Table of Contents Author Guidelines Submit a Manuscript
The Scientific World Journal
Volume 2014, Article ID 976015, 10 pages
http://dx.doi.org/10.1155/2014/976015
Research Article

Voltage Dependent Anion Channel Is Redistributed during Japanese Encephalitis Virus Infection of Insect Cells

1Institute of Molecular Biosciences, Mahidol University, Salaya Campus, 25/25 Phuttamonthol Sai 4 Road, Salaya, Nakhon Pathom 73170, Thailand
2Proteomics Research Laboratory, Genome Institute, National Science and Technology Development Agency, 113 Thailand Science Park, Phahonyothin Road, Khlong Nueng, Khlong Luang, Pathum Thani 12120, Thailand
3Center for Emerging and Neglected Infectious Diseases, Mahidol University, 25/25 Phuttamonthon 4 Road, Salaya, Nakhon Pathom 73170, Thailand

Received 9 April 2014; Accepted 25 June 2014; Published 10 July 2014

Academic Editor: Mehmet Yakup Arica

Copyright © 2014 Chanida Fongsaran 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. S. C. Weaver and A. D. T. Barrett, “Transmission cycles, host range, evolution and emergence of arboviral disease,” Nature Reviews Microbiology, vol. 2, no. 10, pp. 789–801, 2004. View at Publisher · View at Google Scholar · View at Scopus
  2. S. Mukhopadhyay, R. J. Kuhn, and M. G. Rossmann, “A structural perspective of the Flavivirus life cycle,” Nature Reviews Microbiology, vol. 3, no. 1, pp. 13–22, 2005. View at Publisher · View at Google Scholar · View at Scopus
  3. B. D. Lindenbach and C. M. Rice, “Molecular biology of flaviviruses,” Advances in Virus Research, vol. 59, pp. 23–61, 2003. View at Publisher · View at Google Scholar · View at Scopus
  4. U. K. Misra and J. Kalita, “Overview: japanese encephalitis,” Progress in Neurobiology, vol. 91, no. 2, pp. 108–120, 2010. View at Publisher · View at Google Scholar · View at Scopus
  5. S. C. Weaver and W. K. Reisen, “Present and future arboviral threats,” Antiviral Research, vol. 85, no. 2, pp. 328–345, 2010. View at Publisher · View at Google Scholar · View at Scopus
  6. L. Rosen, “The natural history of Japanese encephalitis virus,” Annual Review of Microbiology, vol. 40, pp. 395–414, 1986. View at Publisher · View at Google Scholar · View at Scopus
  7. A. F. van den Hurk, S. A. Ritchie, and J. S. Mackenzie, “Ecology and geographical expansion of japanese encephalitis virus,” Annual Review of Entomology, vol. 54, pp. 17–35, 2009. View at Publisher · View at Google Scholar · View at Scopus
  8. J. S. Mackenzie, D. J. Gubler, and L. R. Petersen, “Emerging flaviviruses: the spread and resurgence of Japanese encephalitis, West Nile and dengue viruses,” Nature Medicine, vol. 10, no. 12, pp. S98–S109, 2004. View at Publisher · View at Google Scholar · View at Scopus
  9. G. J. Sips, J. Wilschut, and J. M. Smit, “Neuroinvasive flavivirus infections,” Reviews in Medical Virology, vol. 22, no. 2, pp. 69–87, 2012. View at Publisher · View at Google Scholar · View at Scopus
  10. T. Solomon, “Flavivirus encephalitis,” The New England Journal of Medicine, vol. 351, no. 4, pp. 370–378, 2004. View at Publisher · View at Google Scholar · View at Scopus
  11. M. Kalia, R. Khasa, M. Sharma, M. Nain, and S. Vrati, “Japanese encephalitis virus infects neuronal cells through a clathrin-independent endocytic mechanism,” Journal of Virology, vol. 87, no. 1, pp. 148–162, 2013. View at Publisher · View at Google Scholar · View at Scopus
