Table of Contents Author Guidelines Submit a Manuscript
Mediators of Inflammation
Volume 2015, Article ID 367670, 7 pages
http://dx.doi.org/10.1155/2015/367670
Research Article

Evolutionary Insights into IL17A in Lagomorphs

1CIBIO, InBIO-Research Network in Biodiversity and Evolutionary Biology, Universidade do Porto, Campus de Vairão, Rua Padre Armando Quintas, 4485-661 Vairão, Portugal
2Unidade Multidisciplinar de Investigação Biomédica (UMIB), Universidade do Porto (UP), Rua de Jorge Viterbo Ferreira, No. 228, 4050-313 Porto, Portugal
3Departamento de Genética, CSPGF, Instituto Nacional de Saúde Dr. Ricardo Jorge, Rua Alexandre Herculano, No. 321, 4000-055 Porto, Portugal
4Departamento de Biologia, Faculdade de Ciências da Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal
5Centro de Investigação em Tecnologias de Saúde (CITS), CESPU, Rua Central de Gandra, No. 1317, 4585-116 Gandra, Portugal

Received 22 September 2015; Accepted 22 November 2015

Academic Editor: Kong Chen

Copyright © 2015 Fabiana Neves 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. Z. Yao, S. L. Painter, W. C. Fanslow et al., “Human IL-17: a novel cytokine derived from T cells,” Journal of Immunology, vol. 155, no. 12, pp. 5483–5486, 1995. View at Google Scholar · View at Scopus
  2. E. Rouvier, M.-F. Luciani, M.-G. Mattei, F. Denizot, and P. Golstein, “CTLA-8, cloned from an activated T cell, bearing AU-rich messenger RNA instability sequences, and homologous to a herpesvirus Saimiri gene,” Journal of Immunology, vol. 150, no. 12, pp. 5445–5456, 1993. View at Google Scholar · View at Scopus
  3. S. L. Gaffen, “An overview of IL-17 function and signaling,” Cytokine, vol. 43, no. 3, pp. 402–407, 2008. View at Publisher · View at Google Scholar · View at Scopus
  4. W. Ouyang, J. K. Kolls, and Y. Zheng, “The biological functions of T helper 17 cell effector cytokines in inflammation,” Immunity, vol. 28, no. 4, pp. 454–467, 2008. View at Publisher · View at Google Scholar · View at Scopus
  5. S. Gerhardt, W. M. Abbott, D. Hargreaves et al., “Structure of IL-17A in complex with a potent, fully human neutralizing antibody,” Journal of Molecular Biology, vol. 394, no. 5, pp. 905–921, 2009. View at Publisher · View at Google Scholar · View at Scopus
  6. L. K. Ely, S. Fischer, and K. C. Garcia, “Structural basis of receptor sharing by interleukin 17 cytokines,” Nature Immunology, vol. 10, no. 12, pp. 1245–1251, 2009. View at Publisher · View at Google Scholar · View at Scopus
  7. F. Shen and S. L. Gaffen, “Structure-function relationships in the IL-17 receptor: implications for signal transduction and therapy,” Cytokine, vol. 41, no. 2, pp. 92–104, 2008. View at Publisher · View at Google Scholar · View at Scopus
  8. N. Y. Hemdan, G. Birkenmeier, G. Wichmann et al., “Interleukin-17-producing T helper cells in autoimmunity,” Autoimmunity Reviews, vol. 9, no. 11, pp. 785–792, 2010. View at Publisher · View at Google Scholar · View at Scopus
  9. F. L. van de Veerdonk, M. S. Gresnigt, B. J. Kullberg, J. W. M. van der Meer, L. A. B. Joosten, and M. G. Netea, “Th17 responses and host defense against microorganisms: an overview,” BMB Reports, vol. 42, no. 12, pp. 776–787, 2009. View at Publisher · View at Google Scholar · View at Scopus
  10. E. Bettelli, T. Korn, and V. K. Kuchroo, “Th17: the third member of the effector T cell trilogy,” Current Opinion in Immunology, vol. 19, no. 6, pp. 652–657, 2007. View at Publisher · View at Google Scholar · View at Scopus
  11. Y. Iwakura, H. Ishigame, S. Saijo, and S. Nakae, “Functional specialization of interleukin-17 family members,” Immunity, vol. 34, no. 2, pp. 149–162, 2011. View at Publisher · View at Google Scholar · View at Scopus
