The first release of the Chinese Academy of Sciences Xu Huaqiang/Yin Wanchao team to jointly tackle the new coronavirus Omicron mutant strain spike protein and its complex structure with receptors and antiviral antibodies

It has been 2 years since the outbreak of the new crown epidemic.
The number of confirmed cases worldwide has exceeded 280 million, and the death toll has exceeded 5.
4 million
.

What is more worrying is that the new coronavirus has evolved a variety of "worrying mutant strains", which continue to bring uncertainty and new challenges to the global epidemic prevention and control, especially the latest Omicron mutant strains, The global raging has caused a new round of infection peaks

The number of mutation sites of the new coronavirus Omicron mutant strain is significantly more than that of all new coronavirus mutants that have been circulating in the past two years, especially in the virus spike protein mutations as many as 37
.

At present, it is not clear how these mutations affect the infectivity of Omicron mutant strains and the mechanism that leads to immune escape

Figure 1 The structure of the Omicron mutant new coronavirus spike protein binding receptor ACE2
.

A shows the structure and conformation, B is the interaction interface of RBD and ACE2, and C is the interaction interface of RBD dimer

The team of Xu Huaqiang and Yin Wanchao of Shanghai Institute of Materia Medica, Chinese Academy of Sciences urgently tackled the problem and quickly resolved the Omicron mutant spike protein and the high-resolution cryo-EM structure that binds to the human receptor ACE2 in less than one month (Figures 1A and 1B)
.

The biochemical level binding showed that the receptor-binding domain (RBD) of the Omicron mutant strain’s receptor-binding domain (RBD) binding to the receptor ACE2 was significantly enhanced compared to the wild-type, which was probably increased by nearly 10 times; thermodynamic experiments showed that, The RBD of the Omicron mutant strain is highly flexible and unstable, which makes it easier for the spike protein to switch from a closed conformation to an open conformation.

Figure 2 The structure of the Omicron mutant new coronavirus spike protein binding antibody JMB2002
.

A shows the binding of JMB2002 antibody fragment to the Omicron mutant and wild-type new coronavirus spike protein, B shows the inhibition of the JMB2002 antibody on the Omicron mutant and wild-type, respectively, and C is the Omicron mutant new coronavirus spike protein binding antibody JMB2002 Structure, D is the structural comparison of RBD binding to JMB2002 antibody fragment, E is the classification of neutralizing antibodies against the new coronavirus, and JMB2002 antibody is a new type of antibody and is classified as the fifth category