Table of Contents Author Guidelines Submit a Manuscript
Advances in Bioinformatics
Volume 2018, Article ID 7963401, 12 pages
https://doi.org/10.1155/2018/7963401
Research Article

In Silico Characterization and Structural Modeling of Dermacentor andersoni p36 Immunosuppressive Protein

1Department of Biochemistry, Jomo Kenyatta University of Agriculture and Technology, P.O. Box 62000, Nairobi 00200, Kenya
2Cooperative University of Kenya, P.O. Box 24814, Nairobi 00502, Kenya
3Department of Biochemistry, Kenyatta University, P.O. Box 43844, Nairobi 00100, Kenya
4Unit of Animal Experimentation, State University of North Fluminense, Centre of Biosciences and Biotechnology, Campos dos Goytacazes, RJ, Brazil
5Animal and Human Health Program, International Livestock Research Institute, P.O. Box 30709, Nairobi 00100, Kenya

Correspondence should be addressed to Martin Omulindi Oyugi; moc.liamg@nitramidnilumo

Received 5 November 2017; Accepted 14 February 2018; Published 8 April 2018

Academic Editor: David A. McClellan

Copyright © 2018 Martin Omulindi Oyugi 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. J. De La Fuente, A. Estrada-Pena, J. M. Venzal, K. M. Kocan, and D. E. Sonenshine, “Overview: Ticks as vectors of pathogens that cause disease in humans and animals,” Frontiers in Bioscience, vol. 13, no. 18, pp. 6938–6946, 2008. View at Publisher · View at Google Scholar · View at Scopus
  2. F. Jongejan and G. Uilenberg, “The global importance of ticks,” Parasitology, vol. 129, supplement 1, pp. S3–S14, 2004. View at Publisher · View at Google Scholar · View at Scopus
  3. R. Z. Abbas, M. A. Zaman, D. D. Colwell, J. Gilleard, and Z. Iqbal, “Acaricide resistance in cattle ticks and approaches to its management: The state of play,” Veterinary Parasitology, vol. 203, no. 1-2, pp. 6–20, 2014. View at Publisher · View at Google Scholar · View at Scopus
  4. J. Fuente, K. M. Kocan, and E. F. Blouin, “Tick vaccines and the transmission of tick-borne pathogens,” Veterinary Research Communications, vol. 31, no. 1, pp. 85–90, 2007. View at Publisher · View at Google Scholar · View at Scopus
  5. O. Merino, P. Alberdi, J. M. Pérez De La Lastra, and J. de la Fuente, “Tick vaccines and the control of tick-borne pathogens,” Frontiers in Cellular and Infection Microbiology, vol. 4, Article ID Article 30, 2013. View at Publisher · View at Google Scholar · View at Scopus
  6. J. De La Fuente and M. Contreras, “Tick vaccines: Current status and future directions,” Expert Review of Vaccines, vol. 14, no. 10, pp. 1367–1376, 2015. View at Publisher · View at Google Scholar · View at Scopus
  7. D. P. Oldiges, J. M. Laughery, N. J. Tagliari et al., “Transfected Babesia bovis Expressing a Tick GST as a Live Vector Vaccine,” PLOS Neglected Tropical Diseases, vol. 10, no. 12, Article ID e0005152, 2016. View at Publisher · View at Google Scholar · View at Scopus
  8. J. C. García-García, C. Montero, M. Redondo et al., “Control of ticks resistant to immunization with Bm86 in cattle vaccinated with the recombinant antigen Bm95 isolated from the cattle tick, Boophilus microplus,” Vaccine, vol. 18, no. 21, pp. 2275–2287, 2000. View at Publisher · View at Google Scholar · View at Scopus
  9. D. Odongo, L. Kamau, R. Skilton et al., “Vaccination of cattle with TickGARD induces cross-reactive antibodies binding to conserved linear peptides of Bm86 homologues in Boophilus decoloratus,” Vaccine, vol. 25, no. 7, pp. 1287–1296, 2007. View at Publisher · View at Google Scholar · View at Scopus
