Vijaya Satchidanandam
  • Department of Microbiology and Cell Biology, Indian Institute of Science, India
研究方向
  • Immunology
个人信息

Education

Ph.D. in Biochemistry, Indian Institute of Science, 1983

Current position

Professor, Indian Institute of Science (10/2003-present)

Publications (since 2000)

  1. Asokan, M., Sachidanandam, V., Satish, K. S. and Ranga, U. (2014). Attenuation of immune activation in an open-label clinical trial for HIV-AIDS using a polyherbal formulation. Virusdisease 25(3): 302-313.
  2. Satchidanandam, V., Kumar, N., Jumani, R. S., Challu, V., Elangovan, S. and Khan, N. A. (2014). The glycosylated Rv1860 protein of Mycobacterium tuberculosis inhibits dendritic cell mediated TH1 and TH17 polarization of T cells and abrogates protective immunity conferred by BCG. PLoS Pathog 10(6): e1004176.
  3. Surana, P., Satchidanandam, V. and Nair, D. T. (2014). RNA-dependent RNA polymerase of Japanese encephalitis virus binds the initiator nucleotide GTP to form a mechanistically important pre-initiation state. Nucleic Acids Res 42(4): 2758-2773.
  4. Tyagi, A. K., Nangpal, P. and Satchidanandam, V. (2011). Development of vaccines against tuberculosis. Tuberculosis (Edinb) 91(5): 469-478.
  5. Krishna, V. D., Rangappa, M. and Satchidanandam, V. (2009). Virus-specific cytolytic antibodies to nonstructural protein 1 of Japanese encephalitis virus effect reduction of virus output from infected cells. J Virol 83(10): 4766-4777.
  6. Satchidanandam, V., Uchil, P. D. and Kumar, P. (2006). Organization of flaviviral replicase proteins in virus-induced membranes: a role for NS1' in Japanese encephalitis virus RNA synthesis. Novartis Found Symp 277: 136-145; discussion 145-138, 251-133.
  7. Sinha, A., Singh, A., Satchidanandam, V. and Natarajan, K. (2006). Impaired generation of reactive oxygen species during differentiation of dendritic cells (DCs) by Mycobacterium tuberculosis secretory antigen (MTSA) and subsequent activation of MTSA-DCs by mycobacteria results in increased intracellular survival. J Immunol 177(1): 468-478.
  8. Uchil, P. D., Kumar, A. V. and Satchidanandam, V. (2006). Nuclear localization of flavivirus RNA synthesis in infected cells. J Virol 80(11): 5451-5464.
  9. Satchidanandam, V., Uchil, P. D. and Kumar, P. (2006). Organization of flaviviral replicase proteins in virus-induced membranes: a role for NS1' in Japanese encephalitis virus RNA synthesis. Novartis Found Symp 277: 136-145; discussion 145-138, 251-133.
  10. Kumar, P., Sulochana, P., Nirmala, G., Haridattatreya, M. and Satchidanandam, V. (2004). Conserved amino acids 193-324 of non-structural protein 3 are a dominant source of peptide determinants for CD4+ and CD8+ T cells in a healthy Japanese encephalitis virus-endemic cohort. J Gen Virol 85(Pt 5): 1131-1143.
  11. Kumar, P., Krishna, V. D., Sulochana, P., Nirmala, G., Haridattatreya, M. and Satchidanandam, V. (2004). Cell-mediated immune responses in healthy children with a history of subclinical infection with Japanese encephalitis virus: analysis of CD4+ and CD8+ T cell target specificities by intracellular delivery of viral proteins using the human immunodeficiency virus Tat protein transduction domain. J Gen Virol 85(Pt 2): 471-482.
  12. Kumar, P., Sulochana, P., Nirmala, G., Chandrashekar, R., Haridattatreya, M. and Satchidanandam, V. (2004). Impaired T helper 1 function of nonstructural protein 3-specific T cells in Japanese patients with encephalitis with neurological sequelae. J Infect Dis 189(5): 880-891.
  13. Uchil, P. D. and Satchidanandam, V. (2003). Architecture of the flaviviral replication complex. Protease, nuclease, and detergents reveal encasement within double-layered membrane compartments. J Biol Chem 278(27): 24388-24398.
  14. Kumar, P., Uchil, P. D., Sulochana, P., Nirmala, G., Chandrashekar, R., Haridattatreya, M. and Satchidanandam, V. (2003). Screening for T cell-eliciting proteins of Japanese encephalitis virus in a healthy JE-endemic human cohort using recombinant baculovirus-infected insect cell preparations. Arch Virol 148(8): 1569-1591.
  15. Satchidanandam, V., Amara, R. R., Uchil, P. D. and Singh, V. (2003). The regulatory elements of the Mycobacterium tuberculosis gene Rv3881c function efficiently in Escherichia coli. FEMS Microbiol Lett 218(2): 365-370.
  16. Kumar, P., Amara, R. R., Challu, V. K., Chadda, V. K. and Satchidanandam, V. (2003). The Apa protein of Mycobacterium tuberculosis stimulates gamma interferon-secreting CD4+ and CD8+ T cells from purified protein derivative-positive individuals and affords protection in a guinea pig model. Infect Immun 71(4): 1929-1937.
  17. Uchil, P. D. and Satchidanandam, V. (2003). Characterization of RNA synthesis, replication mechanism, and in vitro RNA-dependent RNA polymerase activity of Japanese encephalitis virus. Virology 307(2): 358-371.
  18. Uchil, P. D. and Satchidanandam, V. (2001). Phylogenetic analysis of Japanese encephalitis virus: envelope gene based analysis reveals a fifth genotype, geographic clustering, and multiple introductions of the virus into the Indian subcontinent. Am J Trop Med Hyg 65(3): 242-251.
  19. Kumar, P. and Satchidanandam, V. (2000). Ethyleneglycol-bis-(beta-aminoethylether)tetraacetate as a blood anticoagulant: preservation of antigen-presenting cell function and antigen-specific proliferative response of peripheral blood mononuclear cells from stored blood. Clin Diagn Lab Immunol 7(4): 578-583.
  20. Amara, R. R. and Satchidanandam, V. (2000). Refinements of the differential display reverse transcription-polymerase chain reaction technique: use of oligo(dT)-based anchored primers with Escherichia coli messenger RNA identifies a salt-induced promoter in the dcw gene cluster. Anal Biochem 278(1): 83-86.

Books

  1. Ramasarma, T., Vijaya, S., Puranam, R. S. and Kurup, C. K. R. (1988). Electron transfer in hydroxylamine-modified cytochrome c. In: Zaidi, Z. H. (ed). Protein structure-function relationship. Elsevier Science Publishers, pp 251-259.
  2. Satchidanandam, V., Narayanaswamy, E. and Moss, B. (1988). Engineering vaccinia virus vectors that express hybrid proteins containing immunogenic sequences on the cell surface. In: Brown, F., Chanock, R. M. and Lerner, R. A. (eds). Vaccines 88. Cold Spring Harbor Laboratories, pp 211-214.
  3. Ramasarma, T., Vijaya, S., Rau, M., Khandke, L., Patole, M. S., Gulapalli, S., Penta, K., Chauduri, M. and Kurup, C. K. R. (1990). Vanadium as a biological hydrogen abstractive agent. In: Proceedings of Int. Symp. on Biological Oxidation Systems. Academic Press, pp 909-928.