6LP9
the protein of cat virus
Summary for 6LP9
| Entry DOI | 10.2210/pdb6lp9/pdb |
| Descriptor | nsp1 protein (2 entities in total) |
| Functional Keywords | cat virus, viral protein |
| Biological source | Feline infectious peritonitis virus |
| Total number of polymer chains | 4 |
| Total formula weight | 54041.66 |
| Authors | Shen, Z.,Peng, G.Q. (deposition date: 2020-01-09, release date: 2020-08-12, Last modification date: 2023-11-29) |
| Primary citation | Shen, Z.,Yang, Y.,Yang, S.,Zhang, G.,Xiao, S.,Fu, Z.F.,Peng, G. Structural and Biological Basis of Alphacoronavirus nsp1 Associated with Host Proliferation and Immune Evasion. Viruses, 12:-, 2020 Cited by PubMed Abstract: Non-structural protein 1 (nsp1) is only characterized in alphacoronaviruses (α-CoVs) and betacoronaviruses (β-CoVs). There have been extensive researches on how the β-CoVs nsp1 regulates viral virulence by inhibiting host protein synthesis, but the regulatory mechanism of the α-CoVs nsp1 is still unclear. Here, we report the 2.1-Å full-length crystal structure of nsp1 in emerging porcine SADS-CoV and the 1.8-Å full-length crystal structure of nsp1 in the highly lethal cat FIPV. Although they belong to different subtypes of α-CoVs, these viruses all have a bucket-shaped fold composed of six β-sheets, similar to the crystal structure of PEDV and TGEV nsp1. Comparing the above four structures, we found that the structure of α-CoVs nsp1 in the same subtype was more conserved. We then selected mammalian cells that were treated with SADS-CoV and FIPV nsp1 for RNA sequencing analysis and found that nsp1 had a specific inhibitory effect on interferon (IFN) and cell cycle genes. Using the Renilla luciferase (Rluc) assay and Western blotting, we confirmed that seven representative α-CoVs nsp1s could significantly inhibit the phosphorylation of STAT1-S727 and interfere with the effect of IFN-I. Moreover, the cell cycle experiment confirmed that α-CoVs nsp1 could encourage host cells to stay in the G0/G1 phase. Based on these findings, we not only greatly improved the crystal structure data on α-CoVs nsp1, but we also speculated that α-CoVs nsp1 regulated host proliferation and immune evasion-related biological functions by inhibiting the synthesis of host proteins, thus creating an environment conducive to the virus. PubMed: 32731335DOI: 10.3390/v12080812 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.803 Å) |
Structure validation
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