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Candidial vulvovaginitis is one of the most common forms of vaginal infection. However, the origin of the infecting organism is sometimes doubtful. Therefore, epidemiological investigation can help to recognize routes of infection spreading. The aim of the present study was to determine the ability to produce esterases by clinical isolates of C. albicans and to find the relationship between their serotypes. Also, it was intended to determine the ability of these strains to produce proteases and lipases as well as the ability of the strains to assimilate carbohydrates. 46 strains of C. albicans isolates from the vagina of women suffering from vulvovaginitis were examined. Three main kinds of esterases were distinquished by their spectra of hydrolytic activity toward a-naphthyl acetate, P-naphthyl propionate and indoxyl acetate. The strains were grouped into four categories: three categories in which esterase patterns were observed and one category in which esterase bands were not observed. On the basis of the 20 carbon sources assimilated, the C. albicans strains were categorized into 11 biotypes with the major biotype accounting for 21 (45.7%) strains. The examination of proteolytic activity using casein and albumin enabled to divide the strains into four groups. All of the examined strains belonged to serotype A and all of them expressed lipolytic activity. Esterase electrophoretic patterns and biotypes based on proteolytic activities were compared with the ability to assimilate carbon from various sources.
Sexually transmitted diseases are a major cause of acute disease worldwide, and trichomoniasis is the most common and curable disease, generating more than 170 million cases annually worldwide. Trichomonas vaginalis is the causal agent of trichomoniasis and has the ability to destroy in vitro cell monolayers of the vaginal mucosa, where the phospholipases A2 (PLA2) have been reported as potential virulence factors. These enzymes have been partially characterized from the subcellular fraction S30 of pathogenic T. vaginalis strains. The main objective of this study was to purify a phospholipase A2 from T. vaginalis, make a partial characterization, obtain a partial amino acid sequence, and determine its enzymatic participation as hemolytic factor causing lysis of erythrocytes. Trichomonas S30, RF30 and UFF30 sub-fractions from GT-15 strain have the capacity to hydrolyze [2-14C-PA]-PC at pH 6.0. Proteins from the UFF30 sub-fraction were separated by affinity chromatography into two eluted fractions with detectable PLA A2 activity. The EDTA-eluted fraction was analyzed by HPLC using on-line HPLC-tandem mass spectrometry and two protein peaks were observed at 8.2 and 13 kDa. Peptide sequences were identified from the proteins present in the eluted EDTA UFF30 fraction; bioinformatic analysis using Protein Link Global Server charged with T. vaginalis protein database suggests that eluted peptides correspond a putative ubiquitin protein in the 8.2 kDa fraction and a phospholipase preserved in the 13 kDa fraction. The EDTA-eluted fraction hydrolyzed [2-14C-PA]-PC lyses erythrocytes from Sprague-Dawley in a time and dose-dependent manner. The acidic hemolytic activity decreased by 84% with the addition of 100 μM of Rosenthal’s inhibitor.
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