Viruses have evolved a wide variety of ways to exploit parts of their host cells to avoid detection and to grow. Researchers at the Scripps Research Institute and the Berkeley Center for Structural Biology are learning more about how hepatitis C works to deceive its host cells.
At the cellular level, as a virus invades, its DNA or RNA trigger immune responses in the healthy host cells. How this process is triggered and a better understanding of the specific enzymes involved is still being defined. A collaboration across multiple X-ray facilities, including the Berkeley Center for Structural Biology beamlines at the Advanced Light Source (ALS), compared the enzymes involved in both human and insect immune responses. They used protein crystallography to closely examine the structures, and learned that although overall function is similar, each group of organisms has a slightly different DNA-binding surface and resulting molecular immune response.
Every time our cells divide, the DNA inside must be copied accurately to avoid mistakes that could be harmful to our health. Known as DNA synthesis, the precise sequence of steps has until now only been hypothesized. In a recent study, timestamps have been added to step-by-step snapshots, revealing a switch-up between two of the steps that, if replicated in additional studies, would upend our current assumptions of the process.
Researchers from the Baylor College of Medicine employed previously constructed DNA-encoded chemistry technology (DEC-tec) libraries to identify several candidate molecules that could inhibit the action of Mpro, the main protease of SARS-CoV-2. In a recent study, the researchers described CDD-1713, a new inhibitor to the enzyme Mpro that is involved in propagating the virus. The X-ray crystallographic data, which was collected by Banumathi Sankaran in the Molecular Biophysics and Integrated Bioimaging Division, allowed the researchers to determine that CDD-1713 inhibits the activity of Mpro by binding in the active site of this enzyme.
Scientists at the Berkeley Center for Structural Biology contributed resources and data to a recently-published study revealing a new site on the coronavirus spike protein used by antibodies to block the invasion of the virus into healthy cells. The discovery of this new antibody binding site will help scientists as they work to continue improving treatment and vaccine formulations for COVID-19 and its variants.