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. 2023 Jun 2;14:1200195. doi: 10.3389/fimmu.2023.1200195

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Copyright © 2023 Sarker, Dhama and Gupta

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Structural organization of dengue virus envelope protein. The RNA genome of dengue virus is composed of a single ORF, flanking by 5’ and 3’ untranslated region. The ORF includes coding sequence of three structural proteins, and seven non-structural proteins. The envelope (E) is the most significant structural protein of dengue virus surface. The monomer of each of the envelope protein is arranged into head-to-tail homo-dimer and 90 of such dimers are arrange in icosahedral symmetry to constitute the complete surface of dengue virus. Each of the monomeric envelope protein consists of three ecto-domains: EDI, EDII and EDIII. The domain I, II and III are denoting by red, golden and violet color respectively.