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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Escobedo-Guajardo, Brenda L. González-Salazar, Francisco Palacios-Corona, Rebeca Torres de la Cruz, Víctor M. Morales-Vallarta, Mario Mata-Cárdenas, Benito D. Garza-González, Jesús N. Rivera-Silva, Gerardo Vargas-Villarreal, Javier
Description	Author Affiliation: Escobedo-Guajardo BL ( División de Biología Celular y Molecular, Centro de Investigación Biomédica del Noreste, Instituto Mexicano del Seguro Social. Administración de Correo No. 4, Apartado Postal 020-E, Colonia Independencia, Monterrey Nuevo León, México.)
Abstract	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-(14)C-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-(14)C-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.
File Format	HTM / HTML
ISSN	12302821
Issue Number	4
Volume Number	58
e-ISSN	18961851
Journal	Acta Parasitologica
Language	English
Publisher	De Gruyter
Publisher Date	2013-12-01
Publisher Place	Poland
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Parasitology Phospholipases A2 Isolation & Purification Metabolism Trichomonas Vaginalis Enzymology Amino Acid Sequence Animals Chromatography, Affinity Chromatography, High Pressure Liquid Erythrocytes Drug Effects Hemolysis Hydrogen-ion Concentration Molecular Weight Chemistry Genetics Rats Rats, Sprague-dawley Tandem Mass Spectrometry Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Parasitology

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