Understanding what makes COVID-19 more infectious than SARS

Australian and International researchers continue to have rapid access to the macromolecular and microfocus beamlines at the Australian Synchrotron to solve protein structures in the fight against COVID-19.

“Since coming out of a hard lockdown, we are now accepting proposals for other research,” said Principal Scientist Dr Alan Riboldi-Tunnicliffe.

“Because scientists can access the beamline remotely, they do not have to worry about changes to borders and travel restrictions.”

There have been a number of COVID-19 publications, which included structural information about key proteins in the virus, from the beamlines.

Instrument scientist Dr Eleanor Campbell reports that an international team of researchers led by the University of Bristol (UK) have identified a possible cause of SARS-CoV-2’s increased infectivity compared to SARS-CoV (the virus which emerged in China in 2003) , which could provide a target for developing COVID-19 therapies.

Australian collaborators included researchers from the Institute of Molecular Bioscience at the University of Queensland, who sent the samples to the Australian Synchrotron.

Read more on the Australian Synchrotron website

In search of the perfect system

Researchers take a new approach to improve widely used biotechnology tool

The unique relationship between an essential vitamin and a purified bacterial protein has been used as a valuable tool in science and medicine for several decades. Together these two molecules, known as streptavidin and biotin, form a very strong and specific interaction that is invaluable for many biotechnological applications.

Labeling molecules with biotin and detecting them with streptavidin is a common part of many lab tests and has enabled many scientific discoveries in medicine. Streptavidin and biotin are as essential to lab technicians as hammers and nails are to a carpenter. The two molecules combine to form “molecular glue” for many of the tests used to diagnose infectious diseases like HIV, Hepatitis C and Lyme disease, to discover new proteins, viruses and bacteria, and to explore how molecules function in living organisms.

Read more on the Canadian Light Source website

Image: Trapped biotin: A crystal structure of the M88 mutein, determined at the CMCF beamline at CLS, reveals how the engineered disulphide formed between Cys49 and Cys86 (green spheres) partially block the exit pathway for biotin (magenta spheres). Credit: CLS