Phosphoproteome profiling of the sexually transmitted pathogen Trichomonas vaginalis

Journal of Microbiology, Immunology and Infection

Volumn 46, Issue 5, 2013, Pages 366-373

  Yeh, Yuan Ming ^a   Huang, Kuo Yang ^a   Richie Gan, Ruei Chi ^b,c   Huang, Hsien Da ^c   Wang, Tzu Chien V ^a   Tang, Petrus ^a,b  

^a CHANG GUNG UNIVERSITY COLLEGE OF MEDICINE   (Taiwan)

^b CHANG GUNG UNIVERSITY   (Taiwan)

^c NATIONAL CHIAO TUNG UNIVERSITY   (Taiwan)

Author keywords

Phosphoproteome; Titanium dioxide enrichment; Trichomonas vaginalis

Indexed keywords

PHOSPHOPROTEIN; TITANIUM DIOXIDE;

ARTICLE; LIQUID CHROMATOGRAPHY; NONHUMAN; PROTEIN PHOSPHORYLATION; TANDEM MASS SPECTROMETRY; TRICHOMONAS VAGINALIS;

PHOSPHOPROTEOME; TITANIUM DIOXIDE ENRICHMENT; TRICHOMONAS VAGINALIS;

CHROMATOGRAPHY, LIQUID; GENE EXPRESSION PROFILING; PHOSPHOPROTEINS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEOME; PROTOZOAN PROTEINS; TANDEM MASS SPECTROMETRY; TRICHOMONAS VAGINALIS;

EID: 84885191082     PISSN: 16841182     EISSN: 19959133     Source Type: Journal    
DOI: 10.1016/j.jmii.2012.07.010     Document Type: Article

References (40)

