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

Weijia Cheng; Shiyou Chen; Ruiling Li; Yu Chen; Min Wang; Deyin Guo

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

Virol Sin. 2015 Apr;30(2):153-61. doi: 10.1007/s12250-015-3581-8. Epub 2015 Apr 17.

Authors

Weijia Cheng¹, Shiyou Chen, Ruiling Li, Yu Chen, Min Wang, Deyin Guo

Affiliation

¹ School of Basic Medical Sciences, Wuhan University, Wuhan, 430072, China.

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Gene Library
Host-Pathogen Interactions*
Humans
Intracellular Signaling Peptides and Proteins / metabolism*
Protein Binding
Protein Interaction Mapping
Proteolysis
Severe acute respiratory syndrome-related coronavirus / physiology*
Two-Hybrid System Techniques
Ubiquitin / metabolism*
Viral Proteins / metabolism*

Substances

Intracellular Signaling Peptides and Proteins
NMI protein, human
Ubiquitin
Viral Proteins
protein 6, SARS virus