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A carbohydrate microarray provides insights into the antimalarial immune response. Kamena et al. (p 238) spotted synthetic GPI glycans onto glass slides to create a 'GPI chip'. Using this chip, the authors characterized the binding of anti-GPI antibodies from people in malaria-endemic and malaria-free regions and before and after malarial exposure (see also News and Views by Ferguson on p (223). Shown are images of the carbohydrate microarrays incubated with human sera, Giesma-stained red blood cells infected with Plasmodium falciparum and the chemical structures of GPI glycans displayed on the microarrays. Cover art by Erin Boyle based on images provided by Faustin Kamena and Marco Tamborrini.
Synthetic organic chemistry of complex natural products and their substructures provides challenges for the chemist and invaluable tools for the biologist. The production of a 'GPI chip', a device for simultaneously measuring and characterizing antibody responses to GPI structures, is applied to dissect malaria-induced antibody responses.
An in-depth biophysical look at lipids in the influenza viral envelope reveals disordered membranes at physiological temperatures, and will likely reshape the debate over the role of lipids and proteins in biomembranes.
Crystallographic analysis has been instrumental in revealing the molecular basis for the pharmacological properties of several natural and synthetic ligands of steroid receptors, but it is often a long and arduous process. A new method for stabilizing these receptors greatly accelerates this process, allowing generation of apo receptor crystals and the comparison of multiple structures to define pathway-specific interactions.
A20 protein, a regulator of inflammation and cell survival, modulates cellular signaling via two apparently opposite enzyme activities. Recent studies elucidate the unusual structural organization of the A20 protease domain and provide new mechanistic insights into its biological function.
Signaling via phosphorylation-regulated protein-protein interactions often involves flexible or unstructured proteins. Detailed biophysical and computational studies on one such interaction reveal a marvelously intricate, temporally regulated, multistep conduit for signal transduction in the cell cycle.