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Structure of Alphac...
Structure of Alphacoronavirus Transmissible Gastroenteritis Virus nsp1 Has Implications for Coronavirus nsp1 Function and Evolution
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- Jansson, Anna M., 1979- (author)
- Uppsala universitet,Struktur- och molekylärbiologi,T. Alwyn Jones
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(creator_code:org_t)
- American Society for Microbiology, 2013
- 2013
- English.
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In: Journal of Virology. - : American Society for Microbiology. - 0022-538X .- 1098-5514. ; 87:5, s. 2949-2955
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi -- Strukturbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Structural Biology (hsv//eng)
Keyword
- Coronavirus
- Alphacoronavirus
- nsp1
- Molecular Biology
- Molekylärbiologi
Publication and Content Type
- ref (subject category)
- art (subject category)
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