ABSTRACT The major envelope glycoprotein E of dengue (DEN) virus plays a central role in the biology of flaviviruses. It is capable of inducing a protective immune response in vivo and responsible for the viral binding to the cellular receptor. The crystal structures of glycoprotein E ectodomains have already been determined. However, it is still un-clear where the well-defined B-cell epitopes for glycoprotein E which induce the neutralizing an-tibodies locates. Thus, in order to characterize the role of glycoprotein E in the pathogenesis of dengue virus infection, we first used network servers (http://bio.dfci. harvard.edu/Tools/ &amp; http://www. imtech. res. in) to predict and analyze the well defined B-cell and T-cell epitopes of the glycoprotein of the DEN-1 HAWAII strain. Then based on the highly conserved envelop glyco-protein amino acids, the hydrophilicity, antigenic-ity, accessibility and flexibility of envelop glyco-protein E were further predicted by using Biotic softwares (DNASTAR) and network servers (http://bio. dfci.harvard.edu/Tools/), the secondary structure was putatively obtained. In our study, the sequence at 281-295 amino acid (aa) for den-gue virus type 1 HAWAII strain and the sequence at 345-359, 383-397 for dengue virus type 2 NGC strain were predicted as the more prevalent epi-topes by using multiple parameters and different analysis softwares, respectively. Two epitopes of DEN-2 and one of DEN-1 locate on the domain Ш and domainⅡ of the protein E, respectively. Sub-sequently, further studies will be carried out to examine the antigenicity and protection of the synthetic peptides with higher scores in the av-erage antigen index (AI) and better hydrophilic properties determined by our data.
Cite this paper
nullZhong, H. , Zhao, W. , Peng, L. , Li, S. and Cao, H. (2009) Bioinformatics analysis and characteristics of envelop glycoprotein E epitopes of dengue virus. Journal of Biomedical Science and Engineering, 2, 123-127. doi: 10.4236/jbise.2009.22022.
 T. Monath.(1994) Dengue: the risk to developed and developing countries. Proc Natl Acad Sci USA 91, 2395-2400.
 R. J. Kuhn, W. Zhang, M. G. Rossmann. (2002) Structure of dengue virus: implications for flavivirus organization, matu--ration, and fusion. Cell 108, 717-725.
 E. A. Henchal, J. R. Putnak. (1990) The dengue viruses. Clin Microbiol Rev 3, 376-396.
 C. M. Rice, B. N. Fields, D. M. Knipe, P. M. Howley. (1996)Flaviviridae: the viruses and their replication. Virology 3, 931-959.
 J. T. Roehrig. Immunochemistry of the dengue viruses, 199-219 In: D. J. Gubler and G. Kuno (eds), Dengue and dengue hemorrhagic fever. CAB International, New York, N. Y. 1997.
 G. J. Chang, Molecular biology of dengue viruses, 175-198 In: D. J. Gubler, G. Kuno (eds.), Dengue and Dengue Hemorrhagic Fever. CAB International, London, 1997.
 A. S. Kolaskar, P. C. Tongaonkar. (1990) A semi-empirical method for prediction of antigenic determinants on protein anti-gens, FEBS Lett 276, 172-174.
 M. Levitt, J. Greer. (1977) Automatic identification of secondary structure in globular proteins. J Mol Biol 114, 181-239.
 J Cheng. (2008) A multi-template combination algorithm for protein comparative modeling. BMC Structural Biology 8, 18-36.
 G. Deleage, B. Roux. (1987) An algorithm for protein secondary structure prediction based on class prediction. Protein Eng 1, 289-294.
 J. Martin, J. F. Gibrat, F. Rodolphe. (2006) Analysis of an opti-mal hidden Markov model for secondary structure prediction. BMC Structural Biology 6, 25-45.
 E. A. Emini, J. V. Hughes, D. S. Peflow. (1985) Induction of hepa-titis A vires-neutralizing antibody by a vires-specific syn-thetic peptide. J Virol 55,836-839.
 P. A. Karplus, G. Schultz. (1985) Prediction of chain flexibility in proteins. Naturwissenschaften 72, 212-213.
 Y. Modis, S. Ogata, D. Clements. (2003) A ligand-binding pockets in the dengue virus envelop glycoprotein. Science 100, 6986-6991.