The scientists of the Brookhawed National Laboratory of the US Department of Energy published the first detailed model of the protein located on the surface of the Coronavirus shell and participating in cooperation with the key protein of human lung cells. The results of the study published in the Nature Communications journal helped to solve the reason why SARS-COV-2 is able to cause fatally dangerous damage to the respiratory and other organs.
To develop a molecular model, scientists used a cryoelectronic microscope in a biomolecular structure laboratory (LBMS). The cryoelectronic microscopy is suitable for the study of membrane proteins and dynamic protein complexes, of which it is difficult to obtain crystallons for crystallography, and also allows you to trace the dynamics of molecules.
Shell protein E is located on the outer surface of the virus and along with a spike protein helps the penetration of the virus into the cell and its further replication. It also plays a decisive role in the interception of human proteins to facilitate the release and transmission of the virus to other cells. It is assumed that it makes it through binding to PALS1 surface proteins, disturbing the dense adjoining of cells to each other.
Since contacts between lung cells are broken, immune cells are trying to correct damage, releaseing cytokines. This immune response can aggravate the situation, causing systemic inflammation, causing the so-called “cytokine storm” and the subsequent acute respiratory distress syndrome. The weakening of the intercellular ties allows the viruses easier to leave the lungs and penetrate the bloodstream to infect other organs, including liver, kidneys and blood vessels.