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Abstrakty
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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Tom
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Opis fizyczny
p.519-526,fig.,ref.
Twórcy
autor
- Division de Biologia Celular y Molecular, Centro de Investigacion Biomedica del Noreste, Instituto Mexicano del Seguro Social. Administracion de Correo No. 4, Apartado Postal 020-E Colonia Independencia, Monterrey Nuevo Leon, Mexico
autor
- Division de Biologia Celular y Molecular, Centro de Investigacion Biomedica del Noreste, Instituto Mexicano del Seguro Social. Administracion de Correo No. 4, Apartado Postal 020-E Colonia Independencia, Monterrey Nuevo Leon, Mexico
autor
- Division de Biologia Celular y Molecular, Centro de Investigacion Biomedica del Noreste, Instituto Mexicano del Seguro Social. Administracion de Correo No. 4, Apartado Postal 020-E Colonia Independencia, Monterrey Nuevo Leon, Mexico
autor
- Division de Biologia Celular y Molecular, Centro de Investigacion Biomedica del Noreste, Instituto Mexicano del Seguro Social. Administracion de Correo No. 4, Apartado Postal 020-E Colonia Independencia, Monterrey Nuevo Leon, Mexico
autor
- Departamento de Biologia Celular y Genetica, Facultad de Ciencias Biologicas, Universidad Autonoma de Nuevo Leon, San Nicolas de los Garza, C.P. 66451, Nuevo Leon, Mexico
autor
- Facultad de Ciencias Quimicas, Universidad Autonoma de Nuevo Leon, Av. Manuel L Barragan S/N, San Nicolas de los Garza, Nuevo Leon, Mexico
autor
- Division de Biologia Celular y Molecular, Centro de Investigacion Biomedica del Noreste, Instituto Mexicano del Seguro Social. Administracion de Correo No. 4, Apartado Postal 020-E Colonia Independencia, Monterrey Nuevo Leon, Mexico
autor
- Departamento de Ciencias Basicas, Division de Ciencias de la Salud, Universidad de Monterrey, Av. Morones Prieto 4500 Pte. San Pedro Garza Garcia, C.P. 66238, Nuevo Leon, Mexico
autor
- Division de Biologia Celular y Molecular, Centro de Investigacion Biomedica del Noreste, Instituto Mexicano del Seguro Social. Administracion de Correo No. 4, Apartado Postal 020-E Colonia Independencia, Monterrey Nuevo Leon, Mexico
Bibliografia
- Barbour S.E., Marciano-Cabral F. 2001. Naegleria fowleri amoebae express a membrane-associated calcium-independent phospholipase A(2). Biochimica et Biophysica Acta, 1530, 123–33.
- Cohn S.E., Clark R.A. 2003. Sexually transmitted diseases, HIV, and AIDS in women. Medical Clinics of North America, 87, 971–95.
- Demirezen S. 2001. Phagocytosis of erythrocytes by Trichomonas vaginalis: examination of a cervicovaginal smear. Diagnostic Cytopathology, 24, 435.
- Diamond L.S., Harlow D.R., Cunnick C.C. 1978. A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoeba. Transactions of the Royal Society of Tropical Medicine and Hygiene, 72, 431–432.
- Gilbert R.O., Elia G., Beach D.H., Klaessig S., Singh B.N. 2000. Cytopathogenic effect of Trichomonas vaginalis on human vaginal epithelial cells cultured in vitro. Infection and Immunity, 68, 4200–6.
- González-Garza M.T., Castro-Garza J., Cruz-Vega D.E., Vargas-Villarreal J., Carranza-Rosales P., Mata-Cárdenas B.D., Siller-Campos L., Said-Fernández S. 2000. Entamoeba histolytica: diminution of erythrophagocytosis, phospholipase A(2), and hemolytic activities is related to virulence impairment in longterm axenic cultures. Experimental Parasitology, 96, 116–119.
- González-Robles A., Lázaro-Haller A., Espinosa-Cantellano M., Anaya-Velázquez F., Martínez-Palomo A. 1995. Trichomonas vaginalis: ultrastructural bases of the cytopathic effect. Journal of Eukaryotic Microbiology, 42, 641–651.
- Gülmezoglu A.M., Forna F. 2000. Interventions for treating trichomoniasis in women. Cochrane Database of Systematic Reviews, 2: CD000218.
- Heath J.P. 1981. Behaviour and pathogenicity of Trichomonas vaginalis in epithelial cell cultures: a study by light and scanning electron microscopy. British Journal of Venereal Diseases, 57106–17.
