The new coronavirus SARS-CoV-2 caused Coronavirus Disease (COVID-19) in 2019 and is currently rampant worldwide. Scientists are working overtime to develop vaccines and drugs to defeat SARS-CoV-2. Much work is focused on the coronavirus spike protein (S protein), which interacts with angiotensin converting enzyme 2 (ACE2) on the surface of human cells. Combine and allow the virus to invade the cell.
At present, in a new study, researchers from the University of California, San Diego, the University of Texas at Austin, and the University of Maynooth in Ireland have discovered that glycans (glycans), as a type of sugar molecules that modify S protein, are here Play a positive role in the process. It may provide new targets for the development of vaccines and drugs. Before the S protein of SARS-CoV-2 interacts with ACE2 on the surface of human cells, the S protein changes its shape to form a receptor binding domain (RBD), which is a protein that interacts with ACE2. Exposed. section. Like many viral proteins, the S protein is covered by a thick layer of glycans. These glycans attached to specific locations help protect the viral protein from the host's immune system. In this new study, these researchers want to know whether certain glycans of the SARS-CoV-2S protein may also play an active role in the process of this virus infection. In order to find
Answer, these researchers used structure and sugar mixture data to establish a molecular dynamics model of the SARS-CoV-2S protein embedded in the viral membrane. These computer models show detailed snapshots of each atom of the S protein, revealing that the N-glycans bound to the protein at specific locations (N165 and N234) in the S protein help stabilize RBD exposure. I did it. It changes shape and promotes infection. These models also identified regions of S protein that were not encapsulated by glycans, which were vulnerable to antibody attack, especially after shape changes. In laboratory experiments using the interference of reflected light from the biofilm layer, it was found that the mutations at the N165 and N234 positions of the S protein no longer carry glycans. This can reduce the binding of S protein to ACE2. These researchers say these findings lay the foundation for the development of new strategies against the threat of this epidemic.