An official celebration of ERIC status adoption takes place at the Royal Society, London on the 18th July 2017.
Instruct-ERIC launched in London
Jo Johnson recognised the value and relevance of collaborative work between the UK and European scientists.
2nd iNEXT Annual Users Meeting
The 2nd iNEXT Annual Users Meeting took place on 22nd-24th May 2017, in Brno (Czech Republic). The venue was the “BEST WESTERN PREMIER Hotel International Brno”, in the very center of the second largest city of the Czech Republic, where Gregor Mendel conducted his groundbreaking experiments and established a new scientific field of genetics.
The 3rd Instruct Biennial Structural Biology Conference
The 3rd Instruct Biennial Structural Biology Conference took place in Brno, Czech Republic, from May 24 to May 26, 2017 hosted by Instruct-CZ/CEITEC. Brno is the city of Johann Gregor Mendel, a founder of modern genetics and one of the first scientists who applied a multidisciplinary approach to explain his observations. The social programme of the meeting included a visit to the Mendel’s Museum and dinner at the Augustinian Abbey, where Mendel worked and lived.
Highlights of Coronavirus Structural Studies
Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved a-ketoamide inhibitors Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved a-ketoamide inhibitors
The coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome– coronavirus 2 (SARS-CoV-2) is a global health emergency. An attractive drug target among coronaviruses is the main protease (Mpro, also called 3CLpro) because of its essential role in processing the polyproteins that are translated from the viral RNA. Rolf Hingenfeld et. al. report in Science the x-ray structures of the unliganded SARS-CoV-2 Mpro and its complex with an a-ketoamide inhibitor. This was derived from a previously designed inhibitor but with the P3-P2 amide bond incorporated into a pyridone ring to enhance the half-life of the compound in plasma. On the basis of the unliganded structure, they developed the lead compound into a potent inhibitor of the SARS-CoV-2 Mpro. The pharmacokinetic characterization of the optimized inhibitor reveals a pronounced lung tropism and suitability for administration by the inhalative route.
Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein
The emergence of SARS-CoV-2 has resulted in >90,000 infections and >3,000 deaths. Coronavirus spike (S) glycoproteins promote entry into cells and are the main target of antibodies. We show that SARS-CoV-2 S uses ACE2 to enter cells and that the receptor-binding domains of SARS-CoV-2 S and SARS-CoV S bind with similar affinities to human ACE2, correlating with the efficient spread of SARS-CoV-2 among humans. We found that the SARS-CoV-2 S glycoprotein harbors a furin cleavage site at the boundary between the S1/S2 subunits, which is processed during biogenesis and sets this virus apart from SARS-CoV and SARS-related CoVs. In the study published in Cell, David Veesler with coworkers determined cryo-EM structures of the SARS-CoV-2 S ectodomain trimer, providing a blueprint for the design of vaccines and inhibitors of viral entry. Finally, they demonstrate that SARS-CoV S murine polyclonal antibodies potently inhibited SARS-CoV-2 S mediated entry into cells, indicating that cross-neutralizing antibodies targeting conserved S epitopes can be elicited upon vaccination.
Reader's Corner Archive
Visualization of biological macromolecules at near-atomic resolution: cryo-electron microscopy comes of age
The topical review by Alok K. Mitra recapitulates developments and transformational advances of cryo-EM technology.
The expanding toolkit for structural biology: synchrotrons, X-ray lasers and cryo-EM
Samar Hasnain et. al. describe the steadily-expanding methodologies for atomic resolution studies in The expanding toolkit for structural biology: synchrotrons, X-ray lasers and cryo-EM. Of note is the following statistics: Despite the wealth of structures in the Protein Data Bank, a closer examination reveals that 89% of the structures, i.e. 126 994, are of proteins or complexes with a molecular weight of less than 160 kDa. Furthermore, only 4% of the deposited structures have a molecular weight in excess of 300 kDa.