A conserved element in the flavivirus genomic 5′ terminus switches its conformation in response to long-range RNA interactions, and thereby regulates the dynamic recruitment of viral replicase for efficient viral RNA replication.

The ER membrane protein complex (EMC) facilitates the correct topology of the flavivirus non-structural proteins NS4A and NS4B at the ER membrane critical for viral replication.

The Zika virus subgenomic flaviviral RNA binds to and inhibits the fragile X mental retardation protein, a novel Zika virus restriction factor.

Benzene mapping simulations of envelope protein rafts from six different flaviviruses reveal a conserved cryptic site whose cluster of ionisable residues is likely responsible for orchestrating pH-dependent conformational changes during fusion, thereby representing an attractive target for antiviral development.

The West Nile Virus envelope protein catalyzes membrane fusion through low-pH induced conformational rearrangement, with a rate determined by the formation of two trimeric complexes at the contact zone between the virus and target membrane.

A novel virus-inclusive single cell RNA-Seq approach enables identification of novel pro- and antiviral host factors in human cells in response to dengue and Zika virus infection.

Single-particle studies of dengue-virus membrane fusion and the effect of small-molecule inhibitors of infection clarify the viral fusion mechanism.

The Dengue virus contains discretely folded RNA structures that confer the ability to resist a powerful host cell enzyme and produce a disease-inducing noncoding RNA.

Data-driven methods predict over 35 mosquitoes are potential vectors of Zika virus, suggesting a larger geographic area and a greater human population is at risk of infection.