  10. P. A. Nuttall, A. R. Trimnell, M. Kazimirova, and M. Labuda, “Exposed and concealed antigens as vaccine targets for controlling ticks and tick-borne diseases,” Parasite Immunology, vol. 28, no. 4, pp. 155–163, 2006. View at Publisher · View at Google Scholar · View at Scopus
  11. A. Fontaine, A. Pascual, I. Diouf et al., “Mosquito salivary gland protein preservation in the field for immunological and biochemical analysis,” Parasites & Vectors, vol. 4, no. 1, article no. 33, 2011. View at Publisher · View at Google Scholar · View at Scopus
  12. G. Leboulle, M. Crippa, Y. Decrem et al., “Characterization of a novel salivary immunosuppressive protein from Ixodes ricinus ticks,” The Journal of Biological Chemistry, vol. 277, no. 12, pp. 10083–10089, 2002. View at Publisher · View at Google Scholar · View at Scopus
  13. R. G. Titus, J. V. Bishop, and J. S. Mejia, “The immunomodulatory factors of arthropod saliva and the potential for these factors to serve as vaccine targets to prevent pathogen transmission,” Parasite Immunology, vol. 28, no. 4, pp. 131–141, 2006. View at Publisher · View at Google Scholar · View at Scopus
  14. J. Anguita, N. Ramamoorthi, J. W. R. Hovius et al., “Salp15, an Ixodes scapularis salivary protein, inhibits CD4+ T cell activation,” Immunity, vol. 16, no. 6, pp. 849–859, 2002. View at Publisher · View at Google Scholar · View at Scopus
  15. J. Dai, P. Wang, S. Adusumilli et al., “Antibodies against a tick protein, Salp15, protect mice from the Lyme disease agent,” Cell Host & Microbe, vol. 6, no. 5, pp. 482–492, 2009. View at Publisher · View at Google Scholar · View at Scopus
  16. C. Almazán, O. Moreno-Cantú, J. A. Moreno-Cid et al., “Control of tick infestations in cattle vaccinated with bacterial membranes containing surface-exposed tick protective antigens,” Vaccine, vol. 30, no. 2, pp. 265–272, 2012. View at Publisher · View at Google Scholar · View at Scopus
  17. J. A. Moreno-Cid, J. M. Pérez de la Lastra, M. Villar et al., “Control of multiple arthropod vector infestations with subolesin/akirin vaccines,” Vaccine, vol. 31, no. 8, pp. 1187–1196, 2013. View at Publisher · View at Google Scholar · View at Scopus
  18. L. F. Parizi, N. W. Githaka, C. Logullo et al., “The quest for a universal vaccine against ticks: Cross-immunity insights,” The Veterinary Journal, vol. 194, no. 2, pp. 158–165, 2012. View at Publisher · View at Google Scholar · View at Scopus
  19. F. J. Alarcon-Chaidez, U. U. Müller-Doblies, and S. Wikel, “Characterization of a recombinant immunomodulatory protein from the salivary glands of Dermacentor andersoni,” Parasite Immunology, vol. 25, no. 2, pp. 69–77, 2003. View at Publisher · View at Google Scholar · View at Scopus
  20. D. K. Bergman, M. J. Palmer, M. J. Caimano, J. D. Radolf, and S. K. Wikel, “Isolation and molecular cloning of a secreted immunosuppressant protein from Dermacentor andersoni salivary gland,” Journal of Parasitology, vol. 86, no. 3, pp. 516–525, 2000. View at Publisher · View at Google Scholar · View at Scopus
  21. V. Nene, D. Lee, J. Quackenbush et al., “AvGI, an index of genes transcribed in the salivary glands of the ixodid tick Amblyomma variegatum,” International Journal for Parasitology, vol. 32, no. 12, pp. 1447–1456, 2002. View at Publisher · View at Google Scholar · View at Scopus
  22. V. Nene, D. Lee, S. Kang'A et al., “Genes transcribed in the salivary glands of female Rhipicephalus appendiculatus ticks infected with Theileria parva,” Insect Biochemistry and Molecular Biology, vol. 34, no. 10, pp. 1117–1128, 2004. View at Publisher · View at Google Scholar · View at Scopus
