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BioMed Research International
Volume 2013 (2013), Article ID 561979, 18 pages
The TvLEGU-1, a Legumain-Like Cysteine Proteinase, Plays a Key Role in Trichomonas vaginalis Cytoadherence
1Departamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional, Avenida IPN No. 2508, Col. San Pedro Zacatenco, 07360 Mexico City, DF, Mexico
2Departamento de Biotecnología y Bioingeniería, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional, Avenida IPN No. 2508, Col. San Pedro Zacatenco, 07360 Mexico City, DF, Mexico
3Laboratório de Ultraestrutura Celular, Universidade Santa Úrsula, Rua Jornalista Orlando Dantas 36, Botafogo, 22231-010 Rio de Janeiro, RJ, Brazil
Received 31 July 2012; Revised 21 September 2012; Accepted 28 September 2012
Academic Editor: Luis I. Terrazas
Copyright © 2013 Francisco Javier Rendón-Gandarilla et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- D. Petrin, K. Delgaty, R. Bhatt, and G. Garber, “Clinical and microbiological aspects of Trichomonas vaginalis,” Clinical Microbiology Reviews, vol. 11, no. 2, pp. 300–317, 1998.
- J. F. Alderete and G. E. Garza, “Specific nature of Trichomonas vaginalis parasitism of host cell surfaces,” Infection and Immunity, vol. 50, no. 3, pp. 701–708, 1985.
- J. F. Alderete and G. E. Garza, “Identification and properties of Trichomonas vaginalis proteins involved in cytadherence,” Infection and Immunity, vol. 56, no. 1, pp. 28–33, 1988.
- R. Arroyo and J. F. Alderete, “Trichomonas vaginalis surface proteinase activity is necessary for parasite adherence to epithelial cells,” Infection and Immunity, vol. 57, no. 10, pp. 2991–2997, 1989.
- R. Arroyo and J. F. Alderete, “Two Trichomonas vaginalis surface proteinases bind to host epithelial cells and are related to levels of cytoadherence and cytotoxicity,” Archives of Medical Research, vol. 26, no. 3, pp. 279–285, 1995.
- R. Arroyo, J. Engbring, and J. F. Alderete, “Molecular basis of host epithelial cell recognition by Trichomonas vaginalis,” Molecular Microbiology, vol. 6, no. 7, pp. 853–862, 1992.
- M. R. Mendoza-Lopez, C. Becerril-Garcia, L. V. Fattel-Facenda et al., “CP30, a cysteine proteinase involved in Trichomonas vaginalis cytoadherence,” Infection and Immunity, vol. 68, no. 9, pp. 4907–4912, 2000.
- H. Hernández, I. Sariego, G. Garber, R. Delgado, O. López, and J. Sarracent, “Monoclonal antibodies against a 62 kDa proteinase of Trichomonas vaginalis decrease parasite cytoadherence to epithelial cells and confer protection in mice,” Parasite Immunology, vol. 26, no. 3, pp. 119–125, 2004.
- J. M. Carlton, R. P. Hirt, J. C. Silva et al., “Draft genome sequence of the sexually transmitted pathogen Trichomonas vaginalis,” Science, vol. 315, no. 5809, pp. 207–212, 2007.
- K. A. Neale and J. F. Alderete, “Analysis of the proteinases of representative Trichomonas vaginalis isolates,” Infection and Immunity, vol. 58, no. 1, pp. 157–162, 1990.
- P. Cuervo, E. Cupolillo, C. Britto et al., “Differential soluble protein expression between Trichomonas vaginalis isolates exhibiting low and high virulence phenotypes,” Journal of Proteomics, vol. 71, no. 1, pp. 109–122, 2008.
- J. B. De Jesus, P. Cuervo, M. Junqueira 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,” Journal of Mass Spectrometry, vol. 42, no. 11, pp. 1463–1473, 2007.
- J. B. De Jesus, P. Cuervo, C. Britto et al., “Cysteine peptidase expression in Trichomonas vaginalis isolates Displaying High- And low-virulence phenotypes,” Journal of Proteome Research, vol. 8, no. 3, pp. 1555–1564, 2009.
- K. Y. Huang, K. Y. Chien, Y. C. Lin et al., “A proteome reference map of Trichomonas vaginalis,” Parasitology Research, vol. 104, no. 4, pp. 927–933, 2009.
