Coaggregation of Candida albicans oral Actinomyces species

Abstract

Eight strains of Actinomyces were examined for their ability to coaggregate in vitro with four strains of Candida albicans. The Actinomyces coaggregated to various degrees with all of the Candida strains. Exposure of the Candida but not the Actinomyces to heat, trypsin, proteinase K, amphotericin B or trichodermin abolished coaggregation. All sugars tested did not inhibit any of the reactions. All coaggregating pairs were disaggregated by the addition of SDS, but nonionic detergents had no effect. The addition of urea or EDTA completely reversed coaggregation. Actinomyces strains were sensitive to periodate oxidation, whereas the Candida strains were unaffected. These data suggest that the coaggregations involve a protein on the Candida surface that may interact with carbohydrates or carbohydrate-containing molecules on the surface of the Actinomyces. These observations expand the known range of intergeneric coaggregations occurring between human oral microbes and indicate that coaggregation of C. albicans and Actinomyces may be an important factor in oral colonization by this yeast.

Polymicrobial Interactions: Impact on Pathogenesis and Human Disease

“…The latter interactions were inhibited by mannose and therefore were thought to involve a protein component of Fusobacterium binding to a carbohydrate (mannan) receptor on the Candida cell surface (96). In contrast, a study demonstrating the ability of Actinomyces to coaggregate with C. albicans in vitro identified the receptors to be a protein moiety on the Candida surface, interacting with a carbohydrate-containing molecule on the surface of Actinomyces (76). These two examples demonstrate the diversity of ligand-receptor interactions that govern coaggregation on both bacterial and fungal surfaces.…”

“…Although streptococcal species, namely, Streptococcus gordonii, Streptococcus oralis, and Streptococcus sanguinis, exhibit the highest affinities for C. albicans, C. albicans as well as Candida dubliniensis have been shown to coaggregate with Fusobacterium species in suspension (75,76). The latter interactions were inhibited by mannose and therefore were thought to involve a protein component of Fusobacterium binding to a carbohydrate (mannan) receptor on the Candida cell surface (96).…”

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

“…Salivary proteins and glycoproteins can act as receptors for binding of C. albicans cells to enamel surfaces (Cannon et al, 1995b) and to denture acrylic surfaces (Vasilas et al, 1992 ;Edgerton et al, 1993 ;Nikawa et al, 1993) and can modulate the binding of yeast cells to buccal epithelial cells (Kimura & Pearsall, 1978 ;Samaranayake & MacFarlane, 1982). In addition, C. albicans binding to oral viridans streptococci (Jenkinson et al, 1990 ;Holmes et al, 1995aHolmes et al, , b, 1996 and to Actinomyces (Grimaudo et al, 1996) may be enhanced by salivary components Grimaudo et al, 1996). We have now determined that the basic PRPs present in human parotid salivary secretions are not only active in providing receptors for adhesion of C. albicans to enamel pellicles, but also that these salivary components are adsorbed by streptococci and act to promote adhesion of C. albicans ATCC 10261 to bacterial cells.…”

Synergistic Interaction between Candida albicans and Commensal Oral Streptococci in a Novel In Vitro Mucosal Model

“…However, viridans streptococci can cause life-threatening systemic infections if the oral mucosa is disrupted and the host defense mechanisms are compromised (28,34). C. albicans has the ability to coaggregate with a variety of oral bacteria, including most species from the viridans group of streptococci (26,30,33). Physically associated cells of C. albicans and streptococci have been demonstrated in vivo, in tooth-associated biofilms, via fluorescence in situ hybridization (FISH), with streptococcal cells forming "corn-cob-like" structures around C. albicans hyphae (65).…”