Structure of Alphacoronavirus Transmissible Gastroenteritis Virus nsp1 Has Implications for Coronavirus nsp1 Function and Evolution
2013 (English)In: Journal of Virology, ISSN 0022-538X, E-ISSN 1098-5514, Vol. 87, no 5, 2949-2955 p.Article in journal (Refereed) Published
Coronavirus nsp1 has been shown to induce suppression of host gene expression and to interfere with the host immune re- sponse. However, the mechanism is currently unknown. The only available structural information on coronavirus nsp1 is the nuclear magnetic resonance (NMR) structure of the N-terminal domain of nsp1 from severe acute respiratory syndrome corona- virus (SARS-CoV) from the betacoronavirus genus. Here we present the first nsp1 structure from an alphacoronavirus, transmis- sible gastroenteritis virus (TGEV) nsp1. It displays a six-stranded -barrel fold with a long alpha helix on the rim of the barrel, a fold shared with SARS-CoV nsp113–128. Contrary to previous speculation, the TGEV nsp1 structure suggests that coronavirus nsp1s have a common origin, despite the lack of sequence homology. However, comparisons of surface electrostatics, shape, and amino acid conservation between the alpha- and betacoronaviruses lead us to speculate that the mechanism for nsp1-induced suppression of host gene expression might be different in these two genera.
Place, publisher, year, edition, pages
American Society for Microbiology , 2013. Vol. 87, no 5, 2949-2955 p.
Coronavirus, Alphacoronavirus, nsp1
Research subject Molecular Biology
IdentifiersURN: urn:nbn:se:uu:diva-196611DOI: 10.1128/JVI.03163-12ISI: 000314876900051OAI: oai:DiVA.org:uu-196611DiVA: diva2:610499