Multilocus enzyme electrophoresis analysis and exoenzymatic activity of Candida albicans strains isolated from women with vaginal candidiasis. 2012

Patrícia O Santos, and Juliana O Melo, and Camila Monique P B S Ponzzes, and José Antônio B Alves, and Dângelly L F M de Melo, and Nathalia de S Botelho, and Sueli F Yamada-Ogatta, and Renata S Mann, and Rita de Cássia Trindade
Department of Morphology, Applied Microbiology Laboratory, Federal University of Sergipe-FUS, São Cristóvão-SE, Brazil. oliveira.micro@gmail.com

Twenty-eight Candida albicans strains obtained from women with vaginal candidiasis were tested for phospholipase and proteinase production and clustered by multilocus enzyme electrophoresis (MLEE). The proteolytic and phospholipidic activity were considered moderate (0.56 ± 0.12 mm and 0.53 ± 0.09 mm, respectively) for all isolates. The isoenzymes malate dehydrogenase (MDH) and sorbitol dehydrogenase (SDH) showed strong intra-specific discriminatory power. The numerical and genetic interpretation of the bands produced by the isoenzymes tested presented similar discriminatory power. The genetic diversity of the isolates was measured by allelic and genic frequency, perceptual index of polymorphic loci (P = 87.5%), average number of alleles per locus, average number of alleles per polymorphic locus, average heterozygosity observed and average heterozygosity expected. We verified that three isoenzymatic loci (Adh, Gdh and Sdh-2) were not in Hardy-Weinberg equilibrium. A dendrogram constructed based on the genetic distance matrix of Nei showed seven clusters; 57.15% (16) of the isolates were considered highly related or indistinguishable, and 42.85% were considered moderately related or unrelated. We did not find a relationship between the clusters and the exoenzymes production.

UI MeSH Term Description Entries
D007064 L-Iditol 2-Dehydrogenase An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14 Iditol Dehydrogenase,Sorbitol Dehydrogenase,Polyol Dehydrogenase,2-Dehydrogenase, L-Iditol,Dehydrogenase, Iditol,Dehydrogenase, Polyol,Dehydrogenase, Sorbitol,L Iditol 2 Dehydrogenase
D007527 Isoenzymes Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics. Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes
D008291 Malate Dehydrogenase An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37. Malic Dehydrogenase,NAD-Malate Dehydrogenase,Dehydrogenase, Malate,Dehydrogenase, Malic,Dehydrogenase, NAD-Malate,NAD Malate Dehydrogenase
D010641 Phenotype The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment. Phenotypes
D010740 Phospholipases A class of enzymes that catalyze the hydrolysis of phosphoglycerides or glycerophosphatidates. EC 3.1.-. Lecithinases,Lecithinase,Phospholipase
D002176 Candida albicans A unicellular budding fungus which is the principal pathogenic species causing CANDIDIASIS (moniliasis). Candida albicans var. stellatoidea,Candida stellatoidea,Dematium albicans,Monilia albicans,Myceloblastanon albicans,Mycotorula albicans,Parasaccharomyces albicans,Procandida albicans,Procandida stellatoidea,Saccharomyces albicans,Syringospora albicans
D002181 Candidiasis, Vulvovaginal Infection of the VULVA and VAGINA with a fungus of the genus CANDIDA. Moniliasis, Vulvovaginal,Vaginitis, Monilial,Candidiasis, Genital,Genital Vulvovaginal Candidiasis,Vaginal Yeast Infection,Vaginal Yeast Infections,Candidiasis, Genital Vulvovaginal,Genital Candidiasis,Infection, Vaginal Yeast,Infections, Vaginal Yeast,Monilial Vaginitis,Vulvovaginal Candidiasis,Vulvovaginal Candidiasis, Genital,Vulvovaginal Moniliasis,Yeast Infection, Vaginal,Yeast Infections, Vaginal
D004591 Electrophoresis, Polyacrylamide Gel Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D005260 Female Females

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