- L. A. Ramón-Luing, F. J. Rendón-Gandarilla, R. E. Cárdenas-Guerra et al., “Immunoproteomics of the active degradome to identify biomarkers for Trichomonas vaginalis,” Proteomics, vol. 10, no. 3, pp. 435–444, 2010.
- D. J. Mallinson, B. C. Lockwood, G. H. Coombs, and M. J. North, “Identification and molecular cloning of four cysteine proteinase genes from the pathogenic protozoon Trichomonas vaginalis,” Microbiology, vol. 140, no. 10, pp. 2725–2735, 1994.
- C. R. León-Sicairos, I. Pérez-Martînez, M. E. Álvarez-Sánchez, I. López-Villaseñor, and R. Arroyo, “Two Trichomonas vaginalis loci encoding for distinct cysteine proteinases show a genomic linkage with putative inositol hexakisphosphate kinase (IP6K2) or an ABC transporter gene,” The Journal of Eukaryotic Microbiology, vol. 50, pp. 702–705, 2003.
- C. R. León-Sicairos, J. León-Félix, and R. Arroyo, “Tvcp12: a novel Trichomonas vaginalis cathepsin L-like cysteine proteinase-encoding gene,” Microbiology, vol. 150, no. 5, pp. 1131–1138, 2004.
- E. Solano-González, M. E. Alvarez-Sánchez, L. Avila-González, V. H. Rodríguez-Vargas, R. Arroyo, and J. Ortega-López, “Location of the cell-binding domain of CP65, a 65 kDa cysteine proteinase involved in Trichomonas vaginalis cytotoxicity,” International Journal of Biochemistry and Cell Biology, vol. 38, no. 12, pp. 2114–2127, 2006.
- E. Solano-González, E. Burrola-Barraza, C. León-Sicairos et al., “The trichomonad cysteine proteinase TVCP4 transcript contains an iron-responsive element,” FEBS Letters, vol. 581, no. 16, pp. 2919–2928, 2007.
- J. C. Torres-Romero and R. Arroyo, “Responsiveness of Trichomonas vaginalis to iron concentrations: evidence for a post-transcriptional iron regulation by an IRE/IRP-like system,” Infection, Genetics and Evolution, vol. 9, no. 6, pp. 1065–1074, 2009.
- L. D. L. A. Ramón-Luing, F. J. Rendón-Gandarilla, J. Puente-Rivera, L. Ávila-González, and R. Arroyo, “Identification and characterization of the immunogenic cytotoxic TvCP39 proteinase gene of Trichomonas vaginalis,” International Journal of Biochemistry and Cell Biology, vol. 43, no. 10, pp. 1500–1511, 2011.
- A. J. Barrett and N. D. Rawlings, “Evolutionary lines of cysteine peptidases,” Biological Chemistry, vol. 382, no. 5, pp. 727–733, 2001.
- J. C. Mottram, M. J. Helms, G. H. Coombs, and M. Sajid, “Clan CD cysteine peptidases of parasitic protozoa,” Trends in Parasitology, vol. 19, no. 4, pp. 182–187, 2003.
- M. W. Lehker, T. H. Chang, D. C. Dailey, and J. F. Alderete, “Specific erythrocyte binding is an additional nutrient acquisition system for Trichomonas vaginalis,” Journal of Experimental Medicine, vol. 171, no. 6, pp. 2165–2170, 1990.
- J. F. Alderete, D. Provenzano, and M. W. Lehker, “Iron mediates Trichomonas vaginalis resistance to complement lysis,” Microbial Pathogenesis, vol. 19, no. 2, pp. 93–103, 1995.
- D. Provenzano and J. F. Alderete, “Analysis of human immunoglobulin-degrading cysteine proteinases of Trichomonas vaginalis,” Infection and Immunity, vol. 63, no. 9, pp. 3388–3395, 1995.
- D. C. Dailey, T. H. Chang, and J. F. Alderete, “Characterization of Trichomonas vaginalis haemolysis,” Parasitology, vol. 101, no. 2, pp. 171–175, 1990.
- M. E. Alvarez-Sánchez, L. Avila-González, C. Becerril-García, L. V. Fattel-Facenda, J. Ortega-López, and R. Arroyo, “A novel cysteine proteinase (CP65) of Trichomonas vaginalis involved in cytotoxicity,” Microbial Pathogenesis, vol. 28, no. 4, pp. 193–202, 2000.
