Health
A model of SARS-CoV-2 dynamics reveals an opportunity to prevent COVID-19 infection-ScienceDaily
Scientists have simulated the transition of the SARS-CoV-2 peplomer structure from the time it recognizes the host cell to the time it invades. eLife..
Studies show that the structure enabled by the sugar molecule on the peplomer may be essential for cell invasion, and disrupting this structure may be a strategy to stop viral infection. ..
An essential aspect of the SARS-CoV-2 life cycle is its ability to attach to host cells and transfer their genetic material. This is achieved by a transmembrane bundle that anchors the spike to the virus and a peplomer protein that consists of three separate components, two S subunits (S1 and S2) that are external to the virus. To infect human cells, the S1 subunit binds to a molecule on the surface of the human cell called ACE2, which separates and fuses the virus with the human cell membrane. This process is known, but the exact order in which it occurs has not yet been discovered. Nevertheless, understanding the microsecond-scale and atomic-level movements of these protein structures can reveal potential targets for COVID-19 treatment.
“Most current SARS-CoV-2 treatments and vaccines focus on the ACE2 recognition step of viral entry, but alternative strategies target structural changes that allow the virus to fuse with human host cells. It is to do it, “explains in collaboration with the research. -Author José N. Onuchic, Professor of Physics at Rice University (Houston, USA), and Co-Director of Theoretical Biophysics Center. “But it is very difficult to ly investigate these intermediate subunits, so we used a sufficiently simplified computer simulation to investigate this large system, but before and after fusion. Maintains sufficient physical detail to capture the dynamics of the S2 subunit transitioning between-a form of fusion. “
The team was particularly interested in the role of sugar molecules on spike proteins called glycans. Numbers using an all-atom structure-based model to determine whether glycan numbers, types, and positions play a role in the membrane fusion stage of viral cell invasion by mediating these intermediate spike formations. We ran a thousand simulations. Using such a model, you can predict the orbital of an atom over time, taking into account the three-dimensional force, that is, how adjacent atoms affect the movement of other atoms.
Simulations reveal that glycans form a “cage” that traps the “head” of the S2 subunit and pauses in the middle between separation from the S1 subunit and fusion of the viral and cell membranes. became. In the absence of glycans, the S2 subunit spends much less time in this conformation.
The simulation also mobilizes human host cells to fuse with their membranes by holding the S2 head in a specific position, allowing the elongation of short proteins called fusion peptides from the virus. Suggests to help you. In fact, glycosylation of S2 greatly increased the likelihood that the fusion peptide would reach the host cell membrane, but in the absence of glycans, this was very unlikely to occur.
“Our simulations show that glycans can cause pauses during the migration of peplomers, which provides an important opportunity for fusion peptides to capture host cells.” Concludes Paul C. Whitford, an associate professor at the Center for Theoretical Biophysics. Northeastern University, Boston, Faculty of Physics, USA. “In the absence of glycans, viral particles may not be able to invade the host. Our research reveals how sugars control infectivity and influences the dynamics of this prevailing deadly pathogen. Provides a basis for research. “
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