We do not yet know exactly how to combat or prevent it, but we do know many details about the SARS-CoV-2 coronavirus and how it rapidly proliferates in the cells of the infected person.
As we have already explained on other occasions, SARS-CoV-2 (like the first cousin virus SARS-CoV-1) have a high affinity with enzymes that our cells have, so that some proteins on their surface, called proteins Yes, they do match the angiotensin converting enzyme (ACE2 receptor), almost like a key would in a lock.
Today we know that this perfected structure was mutating by natural selection, until it gave rise to a very effective coronavirus when infecting, but not perfect.
Once inside the cell, the virus unfolds its genetic material (RNA) and ‘forces’ our infected cells to make infinite copies of itself. Now, how do you get it?
To achieve this, the virus has to multiply its genetic material which, as we mentioned, consists of a single long chain of RNA. And it does so thanks to the polymerase enzyme that is capable of transcribing or replicating nucleic acids (the pieces that make up RNA or DNA). The polymerase enzyme can, so to speak, ‘copy-paste’ the genetic information of the virus.
Disassembling the polymerase enzyme
The Max Plank Institute for Biophysical Chemistry in Göttingen, Germany, has succeeded in determining the three-dimensional structure of the coronavirus polymerase enzyme. This detailed information on the appearance of this enzyme makes it possible to investigate how antiviral drugs that are being tested against the coronavirus work, such as remdesivir, which blocks polymerase; and, of course, looking for new inhibitory substances that can serve as therapy.
If this enzyme is blocked by a drug, the coronavirus will no longer be able to make copies of itself, and the infection will stop.
The enzyme polymerase has an extra help
The coronavirus polymerase enzyme binds to RNA in the same way as it does to other known virus types. So what’s so special about it?
This polymerase is accompanied by an additional element, with which it binds to the RNA until it has copied all the genetic material , which is very long and, therefore, the task is expensive. This element helps polymerase to accomplish the arduous task of copying the coronavirus. This is how they explain it in a statement from the Max Plank Institute: “The coronavirus genome consists of around 30,000 building blocks and is therefore particularly long, so copying is a major challenge.”
“We were surprised to find that the structure of the coronavirus polymerase enzyme is special: it differs from other structures that we have been investigating so far,” explains Hauke Hillen, one of the principal investigators.
According to the director of the Max Planck Institute, Patrick Cramer, the objective of the study of the structure of the enzyme polymerase is, mainly, to delve into the discovery of new treatment drugs: “Many hopes rest on remdesivir, which directly blocks polymerase, but It might be possible to optimize existing substances like remdesivir and improve their effect. We also want to look for new substances that can stop the virus polymerase enzyme. “
