MBIB News

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.

As instruments in large-scale user facilities are becoming more powerful, the volume of data and its complexity also grow. To leverage these heightened capabilities and accelerate scientific discoveries, a field known as autonomous discovery has emerged. It uses algorithms to learn from a comparatively little amount of input data and determine the best next experimental steps — all with minimal human intervention.

Mary Maxon, Associate Laboratory Director (ALD) for Biosciences, has been granted a one-year leave of absence to help advance science and technology opportunities for engineering biology and the U.S. bioeconomy. Beginning August 23, Maxon will work on temporary assignment with Schmidt Futures, a philanthropic initiative founded by Eric and Wendy Schmidt, as they launch a significant effort to seed the next wave of engineering biology and bioeconomy innovation. 

Paul Adams, Director of the Molecular Biophysics and Integrated Bioimaging (MBIB) Division, has been asked by Lab Director Mike Witherell to serve as the ALD for Biosciences over the coming year. While Adams is serving as Biosciences ALD, MBIB Deputy for Science Junko Yano will take on the role of Interim MBIB Division Director; Greg Hura has agreed to step into the role of Interim MBIB Science Deputy; and Susan Tsutakawa will be the Interim Head of the Structural Biology Department for the coming year.

Scientists from three national laboratories who specialize in revealing the atomic structure of proteins collaborated to model the complex protein responsible for SARS-CoV-2 replication, revealing potential weak spots for drug development. 

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.