A team of researchers led by NCXT Director Carolyn Larabell, in collaboration with scientists at Heidelberg University in Germany, used a technique called soft X-ray tomography (SXT) to quickly scan and analyze human lung cells infected with SARS-CoV-2. SXT not only significantly shortens the time frame, but provides more detail—increasing the chances of distinguishing subtle changes in the cell.
BCSB Determines Interactions of Potential Inhibitor with SARS-CoV-2 Protease
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.
Scientist at Berkeley Lab Played a Hand in ‘Inescapable’ COVID-19 Antibody Discovery
An antibody therapy that appears to neutralize all known SARS-CoV-2 strains, and other coronaviruses, was developed with a little help from structural biologist Jay Nix.
Shape-shifting Protein Helps SARS-CoV-2 Evade Human Immune Defenses
Papain-like protease (PLpro) from SARS-CoV-2 plays essential roles in the replication cycle of the virus that is the cause of the global COVID-19 pandemic. In human cells that the virus has infected, PLpro seeks out and binds with the interferon-stimulated gene 15 (ISG15) protein, a key component of the cells’ immune response. PLpro strips ISG15 from other cellular proteins to aid SARS-CoV-2 in evading the body’s immune system.
Scientists at Oak Ridge National Laboratory (ORNL) used small-angle neutron scattering (SANS) at the High Flux Isotope Reactor (HFIR) combined with computational techniques to reveal the molecular details of how the two proteins interact. Susan Tsutakawa, a staff scientist in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division, obtained small-angle x-ray scattering (SAXS) data on the PLpro-ISG15 complex at Berkeley Lab’s Advanced Light Source (ALS) to augment the SANS work.
Scientists Analyze Dry-sanitizing Device for Reusable PPE
Current methods to decontaminate PPE are successful at eradicating the virus but compromise the PPE material, ultimately increasing the wearer’s potential exposure to pathogens. But scientists at the Berkeley Lab, in collaboration with the University of Nevada, Reno (UNR) School of Medicine, have confirmed that a new dry-sanitizing device may provide a safe and reliable solution that doesn’t alter the integrity of the PPE material.
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