Zhou Shen

TL;DR: It is demonstrated that alphacoronavirus nsp1 is an essential virulence determinant, providing a potential paradigm for the development of a new attenuated vaccine based on modified nSp1.

TL;DR: Structural characterization, mutagenesis and biochemical analysis reveal the substrate-binding pockets and the residues that comprise the active site of PEDV 3CLpro and the non-conserved motifs in the pockets cause different cleavage of substrate between P EDV and SARS-CoV3CLpros, which may provide new insights into the recognition of substrates by 3CL Pros in various coronavirus genera.

TL;DR: The first full-length crystal structure of Alphacoronavirus nsp1 from PEDV is reported, the first among coronaviruses to be reported, and shows high similarity to severe acute respiratory syndrome coronavirus (SARS-CoV), and transmissible gastroenteritis virus (TGEV) nsp11–104, despite a lack of sequence homology.

TL;DR: The first dimeric structure of the arterivirus nsp11 from PRRSV is reported, which exhibits a unique structure and assembles into an asymmetric dimer whose structure is completely different from the hexameric structure of coronav virus nsp15.

TL;DR: Bioinformatics and biochemical experiments showed that by interacting with 40S ribosomal subunit, the lysine located at amino acid 164 (K164) was the key residue that enabled SARS-CoV-2 nsp1 to suppress host gene expression.