  23. S. Konnai, C. Nakajima, S. Imamura et al., “Suppression of cell proliferation and cytokine expression by HL-p36, a tick salivary gland-derived protein of Haemaphysalis longicornis,” The Journal of Immunology, vol. 126, no. 2, pp. 209–219, 2009. View at Publisher · View at Google Scholar · View at Scopus
  24. F. Wang, X. Lu, F. Guo et al., “The immunomodulatory protein RH36 is relating to blood-feeding success and oviposition in hard ticks,” Veterinary Parasitology, vol. 240, pp. 49–59, 2017. View at Publisher · View at Google Scholar · View at Scopus
  25. L. F. Parizi, J. Reck, D. P. Oldiges et al., “Multi-antigenic vaccine against the cattle tick Rhipicephalus (Boophilus) microplus: A field evaluation,” Vaccine, vol. 30, no. 48, pp. 6912–6917, 2012. View at Publisher · View at Google Scholar · View at Scopus
  26. D. W. Kulp and W. R. Schief, “Advances in structure-based vaccine design,” Current Opinion in Virology, vol. 3, no. 3, pp. 322–331, 2013. View at Publisher · View at Google Scholar · View at Scopus
  27. S. F. Altschul, W. Gish, W. Miller, E. W. Myers, and D. J. Lipman, “Basic local alignment search tool,” Journal of Molecular Biology, vol. 215, no. 3, pp. 403–410, 1990. View at Publisher · View at Google Scholar
  28. S. Fischer, B. P. Brunk, F. Chen et al., “Using OrthoMCL to assign proteins to OrthoMCL-DB groups or to cluster proteomes into new ortholog groups,” Current Protocols in Bioinformatics, Chapter 6, pp. 19–10, 2011. View at Publisher · View at Google Scholar
  29. L. Li, C. J. Stoeckert Jr., and D. S. Roos, “OrthoMCL: identification of ortholog groups for eukaryotic genomes,” Genome Research, vol. 13, no. 9, pp. 2178–2189, 2003. View at Publisher · View at Google Scholar · View at Scopus
  30. S. Whelan and N. Goldman, “A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach,” Molecular Biology and Evolution, vol. 18, no. 5, pp. 691–699, 2001. View at Publisher · View at Google Scholar · View at Scopus
  31. E. Zuckerkandl and L. Pauling, Evolutionary divergence and convergence in proteins, E, 1965. View at Publisher · View at Google Scholar
  32. B. Yao, L. Zhang, S. Liang, and C. Zhang, “SVMTriP: a method to predict antigenic epitopes using support vector machine to integrate tri-peptide similarity and propensity,” PLoS ONE, vol. 7, no. 9, Article ID e45152, 2012. View at Publisher · View at Google Scholar · View at Scopus
  33. D. Xu and Y. Zhang, “Ab initio protein structure assembly using continuous structure fragments and optimized knowledge-based force field,” Proteins: Structure, Function, and Bioinformatics, vol. 80, no. 7, pp. 1715–1735, 2012. View at Publisher · View at Google Scholar · View at Scopus
  34. D. Eisenberg, R. Lüthy, and J. U. Bowie, “VERIFY3D: assessment of protein models with three-dimensional profiles,” Methods in Enzymology, vol. 277, pp. 396–404, 1997. View at Publisher · View at Google Scholar · View at Scopus
  35. D. Xu and Y. Zhang, “Improving the physical realism and structural accuracy of protein models by a two-step atomic-level energy minimization,” Biophysical Journal, vol. 101, no. 10, pp. 2525–2534, 2011. View at Publisher · View at Google Scholar · View at Scopus
  36. J. de la Fuente, C. Almazán, U. Blas-Machado et al., “The tick protective antigen, 4D8, is a conserved protein involved in modulation of tick blood ingestion and reproduction,” Vaccine, vol. 24, no. 19, pp. 4082–4095, 2006. View at Publisher · View at Google Scholar · View at Scopus
  37. J. Chmelař, J. Kotál, J. Kopecký, J. H. F. Pedra, and M. Kotsyfakis, “All For One and One For All on the Tick-Host Battlefield,” Trends in Parasitology, vol. 32, no. 5, pp. 368–377, 2016. View at Publisher · View at Google Scholar · View at Scopus
