Résumé de l'article

During the early stages of infection, the NSP1 protein is one of the first viral proteins produced. This NSP1 protein will immediately bind to the ribosome of the host cell and block the entry site to prevent access of the cell's messenger RNAs, which will then no longer be translated. In this way, the virus takes control of the cell's translational machinery and literally turns off cellular translation. However, the virus genome continues to be translated despite the presence of NSP1 on the ribosome. The experiments carried out made it possible to understand how the virus can bypass this blockage by the NSP1 protein. The virus has a small hairpin structure called SL1 in its messenger RNAs that allows it to open up access to the ribosome by acting on NSP1. The virus has a sort of key that allows it to continue translating by unlocking the ribosome blocked by the viral protein NSP1 during infection. This discovery is extremely important as it opens the way to new antiviral therapeutic approaches aimed at blocking the virus' cell cycle. Indeed, the primordial role of SL1 in the infection process makes this element of the virus a prime target for the development of new inhibiting molecules. Such molecules would be capable of specifically blocking the action of SL1, thus enabling the virus to be turned off. In short, the fact that SL1 is essential for viral translation suggests that this structure is a real 'Achilles heel' of the virus.