Table of Contents Author Guidelines Submit a Manuscript
BioMed Research International
Volume 2015, Article ID 430436, 8 pages
http://dx.doi.org/10.1155/2015/430436
Research Article

Effect of Recombinant Prophenin 2 on the Integrity and Viability of Trichomonas vaginalis

1Unidad Irapuato, Departamento de Ingeniería Genética, Centro de Investigación y de Estudios Avanzados del IPN, P.O. Box 629, 36500 Irapuato, GTO, Mexico
2Division de Ciencias Naturales y Exactas, Departamento de Biologia, Universidad de Guanajuato, Col. Noria Alta, 36040 Guanajuato, GTO, Mexico
3Universidad Politécnica del Mar y la Sierra, Carretera a La Cruz km 15.5, Col. Arroyitos, La Cruz, 82700 Elota, SIN, Mexico

Received 31 July 2014; Accepted 26 September 2014

Academic Editor: J. Eleazar Barboza-Corona

Copyright © 2015 J. L. Hernandez-Flores 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.

Linked References

  1. K. A. Brogden, M. Ackermann, P. B. McCray Jr., and B. F. Tack, “Antimicrobial peptides in animals and their role in host defences,” International Journal of Antimicrobial Agents, vol. 22, no. 5, pp. 465–478, 2003. View at Publisher · View at Google Scholar · View at Scopus
  2. G. Maróti Gergely, A. Kereszt, É. Kondorosi, and P. Mergaert, “Natural roles of antimicrobial peptides in microbes, plants and animals,” Research in Microbiology, vol. 162, no. 4, pp. 363–374, 2011. View at Publisher · View at Google Scholar · View at Scopus
  3. A. A. Bahar and D. Ren, “Antimicrobial peptides,” Pharmaceuticals, vol. 6, no. 12, pp. 1543–1575, 2013. View at Publisher · View at Google Scholar · View at Scopus
  4. G. K. Mutwiri, W. G. Henk, F. M. Enright, and L. B. Corbeil, “Effect of the antimicrobial peptide, D-hecate, on Trichomonads,” Journal of Parasitology, vol. 86, no. 6, pp. 1355–1359, 2000. View at Publisher · View at Google Scholar · View at Scopus
  5. J. Vizioli and M. Salzet, “Antimicrobial peptides versus parasitic infections?” Trends in Parasitology, vol. 18, no. 11, pp. 475–476, 2002. View at Publisher · View at Google Scholar · View at Scopus
  6. A. J. Mason, W. Moussaoui, T. Abdelrahman et al., “Structural determinants of antimicrobial and antiplasmodial activity and selectivity in histidine-rich amphipathic cationic peptides,” The Journal of Biological Chemistry, vol. 284, no. 1, pp. 119–133, 2009. View at Publisher · View at Google Scholar · View at Scopus
  7. C.-Y. Pan, J.-Y. Chen, T.-L. Lin, and C.-H. Lin, “In vitro activities of three synthetic peptides derived from epinecidin-1 and an anti-lipopolysaccharide factor against Propionibacterium acnes, Candida albicans, and Trichomonas vaginalis,” Peptides, vol. 30, no. 6, pp. 1058–1068, 2009. View at Publisher · View at Google Scholar · View at Scopus
  8. L. Rivas, J. R. Luque-Ortega, and D. Andreu, “Amphibian antimicrobial peptides and Protozoa: lessons from parasites,” Biochimica et Biophysica Acta, vol. 1788, no. 8, pp. 1570–1581, 2009. View at Publisher · View at Google Scholar · View at Scopus
  9. B. Rivas-Santiago, C. J. Serrano, and J. A. Enciso-Moreno, “Susceptibility to infectious diseases based on antimicrobial peptide production,” Infection and Immunity, vol. 77, no. 11, pp. 4690–4695, 2009. View at Publisher · View at Google Scholar · View at Scopus
  10. Y. Sang and F. Blecha, “Porcine host defense peptides: expanding repertoire and functions,” Developmental & Comparative Immunology, vol. 33, no. 3, pp. 334–343, 2009. View at Publisher · View at Google Scholar · View at Scopus
  11. M. F. Cotch, J. G. Pastorek II, R. P. Nugent et al., “Trichomonas vaginalis associated with low birth weight and preterm delivery. The Vaginal Infections and Prematurity Study Group,” Sexually Transmitted Diseases, vol. 24, no. 6, pp. 353–360, 1997. View at Publisher · View at Google Scholar · View at Scopus
  12. M. Laga, A. Manoka, M. Kivuvu et al., “Non-ulcerative sexually transmitted diseases as risk factors for HIV-1 transmission in women: Results from a cohort study,” AIDS, vol. 7, no. 1, pp. 95–102, 1993. View at Publisher · View at Google Scholar · View at Scopus