- M. E. Alvarez-Sánchez, E. Solano-González, C. Yañez-Gómez, and R. Arroyo, “Negative iron regulation of the CP65 cysteine proteinase cytotoxicity in Trichomonas vaginalis,” Microbes and Infection, vol. 9, no. 14-15, pp. 1597–1605, 2007.
- M. E. Alvarez-Sánchez, B. I. Carvajal-Gamez, E. Solano-González et al., “Polyamine depletion down-regulates expression of the Trichomonas vaginalis cytotoxic CP65, a 65-kDa cysteine proteinase involved in cellular damage,” International Journal of Biochemistry and Cell Biology, vol. 40, no. 11, pp. 2442–2451, 2008.
- R. Hernandez-Gutierrez, J. Ortega-López, and R. Arroyo, “A 39-kDa Cysteine Proteinase CP39 from Trichomonas vaginalis, Which Is Negatively Affected by Iron May Be Involved in Trichomonal Cytotoxicity,” The Journal of Eukaryotic Microbiology, vol. 50, supplement 1, pp. 696–698, 2003.
- R. Hernández-Gutiérrez, L. Avila-González, J. Ortega-López, F. Cruz-Talonia, G. Gómez-Gutierrez, and R. Arroyo, “Trichomonas vaginalis: characterization of a 39-kDa cysteine proteinase found in patient vaginal secretions,” Experimental Parasitology, vol. 107, no. 3-4, pp. 125–135, 2004.
- U. Sommer, C. E. Costello, G. R. Hayes et al., “Identification of Trichomonas vaginalis cysteine proteases that induce apoptosis in human vaginal epithelial cells,” The Journal of Biological Chemistry, vol. 280, no. 25, pp. 23853–23860, 2005.
- S. Kummer, G. R. Hayes, R. O. Gilbert, D. H. Beach, J. J. Lucas, and B. N. Singh, “Induction of human host cell apoptosis by Trichomonas vaginalis cysteine proteases is modulated by parasite exposure to iron,” Microbial Pathogenesis, vol. 44, no. 3, pp. 197–203, 2008.
- T. E. Gorrell, “Effect of culture medium iron content on the biochemical composition and metabolism of Trichomonas vaginalis,” Journal of Bacteriology, vol. 161, no. 3, pp. 1228–1230, 1985.
- A. Smith and P. Johnson, “Gene expression in the unicellular eukaryote Trichomonas vaginalis,” Research in Microbiology, vol. 162, no. 6, pp. 646–654, 2011.
- J. León-Félix, J. Ortega-López, R. Orozco-Solís, and R. Arroyo, “Two novel asparaginyl endopeptidase-like cysteine proteinases from the protist Trichomonas vaginalis: their evolutionary relationship within the clan CD cysteine proteinases,” Gene, vol. 335, no. 1-2, pp. 25–35, 2004.
- L. S. Diamond, “The establishment of various trichomonads of animals and man in axenic cultures,” The Journal of Parasitology, vol. 43, no. 4, pp. 488–490, 1957.
- D. Harlow and E. Lane, Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory, New York, NY, USA, 1988.
- P. Meza-Cervantez, A. González-Robles, R. E. Cárdenas-Guerra et al., “Pyruvate: ferredoxin oxidoreductase (PFO) is a surface-associated cell-binding protein in Trichomonas vaginalis and is involved in trichomonal adherence to host cells,” Microbiology, vol. 157, no. 12, pp. 3469–3482, 2011.
- V. Moreno-Brito, C. Yáñez-Gómez, P. Meza-Cervantez et al., “A Trichomonas vaginalis 120 kDa protein with identity to hydrogenosome pyruvate:ferredoxin oxidoreductase is a surface adhesin induced by iron,” Cellular Microbiology, vol. 7, no. 2, pp. 245–258, 2005.
- A. Ovat, F. Muindi, C. Fagan et al., “Aza-peptidyl michael acceptor and epoxide inhibitors—potent and selective inhibitors of Schistosoma mansoni and Ixodes ricinus legumains (asparaginyl endopeptidases),” Journal of Medicinal Chemistry, vol. 52, no. 22, pp. 7192–7210, 2009.
- J. W. Ju, H. N. Joo, M. R. Lee et al., “Identification of a serodiagnostic antigen, legumain, by immunoproteomic analysis of excretory-secretory products of Clonorchis sinensis adult worms,” Proteomics, vol. 9, no. 11, pp. 3066–3078, 2009.
