Table of Contents Author Guidelines Submit a Manuscript
Journal of Parasitology Research
Volume 2017 (2017), Article ID 4342789, 10 pages
https://doi.org/10.1155/2017/4342789
Research Article

Identification, Characterization, and Structure of Tm16 from Trichuris muris

1National School of Tropical Medicine, Baylor College of Medicine and Texas Children’s Hospital Center for Vaccine Development, Houston TX 77030, USA
2Departments of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA

Correspondence should be addressed to Bin Zhan and Oluwatoyin A. Asojo

Received 1 March 2017; Revised 13 June 2017; Accepted 6 July 2017; Published 14 August 2017

Academic Editor: José F. Silveira

Copyright © 2017 Zhuyun Liu 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. G. B. D. DALYs and H. Collaborators, “Global, regional, and national disability-adjusted life-years (DALYs) for 315 diseases and injuries and healthy life expectancy (HALE), 1990–2015: a systematic analysis for the Global Burden of Disease Study 2015, Lancet, 388 (2016) 1603–1658”.
  2. P. J. Hotez, P. J. Brindley, J. M. Bethony, C. H. King, E. J. Pearce, and J. Jacobson, “Helminth infections: the great neglected tropical diseases,” Journal of Clinical Investigation, vol. 118, no. 4, pp. 1311–1321, 2008. View at Publisher · View at Google Scholar · View at Scopus
  3. S. Knopp, P. Steinmann, C. Hatz, J. Keiser, and J. Utzinger, “Nematode infections: filariases,” Infectious Disease Clinics of North America, vol. 26, no. 2, pp. 359–381, 2012. View at Publisher · View at Google Scholar · View at Scopus
  4. S. Knopp, P. Steinmann, J. Keiser, and J. Utzinger, “Nematode infections: soil-transmitted helminths and trichinella,” Infectious Disease Clinics of North America, vol. 26, no. 2, pp. 341–358, 2012. View at Publisher · View at Google Scholar · View at Scopus
  5. J. Keiser and J. Utzinger, “Efficacy of current drugs against soil-transmitted helminth infections: Systematic review and meta-analysis,” JAMA - Journal of the American Medical Association, vol. 299, no. 16, pp. 1937–1948, 2008. View at Publisher · View at Google Scholar · View at Scopus
  6. W. Beck and J. E. Davies, Medical Parasitology, Mosby Company, London, Engalnd, Third Edition edition, 1981. View at Publisher · View at Google Scholar
  7. H. Dixon, C. E. Johnston, and K. J. Else, “Antigen selection for future anti-Trichuris vaccines: a comparison of cytokine and antibody responses to larval and adult antigen in a primary infection,” Parasite Immunology, vol. 30, no. 9, pp. 454–461, 2008. View at Publisher · View at Google Scholar · View at Scopus
  8. H. Dixon, M. C. Little, and K. J. Else, “Characterisation of the protective immune response following subcutaneous vaccination of susceptible mice against Trichuris muris,” International Journal for Parasitology, vol. 40, no. 6, pp. 683–693, 2010. View at Publisher · View at Google Scholar · View at Scopus
  9. E. Lobos, M. Altmann, G. Mengod, N. Weiss, W. Rudin, and M. Karam, “Identification of an Onchocerca volvulus cDNA encoding a low-molecular-weight antigen uniquely recognized by onchocerciasis patient sera,” Molecular and Biochemical Parasitology, vol. 39, no. 1, pp. 135–145, 1990. View at Publisher · View at Google Scholar · View at Scopus
  10. K. Yeung, T. Seitz, S. Li et al., “Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP,” Nature, vol. 401, no. 6749, pp. 173–177, 1999. View at Publisher · View at Google Scholar · View at Scopus
  11. K. C. Yeung, D. W. Rose, A. S. Dhillon et al., “Raf kinase inhibitor protein interacts with NF-κB-inducing kinase and TAK1 and inhibits NF-κB activation,” Molecular and Cellular Biology, vol. 21, no. 21, pp. 7207–7217, 2001. View at Publisher · View at Google Scholar · View at Scopus
  12. T. Kroslak, T. Koch, E. Kahl, and V. Höllt, “Human Phosphatidylethanolamine-binding Protein Facilitates Heterotrimeric G Protein-dependent Signaling,” Journal of Biological Chemistry, vol. 276, no. 43, pp. 39772–39778, 2001. View at Publisher · View at Google Scholar · View at Scopus
  13. U. Hengst, H. Albrecht, D. Hess, and D. Monard, “The phosphatidylethanolamine-binding protein is the prototype of a novel family of serine protease inhibitors,” Journal of Biological Chemistry, vol. 276, no. 1, pp. 535–540, 2001. View at Publisher · View at Google Scholar · View at Scopus
  14. M. J. Banfield and R. L. Brady, “The structure of Antirrhinum centroradialis protein (CEN) suggests a role as a kinase regulator,” Journal of Molecular Biology, vol. 297, no. 5, pp. 1159–1170, 2000. View at Publisher · View at Google Scholar · View at Scopus
  15. C. M. Grimsley, J. M. Kinchen, A.-C. Tosello-Trampont et al., “Dock180 and ELMO1 proteins cooperate to promote evolutionarily conserved rac-dependent cell migration,” Journal of Biological Chemistry, vol. 279, no. 7, pp. 6087–6097, 2004. View at Publisher · View at Google Scholar · View at Scopus
  16. H. Hasegawa, E. Kiyokawa, S. Tanaka et al., “DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane,” Molecular and Cellular Biology, vol. 16, no. 4, pp. 1770–1776, 1996. View at Publisher · View at Google Scholar · View at Scopus