  12. H. Ishigame, S. Kakuta, T. Nagai et al., “Differential roles of interleukin-17A and -17F in host defense against mucoepithelial bacterial infection and allergic responses,” Immunity, vol. 30, no. 1, pp. 108–119, 2009. View at Publisher · View at Google Scholar · View at Scopus
  13. W. Huang, L. Na, P. L. Fidel, and P. Schwarzenberger, “Requirement of interleukin-17A for systemic anti-Candida albicans host defense in mice,” The Journal of Infectious Diseases, vol. 190, no. 3, pp. 624–631, 2004. View at Publisher · View at Google Scholar · View at Scopus
  14. S. A. Khader and R. Gopal, “IL-17 in protective immunity to intracellular pathogens,” Virulence, vol. 1, no. 5, pp. 423–427, 2010. View at Publisher · View at Google Scholar · View at Scopus
  15. J. A. Skyberg, M. F. Rollins, J. W. Samuel, M. D. Sutherland, J. T. Belisle, and D. W. Pascual, “Interleukin-17 protects against the francisella tularensis live vaccine strain but not against a virulent F. tularensis type A strain,” Infection and Immunity, vol. 81, no. 9, pp. 3099–3105, 2013. View at Publisher · View at Google Scholar · View at Scopus
  16. C. Paranavitana, E. Zelazowska, L. Dasilva, P. R. Pittman, and M. Nikolich, “Th17 cytokines in recall responses against francisella tularensis in Humans,” Journal of Interferon & Cytokine Research, vol. 30, no. 7, pp. 471–476, 2010. View at Publisher · View at Google Scholar · View at Scopus
  17. L. A. Tesmer, S. K. Lundy, S. Sarkar, and D. A. Fox, “Th17 cells in human disease,” Immunological Reviews, vol. 223, no. 1, pp. 87–113, 2008. View at Publisher · View at Google Scholar · View at Scopus
  18. S. Zhu and Y. Qian, “IL-17/IL-17 receptor system in autoimmune disease: mechanisms and therapeutic potential,” Clinical Science, vol. 122, no. 11, pp. 487–511, 2012. View at Publisher · View at Google Scholar · View at Scopus
  19. F. Neves, J. Abrantes, J. W. Steinke, and P. J. Esteves, “Maximum-likelihood approaches reveal signatures of positive selection in IL genes in mammals,” Innate Immunity, vol. 20, no. 2, pp. 184–191, 2014. View at Publisher · View at Google Scholar · View at Scopus
  20. K. Kubelkova and A. Macela, “Putting the jigsaw together—a brief insight into the tularemia,” Open Life Sciences, vol. 10, no. 1, pp. 195–216, 2015. View at Publisher · View at Google Scholar
  21. M. D. Valentino, Z. J. Maben, L. L. Hensley et al., “Identification of T-cell epitopes in Francisella tularensis using an ordered protein array of serological targets,” Immunology, vol. 132, no. 3, pp. 348–360, 2011. View at Publisher · View at Google Scholar · View at Scopus
  22. C. L. Carvalho, I. Lopes de Carvalho, L. Zé-Zé, M. S. Núncio, and E. L. Duarte, “Tularaemia: a challenging zoonosis,” Comparative Immunology, Microbiology and Infectious Diseases, vol. 37, no. 2, pp. 85–96, 2014. View at Publisher · View at Google Scholar · View at Scopus
  23. D. Y. Kim, T. J. Reilly, S. K. Schommer, and S. T. Spagnoli, “Rabbit tularemia and hepatic coccidiosis in wild rabbit,” Emerging Infectious Diseases, vol. 16, no. 12, pp. 2016–2017, 2010. View at Publisher · View at Google Scholar · View at Scopus
  24. A. Mailles and V. Vaillant, “10 years of surveillance of human tularaemia in France,” Eurosurveillance, vol. 19, no. 45, Article ID 20956, 2014. View at Publisher · View at Google Scholar
  25. D. A. Lepitzki, A. Woolf, and M. Cooper, “Serological prevalence of tularemia in cottontail rabbits of southern Illinois,” Journal of Wildlife Diseases, vol. 26, no. 2, pp. 279–282, 1990. View at Publisher · View at Google Scholar · View at Scopus
