Atomic-level functional model of dengue virus Envelope protein infectivity.

ABSTRACT: A number of structures have been solved for the Envelope (E) protein from dengue virus and closely related flaviviruses, providing detailed pictures of the conformational states of the protein at different stages of infectivity. However, the key functional residues responsible for mediating the dynamic changes between these structures remain largely unknown. Using a comprehensive library of functional point mutations covering all 390 residues of the dengue virus E protein ectodomain, we identified residues that are critical for virus infectivity, but that do not affect E protein expression, folding, virion assembly, or budding. The locations and atomic interactions of these critical residues within different structures representing distinct fusogenic conformations help to explain how E pro

SUBMITTER: Christian EA 

PROVIDER: S-EPMC3831943 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature