Cell: The spatial structure of SARS-CoV-2 virus neutralizing antibodies
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Cell: Progress in the study of the spatial structure of SARS-CoV-2 virus neutralizing antibodies
Cell: The spatial structure of SARS-CoV-2 virus neutralizing antibodies. The SARS-CoV-2 infection is caused by the binding of the COVID-19 virus spike protein to the host receptor angiotensin-converting enzyme 2 (ACE2), followed by the fusion of the viral membrane with the host membrane.
Although antibodies that block this interaction are urgently used as early COVID-19 treatments, the exact determinants of neutralizing efficacy are still unknown.
The Charles S. Craik research team of the University of California in the United States has discovered a series of antibodies through research. These antibodies have similar high binding power to the spike protein of the virus and can effectively block the binding of ACE2. The neutralizing effect is different.
It is worth noting that these neutralizing antibodies can inhibit or enhance the membrane fusion and syncytial formation mediated by spike protein, which is related to chronic tissue damage in COVID-19 patients.
The various cryo-electron microscopy structures of the Spike antibody complex reveal different binding modes, which not only block ACE2 binding, but also change the conformational cycle of Spike protein triggered by ACE2 binding. Spike: 3D11 complex is relatively homogeneous, with only one state. All three RBDs bind to 3D11-Fab in an open conformation, the Fab is at right angles to the long axis of the RBD, and the epitope is only exposed to the cell in the open state and outside the RBM.
Studies have found that stable and different spike protein conformations can regulate the membrane fusion mediated by the spike protein, which is of great significance in the pathology and immunity of the COVID-19 virus
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