Reverse engineering synthetic antiviral amyloids

Human amyloids have been shown to interact with viruses and interfere with viral replication. Based on this observation, we employed a synthetic biology approach in which we engineered virus-specific amyloids against influenza A and Zika proteins. Each amyloid shares a homologous aggregation-prone fragment with a specific viral target protein. For influenza we demonstrate that a designer amyloid against PB2 accumulates in influenza A-infected tissue in vivo. Moreover, this amyloid acts specifically against influenza A and its common PB2 polymorphisms, but not influenza B, which lacks the homologous fragment. Our model amyloid demonstrates that the sequence specificity of amyloid interactions has the capacity to tune amyloid-virus interactions while allowing for the flexibility to maintain activity on evolutionary diverging variants. Some human amyloid proteins have been shown to interact with viral proteins, suggesting that they may have potential as therapeutic agents. Here the authors design synthetic amyloids specific for influenza A and Zika virus proteins, respectively, and show that they can inhibit viral replication

Local modelling of sea surface topography from (geostrophic) ocean flow

Calculating locally without boundary correction would lead to errors near the boundary. To avoid these Gibbs phenomenona we additionally consider the boundary integral of the corresponding region on the sphere which occurs in the integral formula of the solution. For reasons of simplicity we discuss a spherical cap first, that means we consider a continuously differentiable (regular) boundary curve. In a second step we concentrate on a more complicated domain with a non continuously differentiable boundary curve, namely a rectangular region. It will turn out that the boundary integral provides a major part for stabilizing and reconstructing the approximation of the solution in our multiscale procedure