Bovine herpesvirus-1 VP8 interacts with DNA damage binding protein-1 (DDB1) and is monoubiquitinated during infection

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• 作者：Natalya L. Vasilenko^a ; Marlene Snider^a ; Shaunivan L. Labiuk^c ; Vladislav A. Lobanov^d ; Lorne A. Babiuk^e ; Sylvia van Drunen Littel-van den Hurk^a ; ^b ; ^{sylvia.vandenhurk@usask.ca}
• 关键词：BHV-1 ; VP8 ; Monoubiquitination ; DDB1 ; DDB1-CUL4 E3 ubiquitin ligase
• 刊名：Virus Research
• 出版年：2012
• 期刊代码：92_01681702
• 类别：imm
• 出版时间：July, 2012
• 卷：167
• 期：1
• 页码：56-66
• 文件大小：1825 K

摘要

VP8 is the most abundant tegument protein of bovine herpesvirus-1 (BHV-1). In the present study DNA damage binding protein 1 (DDB1) was identified as interacting partner of VP8. MALDI-TOF mass spectroscopy analysis of proteins co-immunoprecipitated with VP8 identified DDB1 as a protein interacting with VP8. The interaction between VP8 and DDB1 was confirmed based on co-immunoprecipitation and co-localization in both VP8-transfected and BHV-1 infected cells. DDB1 was distributed both in the nucleus and the cytoplasm with some nuclear speckles prior to BHV-1 infection, became perinuclear by 4 h and was predominantly nuclear at 5 h post infection, where it co-localized with VP8. In contrast, in cells infected with a U_L47 deletion mutant DDB1 remained cytoplasmic throughout the course of infection. This suggests that VP8 mediates nuclear re-localization of DDB1. Finally, VP8 was shown to be monoubiquitinated both in VP8-transfected and BHV-1-infected cells. These data suggest that BHV-1 VP8 interacts with DDB1-CUL4 E3 ubiquitin ligase, which correlates to monoubiquitination of this viral protein.