1. Petrin D., Delgaty K., Bhatt R., Garber G. Clinical and microbiological aspects of Trichomonas vaginalis. Clin Microbiol Rev 1998, 11:300-317.
2. McLaren L.C., Davis L.E., Healy G.R., James C.G. Isolation of Trichomonas vaginalis from the respiratory tract of infants with respiratory disease. Pediatrics 1983, 71:888-890.
3. Cotch M.F., Pastorek J.G., Nugent R.P., Hillier S.L., Gibbs R.S., Martin D.H., et al. Trichomonas vaginalis associated with low birth weight and preterm delivery. The Vaginal Infections and Prematurity Study Group. Sex Transm Dis 1997, 24:353-360.
4. Sorvillo F., Kerndt P. Trichomonas vaginalis and amplification of HIV-1 transmission. Lancet 1998, 351:213-214.
5. Arroyo R., Engbring J., Alderete J.F. Molecular basis of host epithelial cell recognition by Trichomonas vaginalis. Mol Microbiol 1992, 6:853-862.
6. Moreno-Brito V., Yanez-Gomez C., Meza-Cervantez P., Avila-Gonzalez L., Rodriguez M.A., Ortega-Lopez J., et al. A Trichomonas vaginalis 120 kDa protein with identity to hydrogenosome pyruvate:ferredoxin oxidoreductase is a surface adhesin induced by iron. Cell Microbiol 2005, 7:245-258.
7. Hernandez H., Sariego I., Garber G., Delgado R., Lopez O., Sarracent J. Monoclonal antibodies against a 62 kDa proteinase of Trichomonas vaginalis decrease parasite cytoadherence to epithelial cells and confer protection in mice. Parasite Immunol 2004, 26:119-125.
8. Lama A., Kucknoor A., Mundodi V., Alderete J.F. Glyceraldehyde-3-phosphate dehydrogenase is a surface-associated, fibronectin-binding protein of Trichomonas vaginalis. Infect Immun 2009, 77:2703-2711.
9. Okumura C.Y., Baum L.G., Johnson P.J. Galectin-1 on cervical epithelial cells is a receptor for the sexually transmitted human parasite Trichomonas vaginalis. Cell Microbiol 2008, 10(10):2078-2090.
10. Pereira-Neves A., Ribeiro K.C., Benchimol M. Pseudocysts in trichomonads - new insights. Protist 2003, 154:313-329.
11. Lipman N.S., Lampen N., Nguyen H.T. Identification of pseudocysts of Tritrichomonas muris in Armenian hamsters and their transmission to mice. Lab Anim Sci 1999, 49:313-315.
12. Pereira-Neves A., Benchimol M. Tritrichomonas foetus: budding from multinucleated pseudocysts. Protist 2009, 160:536-551.
13. Zolnierowicz S., Bollen M. Protein phosphorylation and protein phosphatases. EMBO J 2000, 19:483-488. De Panne, Belgium, September 19-24, 1999.
14. Carlton J.M., Hirt R.P., Silva J.C., Delcher A.L., Schatz M., Zhao Q., et al. Draft genome sequence of the sexually transmitted pathogen Trichomonas vaginalis. Science 2007, 315:207-212.
15. Diamond L.S., Clark C.G., Cunnick C.C. YI-S, a casein-free medium for axenic cultivation of Entamoeba histolytica, related Entamoeba, Giardia intestinalis and Trichomonas vaginalis. J Eukaryot Microbiol 1995, 42:277-278.
16. Wu C.C., Hsu C.W., Chen C.D., Yu C.J., Chang K.P., Tai D.I., et al. Candidate serological biomarkers for cancer identified from the secretomes of 23 cancer cell lines and the human protein atlas. Mol Cell Proteomics 2010, 9:1100-1117.
17. Craig R., Beavis R.C. TANDEM: matching proteins with tandem mass spectra. Bioinformatics 2004, 20:1466-1467.
18. Conesa A., Gotz S., Garcia-Gomez J.M., Terol J., Talon M., Robles M. Blast2GO: a universal tool for annotation, visualization and analysis in functional genomics research. Bioinformatics 2005, 21:3674-3676.
19. Aitken A. 14-3-3 proteins: a historic overview. Semin Cancer Biol 2006, 16:162-172.
20. Siles-Lucas Mdel M., Gottstein B. The 14-3-3 protein: a key molecule in parasites as in other organisms. Trends Parasitol 2003, 19:575-581.
21. Al-Khedery B., Barnwell J.W., Galinski M.R. Stage-specific expression of 14-3-3 in asexual blood-stage Plasmodium. Mol Biochem Parasitol 1999, 102:117-130.
22. Koyama T., Ohsawa T., Shimada S., Omata Y., Xuan X., Inoue N., et al. A 14-3-3 protein homologue is expressed in feline enteroepithelial-stages of Toxoplasma gondii. Vet Parasitol 2001, 96:65-74.
23. Huang K.Y., Chien K.Y., Lin Y.C., Hsu W.M., Fong I.K., Huang P.J., et al. A proteome reference map of Trichomonas vaginalis. Parasitol Res 2009, 104:927-933.
24. Wellerson R., Kupferberg A.B. On glycolysis in Trichomonas vaginalis. J Protozool 1962, 9:418-424.
25. Ekman P., Nilsson E. Phosphorylation of glucokinase from rat liver invitro by protein kinase A with a concomitant decrease of its activity. Arch Biochem Biophys 1988, 261:275-282.
26. Munoz-Alonso M.J., Guillemain G., Kassis N., Girard J., Burnol A.F., Leturque A. A novel cytosolic dual specificity phosphatase, interacting with glucokinase, increases glucose phosphorylation rate. J Biol Chem 2000, 275:32406-32412.
27. Agius L. Glucokinase and molecular aspects of liver glycogen metabolism. Biochem J 2008, 414:1-18.
28. 4UGA stop codon located in the A site of eukaryotic ribosomes. Eur J Biochem 2001, 268:2896-2904.
29. Frolova L., Le Goff X., Zhouravleva G., Davydova E., Philippe M., Kisselev L. Eukaryotic polypeptide chain release factor eRF3 is an eRF1- and ribosome-dependent guanosine triphosphatase. RNA 1996, 2:334-341.
30. Chauvin C., Salhi S., Jean-Jean O. Human eukaryotic release factor 3a depletion causes cell cycle arrest at G1 phase through inhibition of the mTOR pathway. Mol Cell Biol 2007, 27:5619-5629.
31. Sontag E. Protein phosphatase 2A: the Trojan horse of cellular signaling. Cell Signal 2001, 13:7-16.
32. Janssens V., Goris J. Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem J 2001, 353:417-439.
33. Sontag J.M., Sontag E. Regulation of cell adhesion by PP2A and SV40 small tumor antigen: an important link to cell transformation. Cell Mol Life Sci 2006, 63:2979-2991.
34. Pais S.M., Tellez-Inon M.T., Capiati D.A. Serine/threonine protein phosphatases type 2A and their roles in stress signaling. Plant Signal Behav 2009, 4:1013-1015.
35. 2+ signaling and calcium binding chaperones of the endoplasmic reticulum. Cell Calcium 2002, 32:269-278.
36. Gonzalez E., de Leon Mdel C., Meza I., Ocadiz-Delgado R., Gariglio P., Silva-Olivares A., et al. Entamoeba histolytica calreticulin: an endoplasmic reticulum protein expressed by trophozoites into experimentally induced amoebic liver abscesses. Parasitol Res 2011, 108:439-449.
37. Ferreira V., Valck C., Sanchez G., Gingras A., Tzima S., Molina M.C., et al. The classical activation pathway of the human complement system is specifically inhibited by calreticulin from Trypanosoma cruzi. J Immunol 2004, 172:3042-3050.
38. Ramirez G., Valck C., Molina M.C., Ribeiro C.H., Lopez N., Sanchez G., et al. Trypanosoma cruzi calreticulin: a novel virulence factor that binds complement C1 on the parasite surface and promotes infectivity. Immunobiology 2010, 216:265-273.
39. Coppolino M.G., Woodside M.J., Demaurex N., Grinstein S., St-Arnaud R., Dedhar S. Calreticulin is essential for integrin-mediated calcium signalling and cell adhesion. Nature 1997, 386:843-847.
40. Castaneda-Patlan M.C., Razo-Paredes R., Carrisoza-Gaytan R., Gonzalez-Mariscal L., Robles-Flores M. Protein kinase C is involved in the regulation of several calreticulin posttranslational modifications. Int J Biochem Cell Biol 2009, 42:120-131.