  13. G. G. G. Donders, C. E. Depuydt, J.-P. Bogers, and A. J. Vereecken, “Association of Trichomonas vaginalis and cytological abnormalities of the cervix in low risk women,” PLoS ONE, vol. 8, no. 12, Article ID e86266, 2013. View at Publisher · View at Google Scholar · View at Scopus
  14. P. Kissinger and A. Adamski, “Trichomoniasis and HIV interactions: a review,” Sexually Transmitted Infections, vol. 89, no. 6, pp. 426–433, 2013. View at Publisher · View at Google Scholar · View at Scopus
  15. S. L. Cudmore, K. L. Delgaty, S. F. Hayward-McClelland, D. P. Petrin, and G. E. Garber, “Treatment of infections caused by metronidazole-resistant Trichomonas vaginalis,” Clinical Microbiology Reviews, vol. 17, no. 4, pp. 783–793, 2004. View at Publisher · View at Google Scholar · View at Scopus
  16. D. H. H. Robertson, R. Heyworth, C. Harrison, and W. H. R. Lumsden, “Treatment failure in Trichomonas vaginalis infections in females. I. Concentrations of metronidazole in plasma and vaginal content during normal and high dosage,” Journal of Antimicrobial Chemotherapy, vol. 21, no. 3, pp. 373–378, 1988. View at Publisher · View at Google Scholar · View at Scopus
  17. R. L. Dunne, L. A. Dunn, P. Upcroft, P. J. O'Donoghue, and J. A. Upcroft, “Drug resistance in the sexually transmitted protozoan Trichomonas vaginalis,” Cell Research, vol. 13, no. 4, pp. 239–249, 2003. View at Publisher · View at Google Scholar · View at Scopus
  18. J. R. Schwebke and F. J. Barrientes, “Prevalence of Trichomonas vaginalis isolates with resistance to metronidazole and tinidazole,” Antimicrobial Agents and Chemotherapy, vol. 50, no. 12, pp. 4209–4210, 2006. View at Publisher · View at Google Scholar · View at Scopus
  19. J. D. Sobel, V. Nagappan, and P. Nyirjesy, “Metronidazole-resistant vaginal trichomoniasis—an emerging problem,” The New England Journal of Medicine, vol. 341, no. 4, pp. 292–293, 1999. View at Publisher · View at Google Scholar · View at Scopus
  20. 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. View at Publisher · View at Google Scholar · View at Scopus
  21. 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. View at Publisher · View at Google Scholar · View at Scopus
  22. A. F. Garcia and J. F. Alderete, “Characterization of the Trichomonas vaginalis surface-associated AP65 and binding domain interacting with trichomonads and host cells,” BMC Microbiology, vol. 7, article 116, 2007. View at Publisher · View at Google Scholar · View at Scopus
  23. V. V. Infante, A. D. Miranda-Olvera, L. M. de Leon-Rodriguez, F. Anaya-Velazquez, M. C. Rodriguez, and E. E. Avila, “Effect of the antimicrobial peptide tritrpticin on the in vitro viability and growth of trichomonas vaginalis,” Current Microbiology, vol. 62, no. 1, pp. 301–306, 2011. View at Publisher · View at Google Scholar · View at Scopus
  24. A. E. Shinnar, K. L. Butler, and H. J. Park, “Cathelicidin family of antimicrobial peptides: proteolytic processing and protease resistance,” Bioorganic Chemistry, vol. 31, no. 6, pp. 425–436, 2003. View at Publisher · View at Google Scholar · View at Scopus
  25. L. S. Diamond, D. R. Harlow, and C. C. Cunnick, “A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoeba,” Transactions of the Royal Society of Tropical Medicine and Hygiene, vol. 72, no. 4, pp. 431–432, 1978. View at Publisher · View at Google Scholar · View at Scopus
  26. C. Zhao, T. Ganz, and R. I. Lehrer, “Structures of genes for two cathelin-associated antimicrobial peptides: prophenin-2 and PR-39,” FEBS Letters, vol. 376, no. 3, pp. 130–134, 1995. View at Publisher · View at Google Scholar · View at Scopus
  27. T. P. Hopp, K. S. Prickett, V. L. Price et al., “A short polypeptide marker sequence useful for recombinant protein identification and purification,” Nature Biotechnology, vol. 6, no. 10, pp. 1204–1210, 1988. View at Publisher · View at Google Scholar · View at Scopus
  28. R. Rico-Mata, L. M. De Leon-Rodriguez, and E. E. Avila, “Effect of antimicrobial peptides derived from human cathelicidin LL-37 on Entamoeba histolytica trophozoites,” Experimental Parasitology, vol. 133, no. 3, pp. 300–306, 2013. View at Publisher · View at Google Scholar · View at Scopus
