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| 2022-02-09 17:23:17 | onclick： | Shanghai scientists solve the mystery of Omicron's increased appeal |
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Why is the infection of COVID-19's mutation significantly enhanced? Recently, Shanghai scientists jointly analyzed the spike protein of Omicron mutant and its complex structure with receptor and antiviral antibody, and solved the mystery of its enhanced infectivity from the microscopic perspective of atomic level. Relevant papers were published online in the international famous academic journal Science last night.
According to the latest data released by the World Health Organization, there are nearly 400 million newly diagnosed cases worldwide. The emergence of COVID-19's variant has triggered a new round of infection worldwide. Preliminary studies showed that the number of mutation sites of the mutant was significantly higher than that of all COVID-19 mutants that had been prevalent in recent two years, with only 37 mutations in the spike protein.
In December last year, the super-resolution ace receptor structure of Zhongrong and aoqiang strain of Shanghai Institute of cryomedicine were rapidly analyzed by the super-resolution electron microscope. Biochemical level binding experiment showed that the receptor binding region of spike protein of Omicron mutant was significantly enhanced compared with the wild type, and the binding receptor ACE2 was about 10 times higher; Thermokinetic experiments showed that the RBD of Omicron mutant was highly flexible and unstable, which made the spike protein easier to convert from closed conformation to open conformation.
At the same time, scientists observed the specific interaction between adjacent RBDS in the spike protein trimer of Omicron mutant from the analytical structure, which can stabilize the spike protein specific RBD of Omicron mutant in an open state. These studies explain the potential mechanism of the enhanced infectivity of Omicron mutant at the atomic level. At the same time, the analyzed structure shows that most of the mutation sites of spike protein of Omicron mutant are located on the protein surface, including multiple antigen epitopes, which explains the molecular mechanism that Omicron mutant can resist most neutralizing antibodies.
On the basis of this work, Xu Huaqiang and Yin Wanchao team, together with the research team of pharmaceutical enterprises, further analyzed the structure of spike protein of Omicron mutant and specific therapeutic antibody jmb2002. Biochemical level binding experiment showed that the binding force of the antibody to the spike protein of Omicron mutant was four times that of the wild type, showing the strong potential to inhibit Omicron mutant.
From the complex structure obtained by analysis, researchers found that jmb2002 antibody fragment binds to the back of RBD receptor binding motif with a new conformation, which is a neutralizing antibody with a new mechanism of action. At present, the antibody has completed phase I clinical trial, which has strong therapeutic effect and high safety. Combined with biochemical and antiviral neutralization experiments, the researchers elaborated the molecular mechanism of antibody JMB2002 with broad-spectrum anti COVID-19.
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