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The E glycoprotein of dengue virus is responsible for the viral binding to the receptor. The crystal structure of envelope glycoprotein has already been determined. However, where the well-defined Bcell and T-cell epitopes are located is still a question. Because of the large variations among the four dengue genotypes, it is very hard to design conserved epitopes for all of them. Therefore, we selected only one genotype (DENV3). The conserved regions were found in more than 600 DENV E glycoprotein sequences. Both the B-cell and T-cell epitopes were predicted and the hydrophobicity, antigenicity, accessibility and flexibility of the highly conserved E glycoprotein were further predicted by using different bioinformatics algorithms. The secondary structure was obtained and the predicted epitopes were pointed out in it. Binding sites on glycoprotein of DENV-3 for attachment of virus to the receptor was identified, while keeping those attachments in which new drugs for dengue related infections could not be designed.
Key words: Glycoprotein, DENV3, epitopes, antigenecity, B-cell, T-cell, vaccine.