In a previous article we explained that the SARS-CoV-2 coronavirus, which causes COVID-19, owes part of its high infectivity to the peak protein, which allows it to adhere very well to human receptors, and infect cells. So researchers have been paying close attention to this feature, and even this has been the basis for the development of vaccine models.
Recently a team of experts from Lehigh University, the Seoul National University in South Korea and the University of Cambridge in the UK worked together to produce the first models of all the atoms that make up the peak protein (S protein) of full length.
A video has been published illustrating how the membrane system is constructed from SARS-CoV-2 protein S models through the CHARMM-GUI program, in File COVID-19, which simulates biomolecular systems complex simply, accurately and quickly.
Wonpil Im, a professor in Lehigh’s Department of Biological Sciences and Bioengineering, describes it as a “computational microscope” with which scientists can observe molecular interactions.
The researchers determined the structure of protein S with cryo-electron microscopy (cryo-EM), and also modeled the missing amino acid residues and then other missing domains.
The model also included all potential glycans (or carbohydrates) bound to protein S, which prevent antibody recognition, and therefore hinder the development of a vaccine.
“Our team spent days and nights carefully building these models from the known parts of the cryo-EM structure,” Im said. In addition, she stressed that this “modeling was very challenging because there were many regions where simple modeling could not provide high quality models.”
This is the first time that fully glycosylated SARS-CoV-2 spike protein models have been available to other scientists. From them, simulation research can be carried out to better understand the disease and develop preventive or therapeutic measures.