Nature: SARS-CoV-2 RBD antibody has maximum anti-virus escape ability 

At present, the most effective neutralizing antibodies against SARS-CoV-2-including those used in clinical practice and antibodies that dominate in polyclonal serum-are directed against the receptor binding domain (RBD) of the spike protein Antibody
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With the spread of the new crown, RBD mutations that resist antibody binding have appeared in variants of SARS-CoV-2, which highlights the need to develop and design antibodies and vaccines that have the ability to fight the virus

In existing studies, people have described an antibody, S3094, which exhibits powerful effector functions and can neutralize all current SARS-CoV-2 variants and SARS-CoV-1 of the sarbecovirus branch
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S309 forms the basis of an antibody therapy (VIR-7831, recently renamed sotrovimab) that has received emergency use authorization from the FDA for the treatment of COVID-19

In the long run, an ideal anti-SARS-CoV-2 antibody should have the ability to resist virus escape and be active against different SARS-related coronaviruses (sarbecoviruses) , which can be demonstrated through virus neutralization and effector functions A high degree of protection
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A systematic understanding of the relationships between these properties and the differences between different epitopes will help develop antibody therapies and guide vaccine design

Antibody epitope, potency, breadth and escape

Although antibodies targeting the ACE2 receptor binding domain (RBM) have a high neutralizing effect, they usually have a poor breadth and are easily escaped by the mutant virus
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In this study, the researchers described an effective RBM antibody (S2E128), which has a good breadth in sarbecoviruses related to SARS-CoV-2 and has a high resistance to virus escape

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Tyler N.