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The dengue virus envelope protein E is a membrane-spanning glycoprotein that plays a central role in the life cycle of the dengue virus. It is both the principal determinant of icosahedral virion assembly and acts as the fusion catalyst for merging viral and host cell membranes. The mature surface of each dengue virion is covered with 180 copies of this E protein arranged as homodimers. The E protein folds into three distinct domains: Domain I (ED1), Domain II (ED2), and Domain III (ED3). It mediates attachment to host cells and triggers fusion between viral and cellular membranes upon endosomal acidification. It is a major target for neutralizing antibodies.
Small-molecule inhibitors targeting the hydrophobic pocket at an interdomain interface.
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