A “hairpin” structure controls the translation of the SARS-CoV-2 virus genome.
A team from the RNA Laboratory led by Franck Martin has demonstrated the importance of structure in the translation of the SARS-CoV-2 virus genome. Details of this breakthrough can be found in
the CNRS INSB newsletters.
Figure: During infection with CoV-2-SARS, the first viral protein produced is the NSP1 protein. This protein binds to the ribosome of the infected cell and blocks the entry of the messenger RNA channel. It is in this way that the NSP1 protein switches off the host cell’s translation during the early stages of the infection. However, viral translation is not impacted by the presence of the molecular lock that is NSP1. To escape the NSP1 blockade, the virus’ messenger RNAs possess a molecular key that allows access to the ribosome by moving the NSP1. This key is a looped rod structure called SL1 which is present in all messenger RNAs.
The viral protein NSP1 acts as a ribosome gatekeeper for shutting down host translation and fostering SARS-CoV-2 translation. Tidu A, Janvier A, Schaeffer L, Sosnowski P, Kuhn L, Hammann P, Westhof E, Eriani G, Martin F.RNA. 2020 Dec 2:rna.078121.120.
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