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Candida albicans binding to the oral bacterium Streptococcus gordonii involves multiple adhesin-receptor interactions
A R Holmes1, R McNab, H F Jenkinson
1Department of Oral Biology and Oral Pathology, University of Otago, Dunedin, New Zealand.
Infection and Immunity
|November 1, 1996
Summary
Candida albicans adherence to Streptococcus gordonii involves multiple bacterial cell surface proteins, including antigen I/II adhesins and CshA polypeptides. These interactions are crucial for understanding oral microbial communities.
Area of Science:
- Microbiology
- Oral Biology
- Molecular Biology
Background:
- Candida albicans interacts with oral streptococci, notably Streptococcus gordonii, via streptococcal cell wall polysaccharide receptors.
- Previous studies identified polysaccharide receptors mediating this interaction.
Purpose of the Study:
- To investigate the role of Streptococcus gordonii cell surface proteins in Candida albicans adherence.
- To elucidate the specific adhesins and domains involved in the C. albicans-S. gordonii interaction.
Main Methods:
- Generated isogenic cell surface protein mutants of S. gordonii DL1.
- Utilized solid-phase assays to measure C. albicans adherence to S. gordonii mutants.
- Employed polyclonal antiserum and specific antibodies to block adherence.
- Expressed S. gordonii SspB on Enterococcus faecalis to assess binding.
Main Results:
- Inactivation of cshA/cshB and sspA/sspB genes significantly reduced C. albicans adherence (40% and 79% respectively).
- Inactivation of scaA gene had no effect on adherence.
- Antiserum to SpaP and antibodies to CshA's non-repetitive (NR) domain inhibited adherence.
- Recombinant CshA fragments (NR and R domains) supported C. albicans adherence.
- Expression of SspB on Enterococcus faecalis conferred C. albicans binding.
Conclusions:
- Streptococcal cell surface polypeptides, specifically antigen I/II adhesins and CshA, are key mediators of Candida albicans adherence to Streptococcus gordonii.
- The interaction involves multiple adhesin-receptor systems, including bacterial cell wall polysaccharides and potentially unknown yeast cell surface components.