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Query: UMLS:C0006849 (oral candidiasis)
 1,939 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Candida species are the most important pathogenic fungi in the oral cavity with the predominance of Candida albicans. In this review the authors summarise the most important cell-surface bound pathogenical factors such as fibrinogen, fibronectin, thrombin, collagen, laminin and vitronectin-binding proteins and extracellular virulence enzymes of Candida albicans and some microbiological aspects of oral candidiasis (candidosis). Adherence to both artificial and mucosal surfaces is mediated by hydrophobic interactions and by ligand-receptor attachment. Surface bound proteins on Candida cells bind to mucosal surface proteins. Broad spectrum antibacterial treatment liberates binding sites for Candida colonisation by means of reducing the number of bacterial normal flora in the oral cavity. Non immune humoral factors such as iron, lysosyme, hystidine-rich-polypeptides, lactoferrin, lactoperoxidase and immune globulins such as s-IgA, moreover, elements of cellular immunity, especially polymorphonuclear leucocytes contribute to preventing the establishment of Candida infection. A disbalance in these constituents may result in colonisation and biofilm production of Candida. The biofilm consist of serum proteins mainly fibrin, desquamated epithelial cells, dead leukocytes, living and multiplying candida cells, pseudohyphae and extracellular matrix excreted by candida cells. Living candida cells are deeply embedded in the biofilm, thus protected from defence mechanisms of the host. Continuous destruction of mucosal surfaces beneath the biofilm may create a portal of entry for systematic candidal infections.
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PMID:[Molecular pathogenesis of oral candidiasis (candidosis)]. 1177 60

Candida dubliniensis and Candida albicans cause most of the oral candidiasis infections in AIDS patients. Unlike C. albicans, which variably expresses cell surface hydrophobicity (CSH) depending on environmental conditions, C. dubliniensis is hydrophobic under all environmental conditions. C. dubliniensis produces CdCSH1p, a protein related to CaCSH1p that contributes to CSH expression of C. albicans. We investigated whether environmental conditions affect CdCSH1p expression, CSH avidity, and adhesion to fibronectin (Fn). C. dubliniensis CD36 was grown at 23 degrees C and 37 degrees C in four different media. CdCSH1p expression was affected by growth temperature, with cells grown at 37 degrees C expressing the protein, but cells grown at 23 degrees C did not. Hydrophobic avidity for two media was higher in cells grown at 37 degrees C than at 23 degrees C. Cells grown at 23 degrees C were generally less adherent than 37 degrees C-grown cells to Fn. The results suggest CdCSH1p but not hydrophobic avidity may have a role in adhesion of C. dubliniensis to Fn.
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PMID:Relationship between expression of cell surface hydrophobicity protein 1 (CSH1p) and surface hydrophobicity properties of Candida dubliniensis. 1517 Feb 42

The ALS (agglutinin-like sequence) gene family of Candida albicans encodes eight cell-surface glycoproteins, some of which are involved in adherence to host surfaces. A mutational analysis of each ALS gene is currently being performed to deduce the functions of the encoded proteins and to better understand the role of these proteins in C. albicans biology and pathogenesis. This paper describes construction of an als3/als3 mutant and comparison of its phenotype to an als1/als1 strain. Efforts to disrupt ALS3 indicated that the gene could be deleted in two transformation steps, suggesting that the gene is encoded by a single locus and that the ALS3-like locus, ALS8, does not exist. Strains lacking ALS3 or ALS1 did not exhibit a defect in germ tube formation when grown in RPMI 1640 medium, but the als1/als1 mutant formed significantly fewer germ tubes in Lee medium. Analysis of ALS3 and ALS1 promoter activity using green fluorescent protein (GFP) reporter strains and flow cytometry showed that when cells are placed into medium that promotes germ tube formation, ALS1 is transcribed prior to ALS3. Comparison of the mutant strains in adhesion assays showed that the als3/als3 strain was defective in adhesion to both human umbilical vein endothelial cells (HUVEC) and buccal epithelial cells (BEC), but not to fibronectin-coated plastic plates. In contrast, the als1/als1 strain showed decreased adherence to HUVEC, but adherence to BEC and fibronectin were the same as wild-type controls. Inoculation of the buccal reconstituted human epithelium (RHE) model of oral candidiasis with the mutant strains showed nearly a total lack of adhesion and epithelial destruction by the als3/als3 mutant while the als1/als1 strain showed only a slightly reduced degree of epithelial destruction compared to the wild-type control. Adhesion data presented here suggest that, in the assays performed, loss of Als3p affects C. albicans adhesion more than loss of Als1p. Collectively, these results demonstrate functional similarities and differences between Als1p and Als3p, and suggest the potential for more complex interrelationships between the ALS genes and their encoded proteins.
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PMID:ALS3 and ALS8 represent a single locus that encodes a Candida albicans adhesin; functional comparisons between Als3p and Als1p. 1525 83