Ubiquitin-specific protease 9X in host cells interacts with herpes simplexvirus 1 ICP0

Journal of Veterinary Medical Science

Akihisa KATO¹  Yasushi KAWAGUCHI¹  Jun ARII¹  Masaaki OYAMA²  Naoto KOYANAGI¹  Yuka SATO¹  Hiroko KOZUKA-HATA² 

[1] Division of Molecular Virology, Department of Microbiology and Immunology, The Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo 108�?8639, Japan;Medical Proteomics Laboratory, The Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo 108�?8639, Japan

关键词: deubiquitylating enzyme;    E3 ubiquitin ligase;    herpes simplex virus;    ICP0;    USP9X;   

DOI  :  10.1292/jvms.15-0598

学科分类：兽医学

来源: Japanese Society of Veterinary Science

【 摘 要 】

References(24)Herpes simplex virus 1 (HSV-1) expresses infected cell protein 0 (ICP0), amulti-functional protein with E3 ubiquitin ligase activity and a critical regulator of theviral life cycle. To obtain novel insights into the molecular mechanism by which ICP0regulates HSV-1 replication, we analyzed HEp-2 cells infected with HSV-1 by tandemaffinity purification and mass spectrometry-based proteomics. This screen identified 50host-cell proteins that potentially interact with ICP0, including ubiquitin-specificprotease 9X (USP9X). The interaction between ICP0 and USP9X was confirmed byco-immunoprecipitation. Notably, USP9X depletion increased the ICP0 abundance and promotedviral replication. These results suggest that USP9X-dependent regulation of ICP0expression is part of a complex feedback mechanism that facilitates optimal HSV-1replication.

【 授权许可】

Unknown