  12. Y. Zhu, Q. Xu, D. Wu et al., “Japanese encephalitis virus enters rat neuroblastoma cells via a pH dependent, dynamin and caveola-mediated endocytosis pathway,” Journal of Virology, vol. 86, no. 24, pp. 13407–13422, 2012. View at Publisher · View at Google Scholar · View at Scopus
  13. M. Nawa, T. Takasaki, K. Yamada, I. Kurane, and T. Akatsuka, “Interference in Japanese encephalitis virus infection of Vero cells by a cationic amphiphilic drug, chlorpromazine,” Journal of General Virology, vol. 84, no. 7, pp. 1737–1741, 2003. View at Publisher · View at Google Scholar · View at Scopus
  14. S. Yang, M. He, X. Liu, X. Li, B. Fan, and S. Zhao, “Japanese encephalitis virus infects porcine kidney epithelial PK15 cells via clathrin- and cholesterol-dependent endocytosis,” Virology Journal, vol. 10, article 258, 2013. View at Publisher · View at Google Scholar · View at Scopus
  15. S. Das, S. V. Laxminarayana, N. Chandra, V. Ravi, and A. Desai, “Heat shock protein 70 on Neuro2a cells is a putative receptor for Japanese encephalitis virus,” Virology, vol. 385, no. 1, pp. 47–57, 2009. View at Publisher · View at Google Scholar · View at Scopus
  16. Y. Z. Zhu, M. M. Cao, W. B. Wang, H. Ren, P. Zhao, and Z. Qi, “Association of heat-shock protein 70 with lipid rafts is required for japanese encephalitis virus infection in Huh7 cells,” Journal of General Virology, vol. 93, no. 1, pp. 61–71, 2012. View at Publisher · View at Google Scholar · View at Scopus
  17. S. Das, V. Ravi, and A. Desai, “Japanese encephalitis virus interacts with vimentin to facilitate its entry into porcine kidney cell line,” Virus Research, vol. 160, no. 1-2, pp. 404–408, 2011. View at Publisher · View at Google Scholar · View at Scopus
  18. Y. Chien, W. Chen, W. Hsu, and S. Chiou, “Bovine lactoferrin inhibits Japanese encephalitis virus by binding to heparan sulfate and receptor for low density lipoprotein,” Virology, vol. 379, no. 1, pp. 143–151, 2008. View at Publisher · View at Google Scholar · View at Scopus
  19. T. Thongtan, N. Wikan, P. Wintachai et al., “Characterization of putative Japanese encephalitis virus receptor molecules on microglial cells,” Journal of Medical Virology, vol. 84, no. 4, pp. 615–623, 2012. View at Publisher · View at Google Scholar · View at Scopus
  20. W. C. Black, K. E. Bennett, N. Gorrochótegui-Escalante et al., “Flavivirus susceptibility in Aedes aegypti,” Archives of Medical Research, vol. 33, no. 4, pp. 379–388, 2002. View at Publisher · View at Google Scholar · View at Scopus
  21. M. Nawa, “Effects of bafilomycin A1 on Japanese encephalitis virus in C6/36 mosquito cells,” Archives of Virology, vol. 143, no. 8, pp. 1555–1568, 1998. View at Publisher · View at Google Scholar · View at Scopus
  22. J. Ren, T. Ding, W. Zhang, J. Song, and W. Ma, “Does Japanese encephalitis virus share the same cellular receptor with other mosquito-borne flaviviruses on the C6/36 mosquito cells?” Virology Journal, vol. 4, article 83, 2007. View at Publisher · View at Google Scholar · View at Scopus
  23. V. Boonsanay and D. R. Smith, “Entry into and production of the Japanese encephalitis virus from C6/36 cells,” Intervirology, vol. 50, no. 2, pp. 85–92, 2007. View at Publisher · View at Google Scholar · View at Scopus
  24. S. Jindadamrongwech, C. Thepparit, and D. R. Smith, “Identification of GRP 78 (BiP) as a liver cell expressed receptor element for dengue virus serotype 2,” Archives of Virology, vol. 149, no. 5, pp. 915–927, 2004. View at Publisher · View at Google Scholar · View at Scopus
