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2013 | 58 | 4 |

Tytuł artykułu

Trichomonas vaginalis acidic phospholipase A2: isolation and partial amino acid sequence

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
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.

Wydawca

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Czasopismo

Rocznik

Tom

58

Numer

4

Opis fizyczny

p.519-526,fig.,ref.

Twórcy

  • 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
  • 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
  • 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
  • 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
  • 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
  • Facultad de Ciencias Quimicas, Universidad Autonoma de Nuevo Leon, Av. Manuel L Barragan S/N, San Nicolas de los Garza, Nuevo Leon, Mexico
  • 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
  • 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
  • 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

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Typ dokumentu

Bibliografia

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