Scientists have succeeded in implementing the antibody’CV30′ protein, which shows strong resistance to coronavirus, in 3D images. Through this, it is expected that research on the mechanism of antibodies against coronavirus will become more active.
Scientists in the United States have succeeded in visualizing the structure of an antibody with strong resistance to coronavirus in 3D images.
Scientists at the Fred Hutchinson Cancer Research Center in Seattle have isolated antibodies from Coronavirus Infectious Disease-19 (Corona 19) survivors to coronavirus spike protein (a bump structure arranged on the surface of the virus, which binds to protein receptors on cell membranes). It was discovered that it interferes with the main function of human cells) and induces the separation of spike proteins.
The antibody is a Y-shaped protein, and the research team has succeeded in isolating the antibody from blood samples in Washington patients in the early stages of the COVID-19 outbreak. Leading researchers are ▲Leo Stamatos ▲Andrew Maguire ▲Dr.Marie Pansera.Among the dozens of antibodies naturally generated by past patients, the antibody named’CV30′ has 530 times stronger resistance. Was announced.
Structural biologists Dr. Pansera and Dr. Nicholas Hulbert visualized the molecular structure of’CV30′ using equipment used in high-energy physics (a research field that utilizes small particles artificially created through particle accelerators). This result was published on the 27th (local time), an online academic journal <네이처 커뮤니케이션즈>Was published on.
The molecular structure of CV30, implemented as a 3D image through a computer, may look like a lump of noodles to the public eye. However, in the eyes of scientists, this’noodle mass’ is a model that accurately shows the surface structure of antibodies, the spike protein of the coronavirus, and the binding site between the human cell and the spike protein. This model shows how the advanced structures work together like 3D puzzle pieces.
“The research shows that the antibody (CV30) weakens the virus through two mechanisms,” said Pansera. “The antibody overlaps the viral target in human cells, and induces the viral spike protein to separate or separate from human cells. “
At the end of the complex antibody surface, there is a drooping Y-shaped arm, and this very small but large amount of molecular fragments prevents the coronavirus’ spike protein from attaching to human cells like hooks. Coronavirus spikes try to bind to the ACE2 receptor, a protein found on the surface of cells that make up human lung tissue and blood vessels, but if the CV30 antibody intervenes, attempts to bind the virus become difficult.
The antibody separates some of the proteins in the spike known as’S1′. In experiments, Dr. Maguire and his team demonstrated that antibody binding decreased over time in the presence of antibodies. This proves that the S1 protein came off the spike surface.
For reference, the S1 protein plays a crucial role in the penetration of coronavirus into cells. After Spike first binds to the ACE2 receptor, the S1 protein fuses the surface of the human cell caught by the virus, helping the virus to invade the cell. Once the virus invades, it infects genes and protein components in the cell. This is a process for its own replication, and then the copied virus attacks other human cells.
Because the antibody size is so small, it is not easy to know completely what it does. When viewed under a high-magnification microscope (CV30), the protein will appear to be crowded around the virus like a mosquito. However, structural biologists have reached a stage where they can create accurate 3D images of the CV30 protein to show how antibodies work and how the structure of the antibody interacts.
The ability to visualize the nano-sized CV30 protein in 3D is thanks to the use of X-ray crystallography (which is used to reveal the atomic and molecular structures of the crystal by using diffraction of X-rays incident into the crystal). Structural biologists were able to visualize the shape of the protein by freezing the CV30 protein molecule and irradiating strong X-rays.
※ Source: Post of the Korean Association of Science Journalists