Structure of Alphacoronavirus Transmissible Gastroenteritis Virus nsp1 Has Implications for Coronavirus nsp1 Function and Evolution

• 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. 

Ämnesord

NATURVETENSKAP  -- Biologi -- Strukturbiologi (hsv//swe)

NATURAL SCIENCES  -- Biological Sciences -- Structural Biology (hsv//eng)

Nyckelord

Coronavirus

Alphacoronavirus

nsp1

Molecular Biology

Molekylärbiologi

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