  29. A. Ritonja, M. Kopitar, R. Jerala, and V. Turk, “Primary structure of a new cysteine proteinase inhibitor from pig leucocytes,” FEBS Letters, vol. 255, no. 2, pp. 211–214, 1989. View at Publisher · View at Google Scholar · View at Scopus
  30. G. Zhang, C. R. Ross, and F. Blecha, “Porcine antimicrobial peptides: new prospects for ancient molecules of host defense,” Veterinary Research, vol. 31, no. 3, pp. 277–296, 2000. View at Publisher · View at Google Scholar · View at Scopus
  31. J. Pungercar, B. Strukelj, G. Kopitar et al., “Molecular cloning of a putative homolog of proline/arginine-rich antibacterial peptides from porcine bone marrow,” FEBS Letters, vol. 336, no. 2, pp. 284–288, 1993. View at Publisher · View at Google Scholar · View at Scopus
  32. S. S. Harwig, V. N. Kokryakov, K. M. Swiderek, G. M. Aleshina, C. Zhao, and R. I. Lehrer, “Prophenin-1, an exceptionally proline-rich antimicrobial peptide from porcine leukocytes,” FEBS Letters, vol. 362, pp. 65–69, 1995. View at Google Scholar
  33. C. Lawyer, S. Pai, M. Watabe et al., “Antimicrobial activity of a 13 ammo acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides,” The FEBS Letters, vol. 390, no. 1, pp. 95–98, 1996. View at Publisher · View at Google Scholar · View at Scopus
  34. O. Cirioni, A. Giacometti, C. Silvestri et al., “In vitro activities of tritrpticin alone and in combination with other antimicrobial agents against Pseudomonas aeruginosa,” Antimicrobial Agents and Chemotherapy, vol. 50, no. 11, pp. 3923–3925, 2006. View at Publisher · View at Google Scholar · View at Scopus
  35. L. T. Nguyen, L. de Boer, S. A. J. Zaat, and H. J. Vogel, “Investigating the cationic side chains of the antimicrobial peptide tritrpticin: hydrogen bonding properties govern its membrane-disruptive activities,” Biochimica et Biophysica Acta: Biomembranes, vol. 1808, no. 9, pp. 2297–2303, 2011. View at Publisher · View at Google Scholar · View at Scopus
  36. Y. Ishitsuka, D. S. Pham, A. J. Waring, R. I. Lehrer, and K. Y. C. Lee, “Insertion selectivity of antimicrobial peptide protegrin-1 into lipid monolayers: effect of head group electrostatics and tail group packing,” Biochimica et Biophysica Acta, vol. 1758, no. 9, pp. 1450–1460, 2006. View at Publisher · View at Google Scholar · View at Scopus
  37. S.-T. Yang, S. Yub Shin, Y.-C. Kim, Y. Kim, K.-S. Hahm, and J. I. Kim, “Conformation-dependent antibiotic activity of tritrpticin, a cathelicidin-derived antimicrobial peptide,” Biochemical and Biophysical Research Communications, vol. 296, no. 5, pp. 1044–1050, 2002. View at Publisher · View at Google Scholar · View at Scopus
  38. A. M. Cole, J. Shi, A. Ceccarelli, Y.-H. Kim, A. Park, and T. Ganz, “Inhibition of neutrophil elastase prevents cathelicidin activation and impairs clearance of bacteria from wounds,” Blood, vol. 97, no. 1, pp. 297–304, 2001. View at Publisher · View at Google Scholar · View at Scopus
  39. J. Shi and T. Ganz, “The role of protegrins and other elastase-activated polypeptides in the bactericidal properties of porcine inflammatory fluids,” Infection and Immunity, vol. 66, no. 8, pp. 3611–3617, 1998. View at Google Scholar · View at Scopus
  40. Y. Wang, W. J. Griffiths, T. Curstedt, and J. Johansson, “Porcine pulmonary surfactant preparations contain the antibacterial peptide prophenin and a C-terminal 18-residue fragment thereof,” The FEBS Letters, vol. 460, no. 2, pp. 257–262, 1999. View at Publisher · View at Google Scholar · View at Scopus
  41. Y. Wang, J. Johansson, and W. J. Griffiths, “Characterisation of variant forms of prophenin: mechanistic aspects of the fragmentation of proline-rich peptides,” Rapid Communications in Mass Spectrometry, vol. 14, no. 23, pp. 2182–2202, 2000. View at Google Scholar
  42. M. Pazgier, B. Ericksen, M. Ling et al., “Structural and functional analysis of the pro-domain of human cathelicidin, LL-37,” Biochemistry, vol. 52, no. 9, pp. 1547–1558, 2013. View at Publisher · View at Google Scholar · View at Scopus