To develop specific anti-coronavirus therapeutics and prophylactics, the molecular mechanism that underlies viral infection must first be defined. The recent study published in Cell Research solved the X-ray crystal structure of six-helical bundle (6-HB) core of the HR1 and HR2 domains in the SARS-CoV-2 S protein S2 subunit, revealing that several mutated amino acid residues in the HR1 domain may be associated with enhanced interactions with the HR2 domain, as compared to SARS-CoV. Previously developed a pan-coronavirus fusion inhibitor, EK1, which targeted the HR1 domain, was used as a starting molecule to design a series of new inhibitors, of which EK1C4 potently inhibited the replication of 5 live human coronaviruses examined, including SARS-CoV-2. Intranasal application of EK1C4 before or after challenge with HCoV-OC43 protected mice from infection, suggesting that EK1C4 could be used for prevention and treatment of infection by the currently circulating SARS-CoV-2 and other emerging SARSr-CoVs.
In CF Diffraction Techniques, we have successfully upgraded the X-ray source of the SAXS instrument. The upgrade of MetalJet C2 to D2+ brought
more than double intensity of the primary beam. The instrument enables rapid standard SAXS measurements with a low volume autosampler, SEC-SAXS
experiments or special applications, now with substantially improved signal to noise ratio.
The Biomolecular Interactions and Crystallography Core Facility of CEITEC MU is very happy to announce the installation of a new cutting-edge instrument that will assist in the characterization of macromolecular complexes. Mass photometer TwoMP (Refeyn) is designed to precisely determine the molecular mass of proteins, nucleic acids, and other macromolecules in a broad range of sizes.