Streptococcal infections, Physiological aspects, Microbiology, Candidiasis, Microorganisms, Salivary glands, Microbial adhesion, Saliva

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Adherence of Candida albicans to human salivary components adsorbed to hydroxylapatite

Article Abstract:

A study of the adherence of yeast Candida albicans cells to oral surfaces using an assay of the binding of (35S)methionine-labeled C. albicans cells to saliva-coated hydroxylapatite (SHA) beads reveals different extents of adherence for the various C. albicans strains. Glucose depletion and growth at 28 degrees Celsius facilitate the binding. C. albicans ATCC 10261 binding is facilitated by statherin or proline-rich protein-containing fractions. Yeast cell adherence to the SHA beads is enhanced by neuraminidase treatment of the beads due to the exposure of glycoprotein receptors that participate in the binding by neuraminidase activity.

Research, Bacteria, Bacterial adhesion, Thrush (Mouth disease), Oral candidiasis

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Identification of salivary basic proline-rich proteins as receptors for Candida albicans adhesion

Article Abstract:

The basic proline-rich proteins that act as receptors in human parotid saliva for Candida albicans adherence were identified. These proteins were electrophoretically separated, electroblotted into nitrocellulose membranes and incubated with radiolabelled Candida albicans cells. A subset of four protein bands with molecular masses of 17(band A), 20(band B), 24(band C) and 27(band D) promoted the adherence of Candida albicans ATCC 10261 cells. Protein bands A-D were found to be members of the basic proline-rich protein family based on the N-terminal amino acid sequence.

Usage, Proteins

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