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Virologica Sinica logoLink to Virologica Sinica
. 2015 Apr 17;30(2):153–161. doi: 10.1007/s12250-015-3581-8

Severe acute respiratory syndrome coronavirus protein 6 mediates ubiquitin-dependent proteosomal degradation of N-Myc (and STAT) interactor

Weijia Cheng 1, Shiyou Chen 2, Ruiling Li 2, Yu Chen 2, Min Wang 1,, Deyin Guo 1,2
PMCID: PMC7091177  PMID: 25907116

Abstract

Severe acute respiratory syndrome coronavirus (SARS-CoV) encodes eight accessory proteins, the functions of which are not yet fully understood. SARS-CoV protein 6 (P6) is one of the previously studied accessory proteins that have been documented to enhance viral replication and suppress host interferon (IFN) signaling pathways. Through yeast two-hybrid screening, we identified eight potential cellular P6-interacting proteins from a human spleen cDNA library. For further investigation, we targeted the IFN signaling pathway-mediating protein, N-Myc (and STAT) interactor (Nmi). Its interaction with P6 was confirmed within cells. The results showed that P6 can promote the ubiquitin-dependent proteosomal degradation of Nmi. This study revealed a new mechanism of SARS-CoV P6 in limiting the IFN signaling to promote SARS-CoV survival in host cells.

Keywords: severe acute respiratory syndrome coronavirus (SARS-CoV), P6, N-Myc (and STAT) interactor (Nmi), interferon (IFN) signaling pathway, ubiquitination, proteosomal degradation

Footnotes

The authors contributed equally to this work.

ORCID: 0000-0001-8816-3952

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