Dengue neurovirulence in mice: identification of molecular signatures in the E and NS3 helicase domains
Copyright policy )Dengue neurovirulence in mice: identification of molecular signatures in the E and NS3 helicase domains
AbstractRecent observations indicate that the clinical profile of dengue virus (DENV) infection is changing, and that neurological manifestations are becoming frequent. The neuro pathogenesis of dengue, and the contribution of viral and host factors to the disease are not well understood. To define the amino acid substitutions in DENV potentially implicated in the acquisition of a neurovirulent phenotype we used a murine model to characterize two neuroadapted strains of DENV‐1, FGA/NA a5c (previously obtained), and FGA/NA P6 (recently obtained). Only three amino acid substitutions were identified in the neurovirulent strains, mapping to the E and NS3 helicase domains. These mutations enhanced the ability of neuroadapted viral strains to replicate in the CNS of infected mice, causing extensive damage with leptomeningitis and encephalitis. J. Med. Virol. 79:1506–1517, 2007. © Wiley‐Liss, Inc.
Models, Molecular, Neurons, Virulence, Serine Endopeptidases, Dengue Virus, Viral Nonstructural Proteins, Nervous System, Protein Structure, Tertiary, Dengue, Mice, Viral Envelope Proteins, Animals, Point Mutation, Cells, Cultured, RNA Helicases
Models, Molecular, Neurons, Virulence, Serine Endopeptidases, Dengue Virus, Viral Nonstructural Proteins, Nervous System, Protein Structure, Tertiary, Dengue, Mice, Viral Envelope Proteins, Animals, Point Mutation, Cells, Cultured, RNA Helicases
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