In the new study, published in the PNAS journal, researchers have been able to understand why the virus is associated with the "sick" version of the receptor. They used a cryogenic electron microscope to see the link between the virus and the receptor at a resolution of only a few atoms. The researchers compared the molecular structure of the two receptors to understand which part of the ANTXR1 receptor allows it to bind specifically to the virus. After taking about 7,000 pictures, the researchers discovered the critical amino acids that link the receptor to the virus, which differentiates between the two receptors.
Another possibility is suppression of the immune system when treating such a virus to prevent it from attacking it. However, such treatment may harm the ability to attack cancer with the help of the immune system itself, as is currently done practiced in immunotherapy or cancer vaccines, which are aided by the natural ability of the immune system to identify tumors and destroy them. Faced with all these challenges, researchers need to combine creativity and discretion to develop the next drug that will eliminate cancer.
Jayawardena, N., Burga, L. N., Easingwood, R. A., Takizawa, Y., Wolf, M., & Bostina, M. (2018). Structural basis for anthrax toxin receptor 1 recognition by Seneca Valley Virus. Proceedings of the National Academy of Sciences, 115