- Keeling P.J., Doolittle W.F. 1995. Concerted evolution in protists: recent homogenization of a polyubiquitin gene in Trichomonas vaginalis. Journal of Molecular Evolution, 41, 556–62.
- Long-Krug S.A., Fischer K.J., Hysmith R.M., Ravdin J.I. 1985. Phospholipase A enzymes of Entamoeba histolytica: description and subcellular localization. Journal of Infectious Diseases, 152, 536–541.
- Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. 1951. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry, 193, 265–275.
- Lubick K.J., Burgess D.E. 2004. Purification and analysis of a phospholipase A2-like lytic factor of Trichomonas vaginalis. Infection and Immunity, 72, 1284–1290.
- Padilla-Vaca F., Anaya-Velázquez F. 1997. Biochemical properties of a neuraminidase of Trichomonas vaginalis. Journal of Parasitology, 83, 1001–1006.
- Rendón-Maldonado J.G., Espinosa-Cantellano M., González-Robles A., Martínez-Palomo A. 1998. Trichomonas vaginalis: in vitro phagocytosis of lactobacilli, vaginal epithelial cells, leukocytes, and erythrocytes. Experimental Parasitology, 89, 241–250.
- Said-Fernández S., Vargas-Villarreal J., Castro-Garza J., Mata-Cárdenas B.D., Navarro-Marmolejo L., Lozano-Garza G., Martínez-Rodríguez H. 1988. PEHPS medium: an alternative for axenic cultivation of Entamoeba histolytica and E. invadens. Transactions of the Royal Society of Tropical Medicine and Hygiene, 82, 249–253.
- Skispky J.P., Barclay M. 1969. Thin-layer chromatography of lipids. In: Methods in Enzymology, Lowestein J.M. 14 ed. Academic Press, New York, 530–599.
- Sutton M., Sternberg M., Koumans E.H., McQuillan G., Berman S., Markowitz L. 2007. The prevalence of Trichomonas vaginalis infection among reproductive-age women in the United States, 2001–2004. Clinical Infectious Diseases, 45, 1319–1326.
- Vargas-Villarreal J., Martín-Polo J.J., Reinaud E., Alagón A.C. 1991. A new affinity adsorbent for the purification of phospholipases A1 and A2 from animal venoms. Toxicon, 29, 119–24.
- Vargas-Villarreal J., Martínez-Rodríguez H.G., Castro-Garza J., Mata-Cárdenas B.D., González-Garza M.T., Said-Fernández S. 1995. Identification of Entamoeba histolytica intracellular phospholipase A and lysophospholipase L1 activities. Parasitology Research, 81, 320–323.
- Vargas-Villarreal J., Olvera-Rodríguez A., Mata-Cárdenas B.D., Martínez-Rodríguez H., Said-Fernández S., Alagón-Cano A. 1998. Isolation of an Entamoeba histolytica intracellular alkaline phospholipase A2. Parasitology Research, 84, 310–314.
- Vargas-Villarreal J., Mata-Cárdenas B.D., González-Salazar F., Lozano-Garza H.G., Cortes-Gutierrez E.I., Palacios-Corona R., Martínez-Rodríguez H.G., Ramírez-Bon E., Said-Fernández S. 2003. Trichomonas vaginalis: identification of a phospholipase A-dependent hemolytic activity in a vesicular subcellular fraction. Journal of Parasitology, 89, 105–12.
- Vargas-Villarreal J., Mata-Cárdenas B.D., Palacios-Corona R., Gonzalez-Salazar F., Cortes-Gutierrez E.I., Martinez-Rodriguez H.G., Said-Fernández S. 2005. Trichomonas vaginalis: identification of soluble and membrane-associated phospholipase A1 and A2 activities with direct and indirect hemolytic effects. Journal of Parasitology 91, 5–11.
- Van den Bosch H. 1980. Intracellular phospholipases A. Biochimica et Biophysica Acta, 604, 191–246.
- Wainszelbaum M., Isola, E., Wilkowsky S., Cannata J.J., Florin-Christensen J., Florin-Christensen M. 2001. Lysosomal phospholipase A1 in Trypanosoma cruzi: an enzyme with a possible role in the pathogenesis of Chagas’ disease. Biochemical Journal, 355, 765–70.
- WHO — World Health Organization 2010. [homepage on the Internet]. [accessed 30 April 2011]. Available from: http://whqlibdoc.who.int/hq/2001/WHO_HIV_AIDS_2001.02.pdf.
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Bibliografia
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