Publications
2020
Miao Z, Tidu A, Eriani G, Martin F
Secondary structure of the SARS-CoV-2 5'-UTR Article de journal
Dans: RNA Biol, vol. 18, no. 4, p. 447-456, 2020, ISBN: 32965173.
Résumé | Liens | BibTeX | Étiquettes: 5ʹ-UTR SARS-CoV-2 probing secondary structure, ERIANI, Unité ARN
@article{,
title = {Secondary structure of the SARS-CoV-2 5'-UTR},
author = {Z Miao and A Tidu and G Eriani and F Martin},
url = {https://pubmed.ncbi.nlm.nih.gov/32965173/},
doi = {10.1080/15476286.2020.1814556},
isbn = {32965173},
year = {2020},
date = {2020-01-01},
journal = {RNA Biol},
volume = {18},
number = {4},
pages = {447-456},
abstract = {The SARS-CoV-2, a positive-sense single-stranded RNA Coronavirus, is a global threat to human health. Thus, understanding its life cycle mechanistically would be important to facilitate the design of antiviral drugs. A key aspect of viral progression is the synthesis of viral proteins by the ribosome of the human host. In Coronaviruses, this process is regulated by the viral 5' and 3' untranslated regions (UTRs), but the precise regulatory mechanism has not yet been well understood. In particular, the 5'-UTR of the viral genome is most likely involved in translation initiation of viral proteins. Here, we performed inline probing and RNase V1 probing to establish a model of the secondary structure of SARS-CoV-2 5'-UTR. We found that the 5'-UTR contains stable structures including a very stable four-way junction close to the AUG start codon. Sequence alignment analysis of SARS-CoV-2 variants 5'-UTRs revealed a highly conserved structure with few co-variations that confirmed our secondary structure model based on probing experiments.},
keywords = {5ʹ-UTR SARS-CoV-2 probing secondary structure, ERIANI, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
The SARS-CoV-2, a positive-sense single-stranded RNA Coronavirus, is a global threat to human health. Thus, understanding its life cycle mechanistically would be important to facilitate the design of antiviral drugs. A key aspect of viral progression is the synthesis of viral proteins by the ribosome of the human host. In Coronaviruses, this process is regulated by the viral 5' and 3' untranslated regions (UTRs), but the precise regulatory mechanism has not yet been well understood. In particular, the 5'-UTR of the viral genome is most likely involved in translation initiation of viral proteins. Here, we performed inline probing and RNase V1 probing to establish a model of the secondary structure of SARS-CoV-2 5'-UTR. We found that the 5'-UTR contains stable structures including a very stable four-way junction close to the AUG start codon. Sequence alignment analysis of SARS-CoV-2 variants 5'-UTRs revealed a highly conserved structure with few co-variations that confirmed our secondary structure model based on probing experiments.