Coronavirus SARS-CoV2: BESSY II data accelerate drug development

A coronavirus is threatening human health. SARS-CoV-2 is highly infectious and can cause severe pneumonia (COVID-19). A team has now found a promising approach to understanding the virus. Using the high-intensity X-ray light from the Berlin synchrotron source BESSY II, they have decoded the 3D architecture of the main protease of SARS-CoV-2. This protein plays a central role in the reproduction of the virus.

Teams around the world are working hard to develop active substances against SARS-CoV-2. The structural analysis of functional proteins of the virus is very helpful for this goal. The function of a protein is closely related to its 3D architecture. If this 3D architecture is known, it is possible to identify specific points of attack for active substances.

A special protein is responsible for the reproduction of the viruses: the viral main protease (Mpro or also 3CLpro). A team led by Prof. Dr. Rolf Hilgenfeld, University of Lübeck, has now decoded the 3D architecture of the main protease of SARS-CoV-2. The researchers have used the high-intensity X-ray light from the BESSY II facility of the Helmholtz-Zentrum Berlin.

“For such issues of highest relevance, we can offer fast track access to our instruments,” says Dr. Manfred Weiss, who heads the Research Group Macromolecular Crystallography (MX) at HZB. At the so-called MX instruments tiny protein crystals can be analysed with highly brilliant X-ray light. The images contain information about the 3D architecture of the protein molecules. The complex shape of the protein molecule and its electron density is then calculated by computer algorithms.

The 3D architecture provides concrete starting points for developing active substances or inhibitors. These drugs could dock specifically to target points of the macromolecule and impede its function. Rolf Hilgenfeld is an expert in the field of virology and already developed an inhibitor against the SARS-virus during the 2002/2003 SARS pandemic. In 2016, he succeeded in deciphering an enzyme of the Zika virus.

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Materials provided by Helmholtz-Zentrum Berlin für Materialien und Energie. Note: Content may be edited for style and length.

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