Coronary virus structure seds on the evolution of SARS-CoV-2.

In a paper published in nature structure and molecular biology, sars-cov-2 and bat ratg13 spike glycoprotein structures information on virus evolution and furin cleavage effects characterized the spike glycoprotein structure of sars-cov-2 and bat ratg13, which enables the virus to combine with cells and enter cells.this structure provides information for further understanding the evolution process of sars-cov-2 spike, which may be useful for vaccine design.the researchers believe that bat coronavirus may be an evolutionary precursor of sars-cov-2. Previous studies have found that the genetic relationship between bat virus ratg13 and sars-cov-2 is the closest known.however, it is not clear how sars-cov-2 evolved to infect humans, and whether it was transmitted directly to humans through an intermediate host.Antoni Wrobel, Donald Benton and colleagues at the Francis Crick Institute in the UK compared the spike glycoproteins of sars-cov-2 and ratg13.they found that although the structure of sars-cov-2 was similar, the form of spike glycoprotein of sars-cov-2 was more stable, and its affinity with ACE2 was about 1000 times higher.the authors also found that the flint cleavage site on the spike of sars-cov-2 may be beneficial to the virus because it may promote the binding of the virus to cellular receptors.based on these observations, the authors believe that bat viruses similar to ratg13 are unlikely to infect human cells, which also supports the theory that sars-cov-2 evolved after recombination of different coronavirus genomes. The authors pointed out that their sars-cov-2 spike glycoprotein had high resolution, nearly complete structure and more outer loop than previously reported structure, which may be of great significance for vaccine design.@NatureNSMB| doi: 10.1038/s41594-020-0468-7