  25. T. Limjindaporn, W. Wongwiwat, S. Noisakran et al., “Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production,” Biochemical and Biophysical Research Communications, vol. 379, no. 2, pp. 196–200, 2009. View at Publisher · View at Google Scholar · View at Scopus
  26. S. Upanan, A. Kuadkitkan, and D. R. Smith, “Identification of dengue virus binding proteins using affinity chromatography,” Journal of Virological Methods, vol. 151, no. 2, pp. 325–328, 2008. View at Publisher · View at Google Scholar · View at Scopus
  27. D. T. Rutkowski and R. J. Kaufman, “A trip to the ER: coping with stress,” Trends in Cell Biology, vol. 14, no. 1, pp. 20–28, 2004. View at Publisher · View at Google Scholar · View at Scopus
  28. M. Schröder, “Endoplasmic reticulum stress responses,” Cellular and Molecular Life Sciences, vol. 65, no. 6, pp. 862–894, 2008. View at Publisher · View at Google Scholar · View at Scopus
  29. C. Xu, B. Bailly-Maitre, and J. C. Reed, “Endoplasmic reticulum stress: cell life and death decisions,” Journal of Clinical Investigation, vol. 115, no. 10, pp. 2656–2664, 2005. View at Publisher · View at Google Scholar · View at Scopus
  30. A. Delpino and M. Castelli, “The 78 kDa glucose-regulated protein (GRP78/BIP) is expressed on the cell membrane, is released into cell culture medium and is also present in human peripheral circulation,” Bioscience Reports, vol. 22, no. 3-4, pp. 407–420, 2002. View at Publisher · View at Google Scholar · View at Scopus
  31. B. K. Shin, H. Wang, A. M. Yim et al., “Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function,” The Journal of Biological Chemistry, vol. 278, no. 9, pp. 7607–7616, 2003. View at Publisher · View at Google Scholar · View at Scopus
  32. M. Triantafilou, D. Fradelizi, and K. Triantafilou, “Major histocompatibility class one molecule associates with glucose regulated protein (GRP) 78 on the cell surface,” Human Immunology, vol. 62, no. 8, pp. 764–770, 2001. View at Publisher · View at Google Scholar · View at Scopus
  33. G. Xiao, T. Chung, H. Y. Pyun, R. E. Fine, and R. J. Johnson, “KDEL proteins are found on the surface of NG108-15 cells,” Molecular Brain Research, vol. 72, no. 2, pp. 121–128, 1999. View at Publisher · View at Google Scholar · View at Scopus
  34. M. A. Alhoot, S. M. Wang, and S. D. Sekaran, “RNA interference mediated inhibition of dengue virus multiplication and entry in HepG2 cells,” PLoS ONE, vol. 7, no. 3, Article ID e34060, 2012. View at Publisher · View at Google Scholar · View at Scopus
  35. K. Triantafilou, D. Fradelizi, K. Wilson, and M. Triantafilou, “GRP78, a coreceptor for coxsackievirus A9, interacts with major histocompatibility complex class I molecules which mediate virus internalization,” Journal of Virology, vol. 76, no. 2, pp. 633–643, 2002. View at Publisher · View at Google Scholar · View at Scopus
  36. T. Thongtan, P. Cheepsunthorn, V. Chaiworakul, C. Rattanarungsan, N. Wikan, and D. R. Smith, “Highly permissive infection of microglial cells by Japanese encephalitis virus: a possible role as a viral reservoir,” Microbes and Infection, vol. 12, no. 1, pp. 37–45, 2010. View at Publisher · View at Google Scholar · View at Scopus
  37. M. M. Bradford, “A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding,” Analytical Biochemistry, vol. 72, no. 1-2, pp. 248–254, 1976. View at Publisher · View at Google Scholar · View at Scopus
  38. S. Hung, P. Lee, H. Chen, L. Chen, C. Kao, and C. King, “Analysis of the steps involved in dengue virus entry into host cells,” Virology, vol. 257, no. 1, pp. 156–167, 1999. View at Publisher · View at Google Scholar · View at Scopus