- M. W. Lehker, R. Arroyo, and J. F. Alderete, “The regulation by iron of the synthesis of adhesins and cytoadherence levels in the protozoan Trichomonas vaginalis,” Journal of Experimental Medicine, vol. 174, no. 2, pp. 311–318, 1991.
- A. Prado, J. L. R. Arrondo, A. Villena, F. M. Goñi, and J. M. Macarulla, “Membrane-surfactant interactions The effect of triton X-100 on sarcoplasmic reticulum vesicles,” Biochimica et Biophysica Acta, vol. 733, no. 1, pp. 163–171, 1983.
- M. Heffer-Lauc, B. Viljetić, K. Vajn, R. L. Schnaar, and G. Lauc, “Effects of detergents on the redistribution of gangliosides and GPI-anchored proteins in brain tissue sections,” Journal of Histochemistry and Cytochemistry, vol. 55, no. 8, pp. 805–812, 2007.
- P. M. Dando, M. Fortunato, L. Smith, C. G. Knight, J. E. McKendrick, and A. J. Barrett, “Pig kidney legumain: an asparaginyl endopeptidase with restricted specificity,” Biochemical Journal, vol. 339, no. 3, pp. 743–749, 1999.
- E. Dall and H. Brandstetter, “Activation of legumain involves proteolytic and conformational events, resulting in a context-and substrate-dependent activity profile,” Acta Crystallographica Section F, vol. 68, no. 1, pp. 24–31, 2012.
- J. Lee and M. Bogyo, “Synthesis and evaluation of aza-peptidyl inhibitors of the lysosomal asparaginyl endopeptidase, legumain,” Bioorganic and Medicinal Chemistry Letters, vol. 22, no. 3, pp. 1340–1343, 2012.
- A. Øverbye, F. Sætre, L. K. Hagen, H. T. Johansen, and P. O. Seglen, “Autophagic activity measured in whole rat hepatocytes as the accumulation of a novel BHMT fragment (p10), generated in amphisomes by the asparaginyl proteinase, legumain,” Autophagy, vol. 7, no. 9, pp. 1011–1027, 2011.
- J. M. Chen, M. Fortunato, and A. J. Barrett, “Activation of human prolegumain by cleavage at a C-terminal asparagine residue,” Biochemical Journal, vol. 352, no. 2, pp. 327–334, 2000.
- V. Turk, B. Turk, and D. Turk, “Lysosomal cysteine proteases: facts and opportunities,” The EMBO Journal, vol. 20, no. 17, pp. 4629–4633, 2001.
- A. F. Garcia, M. Benchimol, and J. F. Alderete, “Trichomonas vaginalis polyamine metabolism is linked to host cell adherence and cytotoxicity,” Infection and Immunity, vol. 73, no. 5, pp. 2602–2610, 2005.
- M. Sajid, J. H. McKerrow, E. Hansell et al., “Functional expression and characterization of Schistosoma mansoni cathepsin B and its trans-activation by an endogenous asparaginyl endopeptidase,” Molecular and Biochemical Parasitology, vol. 131, no. 1, pp. 65–75, 2003.
- C. R. Caffrey, J. H. McKerrow, J. P. Salter, and M. Sajid, “Blood “n” guts: an update on schistosome digestive peptidases,” Trends in Parasitology, vol. 20, no. 5, pp. 241–248, 2004.
- M. Horn, M. Nussbaumerová, M. Šanda et al., “Hemoglobin digestion in blood-feeding ticks: mapping a multipeptidase pathway by functional proteomics,” Chemistry and Biology, vol. 16, no. 10, pp. 1053–1063, 2009.
- M. G. Götz, K. E. James, E. Hansell et al., “Aza-peptidyl Michael acceptors. A new class of potent and selective inhibitors of asparaginyl endopeptidases (legumains) from evolutionarily diverse pathogens,” Journal of Medicinal Chemistry, vol. 51, no. 9, pp. 2816–2832, 2008.
- M. Yadav, M. L. Dubey, I. Gupta, and N. Malla, “Cysteine proteinase 30 (CP30) and antibody response to CP30 in serum and vaginal washes of symptomatic and asymptomatic Trichomonas vaginalis-infected women,” Parasite Immunology, vol. 29, no. 7, pp. 359–365, 2007.