SARS-CoV-2 5′-UTR stem-loops activate the antiviral protein oligoadenylate synthetase 1 (OAS1)
Alejandro Oviedo, Camden R. Bair, Alexander P. Vasilakopoulos, Kierra Regis, David Vanlnsberghe, Anice C. Lowen, Graeme L. Conn · 2026
Read SARS-CoV-2 5′-UTR stem-loops activate the antiviral protein oligoadenylate synthetase 1 (OAS1) by Alejandro Oviedo, Camden R. Bair, Alexander P. Vasilakopoulos, Kierra Regis, David Vanlnsberghe, Anice C. Lowen, Graeme L. Conn (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13315676.txt.
Description
Alejandro Oviedo and colleagues show, in a 2026 study, how a structured region of the SARS-CoV-2 genome trips a key antiviral sensor. The OAS1 protein detects viral double-stranded RNA and switches on the RNase L pathway, and one spliced form, OAS1-p46, has been tied to milder COVID-19. Anchored to intracellular membranes, it may meet viral RNA at the genome's 5-prime untranslated region. The team tested whether the structured elements there activate OAS proteins.
They could. Through truncations, the team found the smallest fragment that potently activates OAS1: the SL1-4b region, holding the first four stem-loops plus an unstructured tail after SL4. Structure probing suggested SL4 is the contact site, while the SL4b tail and stem-loops SL1 and SL3 present it optimally. The authors present the region as a structurally complex trigger, underscoring how varied the RNAs that strongly activate this sensor can be.
Catalog record
| CREATOR | Alejandro Oviedo, Camden R. Bair, Alexander P. Vasilakopoulos, Kierra Regis, David Vanlnsberghe, Anice C. Lowen, Graeme L. Conn |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 50 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |