Differential soluble protein expression between Trichomonas vaginalis isolates exhibiting low and high virulence phenotypes

Journal of Proteomics

Volumn 71, Issue 1, 2008, Pages 109-122

  Cuervo, Patrícia ^a   Cupolillo, Elisa ^a   Britto, Constança ^a   González, Luis Javier ^b   e Silva Filho, Fernando Costa ^c   Lopes, Letícia Coutinho ^a   Domont, Gilberto Barbosa ^c   De Jesus, Jose Batista ^a,d  

^a INSTITUTO OSWALDO CRUZ   (Brazil)

^b CENTER FOR GENETIC ENGINEERING AND BIOTECHNOLOGY   (Cuba)

^c FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

^d FEDERAL UNIVERSITY OF SÃO JOÃO DEL REI   (Brazil)

Author keywords

Differential proteomic analysis; Human urogenital trichomoniasis; Mass spectrometry; Trichomonas vaginalis; Two dimensional electrophoresis

Indexed keywords

ACTIN; FRUCTOSE BISPHOSPHATE ALDOLASE; ISOENZYME; ISOPROTEIN; MALATE DEHYDROGENASE; ORNITHINE CYCLODEAMIDASE;

ADHESION; AMOEBA; ARTICLE; COMPARATIVE STUDY; CYTOSKELETON; ENERGY TRANSFER; HOST CELL; HOST PARASITE INTERACTION; MASS SPECTROMETRY; NONHUMAN; NUCLEOTIDE SEQUENCE; PARASITE ISOLATION; PARASITE VIRULENCE; PATHOGENESIS; PHENOTYPE; POLYAMINE METABOLISM; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEOMICS; SIGNAL TRANSDUCTION; TRICHOMONAS VAGINALIS; TWO DIMENSIONAL GEL ELECTROPHORESIS;

ANIMALS; CELLS, CULTURED; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; GENE EXPRESSION REGULATION; IMAGE PROCESSING, COMPUTER-ASSISTED; PHENOTYPE; PROTOZOAN PROTEINS; SOLUBILITY; TRICHOMONAS VAGINALIS; VIRULENCE;

PROTOZOA; TRICHOMONAS VAGINALIS;

EID: 44049087806     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2008.01.010     Document Type: Article

References (63)

1. World Health Organization. Global program on AIDS (1995), World Health Organization, Geneva 2-27
2. De Jesus J.B., and Silva Filho F.C. In: Coura J.R. (Ed). Dinâmica das Doenças Infecciosas (2005), Guanabara Koogan Editorial, Rio de Janeiro 753-769
3. Minkoff H., Grunebaum A.N., Schwarz R.H., Feldman J., Cummings M., Crombleholme W., et al. Risk factors for prematurity and premature rupture of membranes: a prospective study of the vaginal flora in pregnancy. Am J Obstet Gynecol 150 (1984) 965-972
4. Cotch M.F., Pastorek II 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 24 (1997) 353-360
5. Zhang Z.F., and Begg C.B. Is Trichomonas vaginalis a cause of cervical neoplasia? Results from a combined analysis of 24 studies. Int J Epidemiol 23 (1994) 682-690
6. Kharsany A.B., Hoosen A.A., Moodley J., Bagaratee J., and Gouws E. The association between sexually transmitted pathogens and `cervical intra-epithelial neoplasia in a developing community. Genitourin Med 69 (1993) 357-360
7. Grodstein F., Goldman M.B., and Cramer D.W. Relation of tubal infertility to history of sexually transmitted diseases. Am J Epidemiol 137 (1993) 577-584
8. Yap E.H., Ho T.H., Chan Y.C., Thong T.W., Ng G.C., Ho L.C., et al. Serum antibodies to Trichomonas vaginalis in invasive cervical cancer patients. Genitourin Med 71 (1995) 402-404
9. Sorvillo F., and Kerndt P. Trichomonas vaginalis and amplification of HIV-1 transmission. Lancet 351 (1998) 213-214
10. Sorvillo F., Smith L., Kerndt P., and Ash L. Trichomonas vaginalis, HIV, and African-Americans. Emerg Infect Dis 7 (2001) 927-932
11. Chesson H.W., Blandford J.M., and Pinkerton S.D. Estimates of the annual number and cost of new HIV infections among women attributable to trichomoniasis in the United States. Sex Transm Dis 31 (2004) 547-551
12. Petrin D., Delgaty K., Bhatt R., and Garber G. Clinical and microbiological aspects of Trichomonas vaginalis. Clin Microbiol Rev 11 (1998) 300-317
13. Honigberg B.M., and Brugerolle G. Structure. In: Honigberg B.M. (Ed). Trichomonads parasitic in humans (1990), Springer-Verlag, New York 5-35
14. Benchimol M. Trichomonads under microscopy. Microsc Microanal 10 (2004) 528-550
15. Müller M. The hydrogenosome. J Gen Microbiol 139 (1993) 2879-2889
16. Arroyo R., González-Robles A., Martínez-Palomo A., and Alderete J.F. Signalling of Trichomonas vaginalis for amoeboid transformation and adhesion synthesis follows cytoadherence. Mol Microbiol 7 (1993) 299-309
17. Rendón-Maldonado J.G., Espinosa-Cantellano M., González-Robles A., and Martínez-Palomo A. Trichomonas vaginalis: in vitro phagocytosis of lactobacilli, vaginal epithelial cells, leukocytes, and erythrocytes. Exp Parasitol 89 (1998) 241-250
18. Fiori P.L., Rappelli P., and Addis M.F. The flagellated parasite Trichomonas vaginalis: new insights into cytopathogenicity mechanisms. Microbes Infect 1 (1999) 149-156
19. Moreno-Brito V., Yáñez-Gómez C., Meza-Cervantez P., Avila-González L., Rodríguez M.A., Ortega-López 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 7 (2005) 245-258
20. Heath J.P. Behaviour and pathogenicity of Trichomonas vaginalis in epithelial cell cultures: a study by light and scanning electron microscopy. Br J Vener Dis 57 (1981) 106-117
21. Krieger J.N., Ravdin J.I., and Rein M.F. Contact-dependent cytopathogenic mechanisms of Trichomonas vaginalis. Infect Immun 50 (1985) 778-786
22. Alderete J.F., Arroyo R., and Lehker M.W. Analysis for adhesins and specific cytoadhesion of Trichomonas vaginalis. Methods Enzymol 253 (1995) 407-414
23. Gilbert R.O., Elia G., Beach D.H., Klaessig S., and Singh B.N. Cytopathogenic effect of Trichomonas vaginalis on human vaginal epithelial cells cultured in vitro. Infect Immun 68 (2000) 4200-4206
24. Rasmussen S.E., Nielsen M.H., Lind I., and Rhodes J.M. Morphological studies of the cytotoxicity of Trichomonas vaginalis to normal human vaginal epithelial cells in vitro. Genitourin Med 62 (1986) 240-246
25. Arroyo R., Engbring J., and Alderete J.F. Molecular basis of host epithelial cell recognition by Trichomonas vaginalis. Mol Microbiol 6 (1992) 853-862
26. Pereira-Neves A., and Benchimol M. Phagocytosis by Trichomonas vaginalis: new insights. Biol Cell 99 (2007) 87-101
27. Kucknoor A.S., Mundodi V., and Alderete J.F. Adherence to human vaginal epithelial cells signals for increased expression of Trichomonas vaginalis genes. Infect Immun 73 (2005) 6472-6478
28. Jesus J.B., Vannier-Santos M.A., Britto C., Godefroy P., Silva-Filho F.C., Pinheiro A.A., et al. Trichomonas vaginalis virulence against epithelial cells and morphological variability: the comparison between a well-established strain and a fresh isolate. Parasitol Res 93 (2004) 369-377
29. Costa e Silva Filho F., Elias C.A., and de Souza W. Further studies on the surface charge of various strains of Trichomonas vaginalis and Tritrichomonas foetus. Cell Biophys 8 (1986) 161-176
30. Diamond L.S. The establishment of various trichomonads of animals and men in axenic culture. J Parasitol 43 (1957) 488-490
31. De Jesus J.B., Ferreira M.A., Cuervo P., Britto C., e Silva-Filho F.C., and Meyer-Fernandes J.R. Iron modulates ecto-phosphohydrolase activities in pathogenic trichomonads. Parasitol Int 55 (2006) 285-290
32. Cuervo P., de Jesus J.B., Junqueira M., Mendonça-Lima L., González L.J., Betancourt L., et al. Proteome analysis of Leishmania (Viannia) braziliensis by two-dimensional gel electrophoresis and mass spectrometry. Mol Biochem Parasitol 154 (2007) 6-21
33. De Jesus J.B., Cuervo P., Junqueira M., Britto C., Silva-Filho F.C., Soares M.J., et al. A further proteomic study on the effect of iron in the human pathogen Trichomonas vaginalis. Proteomics 7 (2007) 1961-1972
34. Neuhoff V., Arold N., Taube D., and Ehrhardt W. Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 9 (1988) 255-262
35. Cupolillo E., Grimaldi Jr. G., and Momen H. A general classification of New World Leishmania using numerical zymotaxonomy. Am J Trop Med Hyg 50 (1994) 296-311
36. Marrero J., González L.J., Sánchez A., Ayala M., Paz-Lago D., González W., et al. Effect of high concentration of Co (II) on Enterobacter liquefaciens strain C-1: a bacterium highly resistant to heavy metals with an unknown genome. Proteomics 4 (2004) 1265-1279
37. Nugent P.G., Karsani S.A., Wait R., Tempero J., and Smith D.F. Proteomic analysis of Leishmania mexicana differentiation. Mol Biochem Parasitol 136 (2004) 51-62
38. Yuan J., Zhu L., Liu X., Li T., Zhang Y., Ying T., et al. A proteome reference map and proteomic analysis of Bifidobacterium longum NCC2705. Mol Cell Proteomics 5 (2006) 1105-1118
39. Kabsch W., and Vandekerckhove J. Structure and function of actin. Annu Rev Biophys Biomol Struct 21 (1992) 49-76
40. Bricheux G., and Brugerolle G. Molecular cloning of actin genes in Trichomonas vaginalis and phylogeny inferred from actin sequences. FEMS Microbiol Lett 153 (1997) 205-213
41. De Jesus J.B., Cuervo P., Junqueira M., Britto C., Silva-Filho F.C., Sabóia-Vahia L., et al. Application of two-dimensional electrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry for proteomic analysis of the sexually transmitted parasite Trichomonas vaginalis. J Mass Spectrom 42 (2007) 1463-1473
42. de Hostos E.L. The coronin family of actin-associated proteins. Trends Cell Biol 9 (1999) 345-350
43. Bricheux G., Coffe G., Bayle D., and Brugerolle G. Characterization, cloning and immunolocalization of a coronin homologue in Trichomonas vaginalis. Eur J Cell Biol 79 (2000) 413-422
44. Fu H., Subramanian R.R., and Masters S.C. 14-3-3 proteins: structure, function, and regulation. Annu Rev Pharmacol Toxicol 40 (2000) 617-647
45. van Hemert M.J., Steensma H.Y., and van Heusden G.P. 14-3-3 proteins: key regulators of cell division, signalling and apoptosis. BioEssays 23 (2001) 936-946
46. Hermeking H., and Benzinger A. 14-3-3 proteins in cell cycle regulation. Semin Cancer Biol 16 (2006) 183-192
47. Bhattacharya S., Bunick C.G., and Chazin W.J. Target selectivity in EF-hand calcium binding proteins. Biochim Biophys Acta 1742 (2004) 69-79
48. Grabarek Z. Structural basis for diversity of the EF-hand calcium-binding proteins. J Mol Biol 359 (2006) 509-525
49. Brugerolle G., Bricheux G., and Coffe G. Centrin protein and genes in Trichomonas vaginalis and close relatives. J Eukaryot Microbiol 47 (2000) 129-138
50. Coombs G.H., and North M.J. An analysis of the proteinases of Trichomonas vaginalis by polyacrylamide gel electrophoresis. Parasitology 86 (1983) 1-6
51. Lockwood B.C., North M.J., Scott K.I., Bremner A.F., and Coombs G.H. The use of a highly sensitive electrophoretic method to compare the proteinases of trichomonads. Mol Biochem Parasitol 24 (1987) 89-95
52. Hernandez-Gutierrez R., Ortega-López J., and Arroyo R. A 39-kDa cysteine proteinase CP39 from Trichomonas vaginalis, which is negatively affected by iron may be involved in trichomonal cytotoxicity. J Eukaryot Microbiol 50 Suppl (2003) 696-698
53. Sommer U., Costello C.E., Hayes G.R., Beach D.H., Gilbert R.O., Lucas J.J., et al. Identification of Trichomonas vaginalis cysteine proteases that induce apoptosis in human vaginal epithelial cells. J Biol Chem 280 (2005) 23853-23860
54. Wu G., Fiser A., ter Kuile B., Sali A., and Müller M. Convergent evolution of Trichomonas vaginalis lactate dehydrogenase from malate dehydrogenase. Proc Natl Acad Sci U S A 96 (1999) 6285-6290
55. Kleydman Y., Yarlett N., and Gorrell T.E. Production of ammonia by Tritrichomonas foetus and Trichomonas vaginalis. Microbiology 150 (2004) 1139-1145
56. 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 315 (2007) 207-212
57. Yarlett N., Martinez M.P., Goldberg B., Kramer D.L., and Porter C.W. Dependence of Trichomonas vaginalis upon polyamine backconversion. Microbiology 146 (2000) 2715-2722
58. Garcia A.F., Benchimol M., and Alderete J.F. Trichomonas vaginalis polyamine metabolism is linked to host cell adherence and cytotoxicity. Infect Immun 73 (2005) 2602-2610
59. Andrulis I.L., Chen J., and Ray P.N. Isolation of human cDNAs for asparagine synthetase and expression in Jensen rat sarcoma cells. Mol Cell Biol 7 (1987) 2435-2443
60. Gong S.S., Guerrini L., and Basilico C. Regulation of asparagine synthetase gene expression by amino acid starvation. Mol Cell Biol 11 (1991) 6059-6066
61. Ponting C.P., and Aravind L. START: a lipid-binding domain in StAR, HD-ZIP and signalling proteins. Trends Biochem Sci 24 (1999) 130-132
62. Tibayrenc M., Kjellberg F., and Ayala F.J. A clonal theory of parasitic protozoa: the population structures of Entamoeba, Giardia, Leishmania, Naegleria, Plasmodium, Trichomonas, and Trypanosoma and their medical and taxonomical consequences. Proc Natl Acad Sci U S A 87 (1990) 2414-2418
63. López L.B., Braga M.B., López J.O., Arroyo R., and Costa e Silva Filho F. Strategies by which some pathogenic trichomonads integrate diverse signals in the decision-making process. An Acad Bras Cienc 72 (2000) 173-186