Major achievements of Science: analyze the structure of S protein of new coronavirus and assist in vaccine research and development

Author: as Wang zhaoyue said, "know yourself and know your enemy, and you will never lose a hundred battles." Novel coronavirus pneumonia spread in China and the world has aroused widespread concern, so the study of SARS-CoV-2 virus control of the epidemic is imminent Doi: 10.1126/science.abb2507 on February 19, science published the high-definition structure of S-protein trimer on the surface of sars-cov-2 virus online, which greatly promoted scientists around the world to develop vaccines and antiviral drugs The study was conducted by researchers at the University of Texas at Austin and NIH, the National Institutes of health 3-D structure of S-protein trimer on the surface of sars-cov-2: Jason McLellan / Univ of Texas at Austin has successfully constructed the first 3-D atom level map of S-protein trimer on the surface of sars-cov-2 by using the latest cryo-EM technology, with a resolution of 3.5 angstroms (1 angstrom = 0.1nm) By analyzing the 3D structure, it is found that when the receptor binding domain (RBD) moves up, S protein can bind to the receptor on the cell surface through RBD; when it moves down, the receptor binding site will be hidden That is, to combine up and hide down The S-protein with receptor binding domain extending down (left) and up (right) is the weapon for the new coronavirus sars-cov-2 to invade human cells, which is the key part for the virus to attach and infect human cells It is a large number of glycosylated trimer protein It first binds to the receptor on the cell surface, and then "deforms" to integrate the virus envelope and cell membrane, so as to inject the genetic material in the virus into the cell and achieve the purpose of infecting the cell The high-resolution map of the protein is conducive to the targeted research of vaccines and drugs Recently, many studies have pointed out that the receptor recognized by sars-cov-2 may be ACE2 like SARS virus To assess this possibility, the researchers tested the ability of the two viruses to bind to ACE2 The results showed that the affinity of S protein domain of sars-cov-2 to ACE2 was stronger, which was 10-20 times higher than that of SARS virus It is speculated that this high affinity may be the reason why sars-cov-2 virus is more likely to pass from person to person, but this speculation needs more research to verify the possibility The molecular structure of S protein obtained by the high affinity between new coronavirus and ACE2 belongs to the extracellular part of sars-cov-2 virus Because it can trigger immune response in human body, it can be used to study vaccine In addition, the team will use s protein as a "probe" to separate antibodies from patients who have been infected with sars-cov-2 virus and successfully recovered, so as to achieve effective treatment of coronavirus infection Reference materials: [1] cryo EM structure of the 2019 ncov spike in the fusion conformation [2] science today: scientists reveal the high-definition structure of the new coronavirus s protein, which is expected to help the development of vaccines and diagnosis and treatment technology [3] science releases the breakthrough results of coronavirus research: key proteins are resolved, which is expected to support the vaccine design