Identification and characterization of a Candida albicans-binding proteoglycan secreted from rat submandibular salivary glands

Hoffman, Maureane; Haidaris, Constantine G.

doi:10.1128/iai.62.3.828-836.1994

Cited by 18 publications

(8 citation statements)

References 53 publications

(57 reference statements)

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“…The reactive component of human saliva was identified as a low-molecular-weight mucin, MG2 in human saliva and rat submandibular gland (RSMG) mucin in rat saliva. The purified RSMG component had characteristics of both mucin and proteoglycan (200). The binding moiety contained glycosaminoglycans and human blood group A oligosaccharide, which are generally associated with proteoglycans and mucins, respectively.…”

Section: Binding Proteins (Receptors) For Host Ligandsmentioning

confidence: 99%

Cell Wall and Secreted Proteins ofCandida albicans: Identification, Function, and Expression

Chaffin

López-Ribot

Casanova

et al. 1998

Microbiol Mol Biol Rev

663

344

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SUMMARY The cell wall is essential to nearly every aspect of the biology and pathogenicity of Candida albicans. Although it was intially considered an almost inert cellular structure that protected the protoplast against osmotic offense, more recent studies have demonstrated that it is a dynamic organelle. The major components of the cell wall are glucan and chitin, which are associated with structural rigidity, and mannoproteins. The protein component, including both mannoprotein and nonmannoproteins, comprises some 40 or more moieties. Wall proteins may differ in their expression, secretion, or topological location within the wall structure. Proteins may be modified by glycosylation (primarily addition of mannose residues), phosphorylation, and ubiquitination. Among the secreted enzymes are those that are postulated to have substrates within the cell wall and those that find substrates in the extracellular environment. Cell wall proteins have been implicated in adhesion to host tissues and ligands. Fibrinogen, complement fragments, and several extracellular matrix components are among the host proteins bound by cell wall proteins. Proteins related to the hsp70 and hsp90 families of conserved stress proteins and some glycolytic enzyme proteins are also found in the cell wall, apparently as bona fide components. In addition, the expression of some proteins is associated with the morphological growth form of the fungus and may play a role in morphogenesis. Finally, surface mannoproteins are strong immunogens that trigger and modulate the host immune response during candidiasis.

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Section: Binding Proteins (Receptors) For Host Ligandsmentioning

confidence: 99%

Cell Wall and Secreted Proteins ofCandida albicans: Identification, Function, and Expression

Chaffin

López-Ribot

Casanova

et al. 1998

Microbiol Mol Biol Rev

663

344

View full text Add to dashboard Cite

show abstract

“…albicans adheres also to extracellular matrix proteins (7,8), possibly with the involvement of adhesins that mimic the complement receptors CR2 and CR3 (9). Moreover, it has been shown that C. albicans binds to salivary components, including mucins (10), proteoglycan (11), and proline-rich protein (12), suggesting that C. albicans has multiple mechanisms for adherence in the oral cavity. It is well known that C. albicans adhesion to mucosal and artificial surfaces in the mouth is enhanced by several factors such as germtube production, phospholipase, protease, other extracellular enzymatic activities, carbohydrates, pH and temperature (2,3).…”

Section: Introductionmentioning

confidence: 99%

The influence of dietary carbohydrates onin vitroadherence of fourCandidaspecies to human buccal epithelial cells

Abu-Elteen

2005

Microbial Ecology in Health and Disease

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The adherence of four Candida species to human buccal epithelial cells (BECs) following treatment with the most commonly consumed dietary carbohydrates was investigated in vitro. Adhesion of C. albicans , C . tropicalis , C. glabrata and C. parapsilosis was significantly promoted by incubation in minimal medium containing a high concentration (500 mM) of fructose, galactose, glucose, maltose, sorbitol or sucrose (pB/ 0.001). C. albicans grown in galactose elicited maximal increase in adhesion followed by glucose and sucrose. Maltose and fructose also promoted adherence of Candida spp. but to a lesser extent than galactose and glucose, while no statistical difference in adherence was observed when Candida spp. were grown in the presence of lactose and trehalose. Xylitol significantly reduced adherence of Candida spp. to BECs. No statistically significant difference in the adherence capabilities of different growth phases of C. albicans was noted, and the effect of galactose and glucose persisted irrespective of the phase of growth used. The dietary carbohydrates, therefore, might represent a risk factor for oral candidosis. The limitation of their consumption by substituting xylitol could be of value in the control of oral Candida colonization and infection.

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“…These adhesins may also assist in avoidance by C. albicans of host immune defenses (3,15). Recently it has been shown that C. albicans binds to salivary components, including mucins (12,17), proteoglycan (18), and fractions enriched in proline-rich proteins (4), suggesting that C. albicans has multiple mechanisms for adherence in the oral cavity.…”

mentioning

confidence: 99%

Adherence of Candida albicans to a cell surface polysaccharide receptor on Streptococcus gordonii

1995

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Candida albicans ATCC 10261 and CA2 bound to cells of the oral bacteria Streptococcus gordonii, Streptococcus oralis, and Streptococcus sanguis when these bacteria were immobilized onto microtiter plate wells, but they did not bind to cells of Streptococcus mutans or Streptococcus salivarius. Cell wall polysaccharide was extracted with alkali from S. gordonii NCTC 7869, the streptococcal species to which C. albicans bound with highest affinity, and was effective in blocking the coaggregation of C. albicans and S. gordonii cells in the fluid phase. When fixed to microtiter plate wells, the S. gordonii polysaccharide was bound by all strains of C. albicans tested. The polysaccharide contained Rha, Glc, GalNAc, GlcNAc, and Gal and was related compositionally to previously characterized cell wall polysaccharides from strains of S. oralis and S. sanguis. The adherence of yeast cells to the immobilized polysaccharide was not inhibitable by a number of saccharides. Antiserum raised to the S. gordonii NCTC 7869 polysaccharide blocked adherence of C. albicans ATCC 10261 to the polysaccharide. The results identify a complex cell wall polysaccharide of S. gordonii as the coaggregation receptor for C. albicans. Adherent interactions of yeast cells with streptococci and other bacteria may be important for colonization of both hard and soft oral surfaces by C. albicans.

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Identification and characterization of a Candida albicans-binding proteoglycan secreted from rat submandibular salivary glands

Cited by 18 publications

References 53 publications

Cell Wall and Secreted Proteins ofCandida albicans: Identification, Function, and Expression

Cell Wall and Secreted Proteins ofCandida albicans: Identification, Function, and Expression

The influence of dietary carbohydrates onin vitroadherence of fourCandidaspecies to human buccal epithelial cells

Adherence of Candida albicans to a cell surface polysaccharide receptor on Streptococcus gordonii

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