  38. C. K. Rangel, L. F. Parizi, G. A. Sabadin et al., “Molecular and structural characterization of novel cystatins from the taiga tick Ixodes persulcatus,” Ticks and Tick-borne Diseases, vol. 8, no. 3, pp. 432–441, 2017. View at Publisher · View at Google Scholar · View at Scopus
  39. R. D. Sleator and P. Walsh, “An overview of in silico protein function prediction,” Archives of Microbiology, vol. 192, no. 3, pp. 151–155, 2010. View at Publisher · View at Google Scholar
  40. D. Tautz and T. Domazet-Lošo, “The evolutionary origin of orphan genes,” Nature Reviews Genetics, vol. 12, no. 10, pp. 692–702, 2011. View at Publisher · View at Google Scholar · View at Scopus
  41. B. V. B. Reddy, W. W. Li, I. N. Shindyalov, and P. E. Bourne, “Conserved key amino acid positions (CKAAPs) derived from the analysis of common substructures in proteins,” in Proteins: Structure, Function and Genetics, pp. 148–163, 2001. View at Publisher · View at Google Scholar
  42. H. Hoogstraal and A. Aeschlimann, “Tick-Host Specificity. Bull. La Société Entomol,” Suisse, vol. 55, pp. 5–32, 1982. View at Publisher · View at Google Scholar
  43. J. D. Bendtsen and K. G. Wooldridge, Bacterial secreted proteins: Secretory mechanisms and role in pathogenesis, Caister Academy Press, Norfolk, UK, 2009.
  44. M. S. Zhang, A. Sandouk, and J. C. D. Houtman, “Glycerol Monolaurate (GML) inhibits human T cell signaling and function by disrupting lipid dynamics,” Scientific Reports, vol. 6, Article ID 30225, 2016. View at Publisher · View at Google Scholar · View at Scopus
  45. M. Paasela, K.-L. Kolho, O. Vaarala, and J. Honkanen, “Lactose inhibits regulatory T-cell-mediated suppression of effector T-cell interferon-γ and IL-17 production,” British Journal of Nutrition, vol. 112, no. 11, pp. 1819–1825, 2014. View at Publisher · View at Google Scholar · View at Scopus
  46. E. Gasteiger, C. Hoogland, A. Gattiker et al., “Protein Identification and Analysis Tools on the ExPASy Server,” in The Proteomics Protocols Handbook, pp. 571–607, 2005. View at Publisher · View at Google Scholar
  47. A. Ikai, “Thermostability and Aliphatic Index of Globular Proteins,” The Journal of Biochemistry, pp. 1895–1898, 1980. View at Publisher · View at Google Scholar
  48. G. A. Dalkas, F. Teheux, J. M. Kwasigroch, and M. Rooman, “Cation-π, amino-π, π-π, and H-bond interactions stabilize antigen-antibody interfaces,” Proteins: Structure, Function, and Bioinformatics, vol. 82, no. 9, pp. 1734–1746, 2014. View at Publisher · View at Google Scholar · View at Scopus
  49. L. Cowen, P. Bradley, M. Menke, J. King, and B. Berger, “Predicting the beta-helix fold from protein sequence data,” Journal of Computational Biology, vol. 9, no. 2, pp. 261–276, 2002. View at Publisher · View at Google Scholar · View at Scopus
  50. M. R. Conte, T. Grüne, J. Ghuman et al., “Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold,” EMBO Journal, vol. 19, no. 12, pp. 3132–3141, 2000. View at Publisher · View at Google Scholar · View at Scopus
  51. R. A. Laskowski, N. M. Luscombe, M. B. Swindells, and J. M. Thornton, “Protein clefts in molecular recognition and function,” Protein Science, vol. 5, pp. 2438–2452, 1996. View at Publisher · View at Google Scholar
  52. K. Ogata, C. Kanei-Ishii, M. Sasaki et al., “The cavity in the hydrophobic core of Myb DNA-binding domain is reserved for DNA recognition and trans-activation,” Nature Structural & Molecular Biology, vol. 3, no. 2, pp. 178–187, 1996. View at Publisher · View at Google Scholar · View at Scopus
  53. M. R. Barnes and I. C. Gray, Bioinformatics for Geneticists, John Wiley & Sons, Ltd, Chichester, UK, 2003. View at Publisher · View at Google Scholar