  17. M. R. S. Erickson, B. J. Galletta, and S. M. Abmayr, “Drosophila myoblast city encodes a conserved protein that is essential for myoblast fusion, dorsal closure, and cytoskeletal organization,” Journal of Cell Biology, vol. 138, no. 3, pp. 589–603, 1997. View at Publisher · View at Google Scholar · View at Scopus
  18. X. Yang, Y. Yang, Y. Wang et al., “Excretory/secretory products from Trichinella spiralis adult worms ameliorate DSS-induced colitis in mice,” PLoS ONE, vol. 9, no. 5, Article ID e96454, 2014. View at Publisher · View at Google Scholar · View at Scopus
  19. X. Bai, X. Wu, X. Wang et al., “Regulation of cytokine expression in murine macrophages stimulated by excretory/secretory products from Trichinella spiralis in vitro,” Molecular and Cellular Biochemistry, vol. 360, no. 1-2, pp. 79–88, 2012. View at Publisher · View at Google Scholar · View at Scopus
  20. M. Langelaar, C. Aranzamendi, F. Franssen et al., “Suppression of dendritic cell maturation by Trichinella spiralis excretory/secretory products,” Parasite Immunology, vol. 31, no. 10, pp. 641–645, 2009. View at Publisher · View at Google Scholar · View at Scopus
  21. H. M. Lun, C. H. Mak, and R. C. Ko, “Characterization and cloning of metallo-proteinase in the excretory/secretory products of the infective-stage larva of Trichinella spiralis,” Parasitology Research, vol. 90, no. 1, pp. 27–37, 2003. View at Google Scholar · View at Scopus
  22. C.-H. Mak and R. C. Ko, “Characterization of endonuclease activity from excretory/secretory products of a parasitic nematode, Trichinella spiralis,” European Journal of Biochemistry, vol. 260, no. 2, pp. 477–481, 1999. View at Publisher · View at Google Scholar · View at Scopus
  23. V. K. Todorova and M. W. Kennedy, “Proteinases in the excretory/secretory products (ES) of adult Trichinella spiralis,” Parasitology, vol. 111, no. 2, pp. 201–208, 1995. View at Publisher · View at Google Scholar · View at Scopus
  24. R. C. Ko and L. Fan, “Changes in host muscles induced by excretory/secretory products of larval Trichinella spiralis and Trichinella pseudospiralis,” Parasitology, vol. 108, no. 2, pp. 195–205, 1994. View at Publisher · View at Google Scholar · View at Scopus
  25. R. C. Ko, L. Fan, and D. L. Lee, “Experimental reorganization of host muscle cells by excretory/secretory products of infective trichinella spiralis larvae,” Transactions of the Royal Society of Tropical Medicine and Hygiene, vol. 86, no. 1, pp. 77-78, 1992. View at Publisher · View at Google Scholar · View at Scopus
  26. J. Yang, W. Pan, X. Sun et al., “Immunoproteomic profile of Trichinella spiralis adult worm proteins recognized by early infection sera,” Parasites and Vectors, vol. 8, no. 1, article no. 20, 2015. View at Publisher · View at Google Scholar · View at Scopus
  27. J. W. Pflugrath, “The finer things in X-ray diffraction data collection,” Acta Crystallographica Section D: Biological Crystallography, vol. 55, no. 10, pp. 1718–1725, 1999. View at Publisher · View at Google Scholar · View at Scopus
  28. A. G. W. Leslie, “The integration of macromolecular diffraction data,” Acta Crystallographica Section D: Biological Crystallography, vol. 62, no. 1, pp. 48–57, 2006. View at Publisher · View at Google Scholar · View at Scopus
  29. A. J. McCoy, R. W. Grosse-Kunstleve, L. C. Storoni, and R. J. Read, “Likelihood-enhanced fast translation functions,” Acta Crystallographica Section D: Biological Crystallography, vol. 61, no. 4, pp. 458–464, 2005. View at Publisher · View at Google Scholar · View at Scopus
  30. L. C. Storoni, A. J. McCoy, and R. J. Read, “Likelihood-enhanced fast rotation functions,” Acta Crystallographica Section D: Biological Crystallography, vol. 60, no. 3, pp. 432–438, 2004. View at Publisher · View at Google Scholar · View at Scopus
  31. M. J. Banfield, J. J. Barker, A. C. F. Perry, and R. L. Brady, “Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction,” Structure, vol. 6, no. 10, pp. 1245–1254, 1998. View at Publisher · View at Google Scholar · View at Scopus
  32. P. Emsley, B. Lohkamp, W. G. Scott, and K. Cowtan, “Features and development of Coot,” Acta Crystallographica Section D: Biological Crystallography, vol. 66, no. 4, pp. 486–501, 2010. View at Publisher · View at Google Scholar · View at Scopus
  33. P. D. Adams, P. V. Afonine, G. Bunkóczi et al., “PHENIX: a comprehensive Python-based system for macromolecular structure solution,” Acta Crystallographica D: Biological Crystallography, vol. 66, part 2, pp. 213–221, 2010. View at Publisher · View at Google Scholar · View at Scopus
  34. W. L. Delano, The PyMOL Molecular Graphics System http://www.pymol.org, (2002).
  35. P. Gouet, X. Robert, and E. Courcelle, “ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins,” Nucleic Acids Research, vol. 31, no. 13, pp. 3320–3323, 2003. View at Publisher · View at Google Scholar
  36. P. Gouet, E. Courcelle, D. I. Stuart, and F. Métoz, “ESPript: analysis of multiple sequence alignments in PostScript,” Bioinformatics, vol. 15, no. 4, pp. 305–308, 1999. View at Publisher · View at Google Scholar · View at Scopus