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Publication Abstract from PubMed

Coronavirus nsp1 have been shown to induce suppression of host mRNA expression and to interfere with host immune response. However, the mechanism is currently unknown. The only available structural information on coronavirus nsp1 is the NMR structure of the N-terminal domain of nsp1 from severe acute respiratory syndrom coronavirus (SARS-CoV) from the genus betacoronavirus. Here we present the first nsp1 structure from an alphacoronavirus, TGEV nsp1. It displays a six-stranded beta-barrel fold with a long alpha helix on the rim of the barrel, a fold shared with SARS-CoV nsp1(13-128). 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 mRNA expression might be different in these two genera.

Structure of alphacoronavirus TGEV nsp1 has implications for coronavirus nsp1 function and evolution.,Jansson AM J Virol. 2012 Dec 26. PMID:23269811^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.