  26. G. Wobeser, G. D. Campbell, A. Dallaire, and S. McBurney, “Tularemia, plague, yersiniosis, and Tyzzer's disease in wild rodents and lagomorphs in Canada: a review,” Canadian Veterinary Journal, vol. 50, no. 12, pp. 1251–1256, 2009. View at Google Scholar · View at Scopus
  27. J. M. Rijks, M. Kik, M. G. Koene et al., “Tularaemia in a brown hare (Lepus europaeus) in 2013: first case in the Netherlands in 60 years,” Eurosurveillance, vol. 18, no. 49, 2013. View at Google Scholar
  28. G. Hestvik, E. Warns-Petit, L. A. Smith et al., “The status of tularemia in Europe in a one-health context: a review,” Epidemiology and Infection, vol. 143, no. 10, pp. 2137–2160, 2015. View at Publisher · View at Google Scholar · View at Scopus
  29. C. A. Matthee, B. J. van Vuuren, D. Bell, and T. J. Robinson, “A molecular supermatrix of the rabbits and hares (Leporidae) allows for the identification of five intercontinental exchanges during the Miocene,” Systematic Biology, vol. 53, no. 3, pp. 433–447, 2004. View at Publisher · View at Google Scholar · View at Scopus
  30. D. S. Horner, K. Lefkimmiatis, A. Reyes, C. Gissi, C. Saccone, and G. Pesole, “Phylogenetic analyses of complete mitochondrial genome sequences suggest a basal divergence of the enigmatic rodent Anomalurus,” BMC Evolutionary Biology, vol. 7, article 16, 2007. View at Publisher · View at Google Scholar · View at Scopus
  31. W. J. Murphy, E. Eizirik, W. E. Johnson, Y. P. Zhang, O. A. Ryder, and S. J. O'Brien, “Molecular phylogenetics and the origins of placental mammals,” Nature, vol. 409, no. 6820, pp. 614–618, 2001. View at Publisher · View at Google Scholar · View at Scopus
  32. P. Schnupf and P. J. Sansonetti, “Quantitative RT-PCR profiling of the rabbit immune response: assessment of acute Shigella flexneri infection,” PLoS ONE, vol. 7, no. 6, Article ID e36446, 2012. View at Publisher · View at Google Scholar · View at Scopus
  33. B. Fischer, P. Chavatte-Palmer, C. Viebahn, A. Santos, and V. Duranthon, “Rabbit as a reproductive model for human health,” Reproduction, vol. 144, no. 1, pp. 1–10, 2012. View at Publisher · View at Google Scholar · View at Scopus
  34. F. Neves, J. Abrantes, T. Almeida, A. L. de Matos, P. P. Costa, and P. J. Esteves, “Genetic characterization of interleukins (IL-1α, IL-1β, IL-2, IL-4, IL-8, IL-10, IL-12A, IL-12B, IL-15 and IL-18) with relevant biological roles in lagomorphs,” Innate Immunity, vol. 21, no. 8, pp. 787–801, 2015. View at Publisher · View at Google Scholar
  35. C. Vaure and Y. Liu, “A comparative review of toll-like receptor 4 expression and functionality in different animal species,” Frontiers in Immunology, vol. 5, article 316, 2014. View at Publisher · View at Google Scholar · View at Scopus
  36. S. Vuillaumier, B. Kaltenboeck, G. Lecointre, P. Lehn, and E. Denamur, “Phylogenetic analysis of cystic fibrosis transmembrane conductance regulator gene in mammalian species argues for the development of a rabbit model for cystic fibrosis,” Molecular Biology and Evolution, vol. 14, no. 4, pp. 372–380, 1997. View at Publisher · View at Google Scholar · View at Scopus
  37. A. Pinheiro, F. Neves, A. Lemos de Matos et al., “An overview of the lagomorph immune system and its genetic diversity,” Immunogenetics, In press. View at Publisher · View at Google Scholar
  38. P. Librado and J. Rozas, “DnaSP v5: a software for comprehensive analysis of DNA polymorphism data,” Bioinformatics, vol. 25, no. 11, pp. 1451–1452, 2009. View at Publisher · View at Google Scholar · View at Scopus
  39. R. C. Edgar, “MUSCLE: multiple sequence alignment with high accuracy and high throughput,” Nucleic Acids Research, vol. 32, no. 5, pp. 1792–1797, 2004. View at Publisher · View at Google Scholar · View at Scopus
