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On February 8, 2022, Science published online the collaboration between the team of Professor Huaqiang Xu/Dr.
Wanchao Yin of Shanghai Institute of Materia Medica, Chinese Academy of Sciences and the team of Dr.
Sujun Deng of Jimin Xinxin, entitled "Structures of the Omicron spike trimer with ACE2 and an anti -Omicron antibody" latest results
.
This study analyzed the high-resolution cryo-EM structure of the complex of Omicron spike protein and human receptor ACE2 or broad-spectrum anti-COVID-19 antibody JMB2002, explained the molecular mechanism of rapid spread and immune escape of Omicron mutants, and revealed the therapeutic antibody JMB2002 The new mechanism of action provides a theoretical basis for JMB2002 to still have the neutralizing function of the new coronavirus Omicron variant and to carry out further clinical trials
.
It provides new ideas for the research and development of broad-spectrum anti-new crown antibodies, and also provides a new reference for the development of global new crown vaccines
.
The researchers found that the Omicron spike protein binds its receptor ACE2 6-9 times more than the wild type.
), it was observed from the structure that there was an interaction between the adjacent RBDs of the Omicron spike protein trimer (Figure 1B).
Scientific experiments found that the RBD of the Omicron spike protein was highly flexible and unstable, and its thermal dissolution temperature dropped by more than 5 degrees Celsius (Fig.
1C), which made the spike protein easier to switch from the closed conformation to the open conformation, further enhancing the infection of the Omicron variant.
sex
.
In short, the interaction and instability of the Omicron spike protein RBD, which promotes the interaction of the Omicron spike protein with ACE2, explains the underlying mechanism of the enhanced infectivity of Omicron mutant strains at the atomic level
.
It can be seen from the resolved structure that many mutation sites of the Omicron spike protein are located on the surface of the protein, resulting in the loss of neutralizing activity of most neutralizing antibodies against Omicron mutant strains
.
Fortunately, the new crown neutralizing antibody JMB2002 independently developed by Jimin Trust has an affinity for Omicron spike protein 4 times that of the wild type, showing a strong potential to inhibit Omicron mutants
.
In order to clarify the molecular mechanism of JMB2002 against Omicron mutants, the researchers analyzed the structure of the Omicron spike protein complex with JMB2002 (Fig.
2A-C); from the structure, we found that there is also RBD interaction in the Omicron spike protein trimer (Fig.
2D), the binding of JMB2002 antibody to Omicron spike protein RBD blocked the binding of human receptor protein ACE2 to RBD (Fig.
2E); surprisingly, JMB2002 bound to RBD in a completely new conformation to bind to human ACE.
At the back of the interface, is a novel neutralizing antibody that binds epitope (Figure 2F)
.
Figure 2 Structure of the Omicron spike protein-binding antibody JMB2002
.
A shows the overall structure of JMB2002 antibody bound to Omicron spike protein, B shows the conformation of Omicron spike protein in complex, C shows the structure comparison of two RBDs bound to JMB2002 antibody, D shows the structure of JMB2002 antibody bound to Omicron spike protein The dimer of RBD-RBD, E shows that JMB2002 antibody binds to Omicron's RBD and blocks further binding of ACE2, F is the classification of anti-new coronavirus neutralizing antibody, and JMB2002 antibody is a new type of antibody, which is classified into the fifth category
.
At the time of the pandemic of the new coronavirus variant Omicron, the results of this research are extremely original and novel.
The paper has been peer-reviewed and published in Science, which will help global researchers to fully understand the characteristics of the Omicron variant.
The Omicron variant of the virus still has neutralizing function and provides a theoretical basis for further clinical trials
.
It provides new ideas for the research and development of broad-spectrum anti-new crown antibodies, and also provides a new reference for the development of global new crown vaccines
.
Wanchao Yin of Shanghai Institute of Materia Medica, Chinese Academy of Sciences and the team of Dr.
Sujun Deng of Jimin Xinxin, entitled "Structures of the Omicron spike trimer with ACE2 and an anti -Omicron antibody" latest results
.
This study analyzed the high-resolution cryo-EM structure of the complex of Omicron spike protein and human receptor ACE2 or broad-spectrum anti-COVID-19 antibody JMB2002, explained the molecular mechanism of rapid spread and immune escape of Omicron mutants, and revealed the therapeutic antibody JMB2002 The new mechanism of action provides a theoretical basis for JMB2002 to still have the neutralizing function of the new coronavirus Omicron variant and to carry out further clinical trials
.
It provides new ideas for the research and development of broad-spectrum anti-new crown antibodies, and also provides a new reference for the development of global new crown vaccines
.
The researchers found that the Omicron spike protein binds its receptor ACE2 6-9 times more than the wild type.
), it was observed from the structure that there was an interaction between the adjacent RBDs of the Omicron spike protein trimer (Figure 1B).
Scientific experiments found that the RBD of the Omicron spike protein was highly flexible and unstable, and its thermal dissolution temperature dropped by more than 5 degrees Celsius (Fig.
1C), which made the spike protein easier to switch from the closed conformation to the open conformation, further enhancing the infection of the Omicron variant.
sex
.
In short, the interaction and instability of the Omicron spike protein RBD, which promotes the interaction of the Omicron spike protein with ACE2, explains the underlying mechanism of the enhanced infectivity of Omicron mutant strains at the atomic level
.
It can be seen from the resolved structure that many mutation sites of the Omicron spike protein are located on the surface of the protein, resulting in the loss of neutralizing activity of most neutralizing antibodies against Omicron mutant strains
.
Fortunately, the new crown neutralizing antibody JMB2002 independently developed by Jimin Trust has an affinity for Omicron spike protein 4 times that of the wild type, showing a strong potential to inhibit Omicron mutants
.
In order to clarify the molecular mechanism of JMB2002 against Omicron mutants, the researchers analyzed the structure of the Omicron spike protein complex with JMB2002 (Fig.
2A-C); from the structure, we found that there is also RBD interaction in the Omicron spike protein trimer (Fig.
2D), the binding of JMB2002 antibody to Omicron spike protein RBD blocked the binding of human receptor protein ACE2 to RBD (Fig.
2E); surprisingly, JMB2002 bound to RBD in a completely new conformation to bind to human ACE.
At the back of the interface, is a novel neutralizing antibody that binds epitope (Figure 2F)
.
Figure 2 Structure of the Omicron spike protein-binding antibody JMB2002
.
A shows the overall structure of JMB2002 antibody bound to Omicron spike protein, B shows the conformation of Omicron spike protein in complex, C shows the structure comparison of two RBDs bound to JMB2002 antibody, D shows the structure of JMB2002 antibody bound to Omicron spike protein The dimer of RBD-RBD, E shows that JMB2002 antibody binds to Omicron's RBD and blocks further binding of ACE2, F is the classification of anti-new coronavirus neutralizing antibody, and JMB2002 antibody is a new type of antibody, which is classified into the fifth category
.
At the time of the pandemic of the new coronavirus variant Omicron, the results of this research are extremely original and novel.
The paper has been peer-reviewed and published in Science, which will help global researchers to fully understand the characteristics of the Omicron variant.
The Omicron variant of the virus still has neutralizing function and provides a theoretical basis for further clinical trials
.
It provides new ideas for the research and development of broad-spectrum anti-new crown antibodies, and also provides a new reference for the development of global new crown vaccines
.
