Structure of SARS-CoV-19 key protein mappedDate: 23 February 2020 Tags: Miscellaneous
Researchers at the University of Texas at Austin and the National Institutes of Health, U.S., have produced a 3D atomic scale map of the protein of the novel coronavirus (SARS-CoV-2) that binds to and infects human cells.
Mapping the 3D structure of the protein, spike (S) glycoprotein, will allow better understanding of how the virus binds to the human cells. Knowing the structure of the spike protein will, in turn, allow scientists to develop vaccines and antivirals against the virus and even better diagnostics.
Like other coronaviruses, SARS-CoV-2 virus particles are spherical and have mushroom-shaped proteins called spikes protruding from their surface, giving the particles a crown-like appearance. The spike binds and fuses to human cells, allowing the virus to gain entry.
The spike protein of the novel coronovirus shares 98% sequence identity with the spike protein of the bat coronavirus.
The researchers also found that like in the case of the SARS coronavirus, the spike protein of the novel coronavirus (SARS-CoV-2) that causes COVID-19 disease binds to the cellular receptor called angiotensin-converting enzyme 2 (ACE2), which serves as the entry point into human cells.
But unlike in the case of SARS, the spike protein of the novel coronavirus binds to the cell receptor with much higher affinity, 10- to 20-fold higher.
The much greater binding affinity to the cell receptor explains the apparent high human-to-human transmissibility of the virus compared with the SARS coronavirus.
The researchers tested three monoclonal antibodies specific to SARS virus for their ability to bind to the novel coronavirus. But none of the three antibodies tested were found to be effective in inhibiting the novel coronavirus from binding to the human receptor.
Knowing the atomic-level structure of the 2019-nCoV spike will allow for additional protein engineering efforts that could improve antigenicity and protein expression for vaccine development.