  40. R. Gupta, E. Jung, and S. Brunak, Prediction of N-Glycosylation Sites in Human Proteins, 2004.
  41. K. Tamura, G. Stecher, D. Peterson, A. Filipski, and S. Kumar, “MEGA6: molecular evolutionary genetics analysis version 6.0,” Molecular Biology and Evolution, vol. 30, no. 12, pp. 2725–2729, 2013. View at Publisher · View at Google Scholar · View at Scopus
  42. D. W. A. Buchan, F. Minneci, T. C. O. Nugent, K. Bryson, and D. T. Jones, “Scalable web services for the PSIPRED Protein Analysis Workbench,” Nucleic Acids Research, vol. 41, pp. W349–W357, 2013. View at Publisher · View at Google Scholar · View at Scopus
  43. D. T. Jones, “Protein secondary structure prediction based on position-specific scoring matrices,” Journal of Molecular Biology, vol. 292, no. 2, pp. 195–202, 1999. View at Publisher · View at Google Scholar · View at Scopus
  44. F. Ferrè and P. Clote, “DiANNA 1.1: an extension of the DiANNA web server for ternary cysteine classification,” Nucleic Acids Research, vol. 34, pp. W182–W185, 2006. View at Publisher · View at Google Scholar · View at Scopus
  45. S. Liu, X. Song, B. A. Chrunyk et al., “Crystal structures of interleukin 17A and its complex with IL-17 receptor A,” Nature Communications, vol. 4, article 188, 2013. View at Publisher · View at Google Scholar · View at Scopus
  46. R. Sabat, E. Witte, K. Witte, and K. Wolk, “IL-22 and IL-17: an overview,” in IL-17, IL-22 and Their Producing Cells: Role in Inflammation and Autoimmunity, V. Quesniaux, B. Ryffel, and F. D. Padova, Eds., Springer, 2013. View at Google Scholar
  47. C. Ferrer-Costa, M. Orozco, and X. de la Cruz, “Characterization of disease-associated single amino acid polymorphisms in terms of sequence and structure properties,” Journal of Molecular Biology, vol. 315, no. 4, pp. 771–786, 2002. View at Publisher · View at Google Scholar · View at Scopus
  48. S. Fang, B. Chen, F. P. L. Tay, B. S. Ng, and D. X. Liu, “An arginine-to-proline mutation in a domain with undefined functions within the helicase protein (Nsp13) is lethal to the coronavirus infectious bronchitis virus in cultured cells,” Virology, vol. 358, no. 1, pp. 136–147, 2007. View at Publisher · View at Google Scholar · View at Scopus
  49. M. W. Yap, S. Nisole, and J. P. Stoye, “A single amino acid change in the SPRY domain of human Trim5α leads to HIV-1 restriction,” Current Biology, vol. 15, no. 1, pp. 73–78, 2005. View at Publisher · View at Google Scholar · View at Scopus
  50. A. Helenius and M. Aebi, “Roles of N-linked glycans in the endoplasmic reticulum,” Annual Review of Biochemistry, vol. 73, pp. 1019–1049, 2004. View at Publisher · View at Google Scholar · View at Scopus
  51. P. M. Rudd, T. Elliott, P. Cresswell, I. A. Wilson, and R. A. Dwek, “Glycosylation and the immune system,” Science, vol. 291, no. 5512, pp. 2370–2376, 2001. View at Publisher · View at Google Scholar · View at Scopus
  52. H. S. Lee, Y. Qi, and W. Im, “Effects of N-glycosylation on protein conformation and dynamics: Protein Data Bank analysis and molecular dynamics simulation study,” Scientific Reports, vol. 5, article 8926, 2015. View at Publisher · View at Google Scholar
  53. D. Fass, “Disulfide bonding in protein biophysics,” Annual Review of Biophysics, vol. 41, no. 1, pp. 63–79, 2012. View at Publisher · View at Google Scholar · View at Scopus
  54. S. G. Hymowitz, E. H. Filvaroff, J. Yin et al., “IL-17s adopt a cystine knot fold: structure and activity of a novel cytokine, IL-17F, and implications for receptor binding,” The EMBO Journal, vol. 20, no. 19, pp. 5332–5341, 2001. View at Publisher · View at Google Scholar · View at Scopus
  55. J. F. Wright, F. Bennett, B. Li et al., “The human IL-17F/IL-17A heterodimeric cytokine signals through the IL-17RA/IL-17RC receptor complex,” The Journal of Immunology, vol. 181, no. 4, pp. 2799–2805, 2008. View at Publisher · View at Google Scholar · View at Scopus
  56. A.-L. Chamorey, N. Magné, X. Pivot, and G. Milano, “Impact of glycosylation on the effect of cytokines. A special focus on oncology,” European Cytokine Network, vol. 13, no. 2, pp. 154–160, 2002. View at Google Scholar · View at Scopus
  57. D. Shental-Bechor and Y. Levy, “Effect of glycosylation on protein folding: a close look at thermodynamic stabilization,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 24, pp. 8256–8261, 2008. View at Publisher · View at Google Scholar · View at Scopus