  39. M. Panyasrivanit, A. Khakpoor, N. Wikan, and D. R. Smith, “Co-localization of constituents of the dengue virus translation and replication machinery with amphisomes,” Journal of General Virology, vol. 90, no. 2, pp. 448–456, 2009. View at Publisher · View at Google Scholar · View at Scopus
  40. M. D. Abramoff, P. J. Magelhaes, and S. J. Ram, “Image processing with image,” Journal of Biophotonics International, vol. 11, pp. 36–42, 2004. View at Google Scholar
  41. A. P. French, S. Mills, R. Swarup, M. J. Bennett, and T. P. Pridmore, “Colocalization of fluorescent markers in confocal microscope images of plant cells,” Nature Protocols, vol. 3, no. 4, pp. 619–628, 2008. View at Publisher · View at Google Scholar · View at Scopus
  42. M. Gonzalez-Gronow, S. J. Kaczowka, S. Payne, F. Wang, G. Gawdi, and S. V. Pizzo, “Plasminogen structural domains exhibit different functions when associated with cell surface GRP78 or the voltage-dependent anion channel,” Journal of Biological Chemistry, vol. 282, no. 45, pp. 32811–32820, 2007. View at Publisher · View at Google Scholar · View at Scopus
  43. M. Gonzalez-Gronow, M. A. Selim, J. Papalas, and S. V. Pizzo, “GRP78: a multifunctional receptor on the cell surface,” Antioxidants and Redox Signaling, vol. 11, no. 9, pp. 2299–2306, 2009. View at Publisher · View at Google Scholar · View at Scopus
  44. A. Nakatsuka, J. Wada, I. Iseda et al., “Visceral adipose tissue-derived serine proteinase inhibitor inhibits apoptosis of endothelial cells as a ligand for the cell-surface GRP78/voltage-dependent anion channel complex,” Circulation Research, vol. 112, no. 5, pp. 771–780, 2013. View at Publisher · View at Google Scholar · View at Scopus
  45. M. Ni, Y. Zhang, and A. S. Lee, “Beyond the endoplasmic reticulum: atypical GRP78 in cell viability, signalling and therapeutic targeting,” Biochemical Journal, vol. 434, no. 2, pp. 181–188, 2011. View at Publisher · View at Google Scholar · View at Scopus
  46. M. Colombini, “VDAC structure, selectivity, and dynamics,” Biochimica et Biophysica Acta: Biomembranes, vol. 1818, no. 6, pp. 1457–1465, 2012. View at Publisher · View at Google Scholar · View at Scopus
  47. V. Shoshan-Barmatz and M. Golan, “Mitochondrial VDAC1: function in cell life and death and a target for cancer therapy,” Current Medicinal Chemistry, vol. 19, no. 5, pp. 714–735, 2012. View at Publisher · View at Google Scholar · View at Scopus
  48. Y. Shi, J. Chen, C. Weng et al., “Identification of the protein-protein contact site and interaction mode of human VDAC1 with Bcl-2 family proteins,” Biochemical and Biophysical Research Communications, vol. 305, no. 4, pp. 989–996, 2003. View at Publisher · View at Google Scholar · View at Scopus
  49. V. Shoshan-Barmatz and A. Israelson, “The voltage-dependent anion channel in endoplasmic/sarcoplasmic reticulum: Characterization, modulation and possible function,” Journal of Membrane Biology, vol. 204, no. 2, pp. 57–66, 2005. View at Publisher · View at Google Scholar · View at Scopus
  50. V. Shoshan-Barmatz, R. Zalk, D. Gincel, and N. Vardi, “Subcellular localization of VDAC in mitochondria and ER in the cerebellum,” Biochimica et Biophysica Acta—Bioenergetics, vol. 1657, no. 2-3, pp. 105–114, 2004. View at Publisher · View at Google Scholar · View at Scopus
  51. L. G. Gebhard, S. B. Kaufman, and A. V. Gamarnik, “Novel ATP-independent RNA annealing activity of the dengue virus NS3 helicase,” PLoS ONE, vol. 7, no. 4, Article ID e36244, 2012. View at Publisher · View at Google Scholar · View at Scopus