Phosphoproteome profiling of the sexually transmitted pathogen Trichomonas vaginalis
Yuan-Ming Yeh, Kuo-Yang Huang, Ruei-Chi Richie Gan, Hsien-Da Huang, Tzu-Chien V. Wang, Petrus Tang
Received: May 23, 2012 Revised: June 13, 2012 Accepted: August 23, 2012
Corresponding author. Molecular Regulation and Bioinformatics Laboratory, Department of Parasitology, College of Medicine, Chung
Gung University, 259 Wenhwa 1st Road, Kweishan, Taoyuan 333, Taiwan.
E-mail address: email@example.com (P. Tang).
Background and purpose:
Trichomoniasis caused by Trichomonas vaginalis is the most common non-viral sexually transmitted infection. Morphological transformation from the trophozoite stage to the amoeboid or pseudocyst stage is crucial for T. vaginalis infection and survival. Protein phosphorylation is a key post-translational modification involved in the regulation of several biological processes in various prokaryotes and eukaryotes. More than 880 protein kinases have been identified in the T. vaginalis genome. However, little is known about the phosphorylation of specific proteins and the distribution of phosphorylated proteins in different stages of the morphological transformation of T. vaginalis.
To obtain a more comprehensive understanding of the T. vaginalis phosphoproteome, we analyzed phosphorylated proteins in the three morphological stages using titanium dioxide combined with LC-MS/MS.
A total of 93 phosphopeptides originating from 82 unique proteins were identified. Among these proteins, 21 were detected in all stages, 29 were identified in two different stages, and 32 were stage specific.
Identification of stage-specific phosphorylated proteins indicates that phosphorylation of these proteins may play a key role in the morphological transformation of T. vaginalis.
Phosphoproteome, Titanium dioxide enrichment, Trichomonas vaginalis