Nsp1 proteins of group I and SARS coronaviruses share structural and functional similarities.
The nsp1 protein of the highly pathogenic SARS coronavirus suppresses host protein synthesis, including genes involved in the innate immune system. A bioinformatic analysis revealed that the nsp1 proteins of group I and SARS coronaviruses have similar structures. Nsp1 proteins of group I coronaviruses interacted with host ribosomal 40S subunit and did not inhibit IRF-3 activation. However, synthesis of host immune and non-immune proteins was inhibited by nsp1 proteins at both transcriptional and translational levels, similar to SARS coronavirus nsp1. These results indicate that different coronaviruses might employ the same nsp1 mechanism to antagonize host innate immunity and cell proliferation. However, nsp1 may not be the key determinant of viral pathogenicity, or the factor used by the SARS coronavirus to evade host innate immunity.
Wang
Yongjin
Y
Laboratory of Wildlife Epidemic Diseases, East China Normal University, Shanghai 200062, China.
Shi
Huiling
H
Rigolet
Pascal
P
Wu
Nannan
N
Zhu
Lichen
L
Xi
Xu-Guang
XG
Vabret
Astrid
A
Wang
Xiaoming
X
Wang
Tianhou
T
D000595:Amino Acid Sequence; D002460:Cell Line; D049109:Cell Proliferation; D017934:Coronavirus / Q000145:classification* / Q000201:enzymology* / Q000235:genetics; D015971:Gene Expression Regulation, Enzymologic; D015967:Gene Expression Regulation, Viral / Q000502:physiology; D006801:Humans; D007113:Immunity, Innate; D008958:Models, Molecular; D008969:Molecular Sequence Data; D012324:RNA-Dependent RNA Polymerase / Q000235:genetics* / Q000378:metabolism*
D012324:RNA-Dependent RNA Polymerase