Genome-Wide Screen of Three Herpesviruses for Protein Subcellular Localization and Alteration of PML Nuclear Bodies

PLoS Pathogens

Tricia Chen¹  Megan Domagala¹  Nicole Zimmerman²  Lori Frappier²  Jayme Salsman² 

[1] Affinium Pharmaceuticals Inc., Toronto, Ontario, Canada;Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada

关键词: Nuclear bodies;    Protein expression;    Cell disruption;    SUMOylation;    293T cells;    Herpesviruses;    Protein structure;    Viral structure;   

DOI  :  10.1371/journal.ppat.1000100

学科分类：生物科学（综合）

来源: Public Library of Science

【 摘 要 】

Herpesviruses are large, ubiquitous DNA viruses with complex host interactions, yet many of the proteins encoded by these viruses have not been functionally characterized. As a first step in functional characterization, we determined the subcellular localization of 234 epitope-tagged proteins from herpes simplex virus, cytomegalovirus, and Epstein–Barr virus. Twenty-four of the 93 proteins with nuclear localization formed subnuclear structures. Twelve of these localized to the nucleolus, and five at least partially localized with promyelocytic leukemia (PML) bodies, which are known to suppress viral lytic infection. In addition, two proteins disrupted Cajal bodies, and 19 of the nuclear proteins significantly decreased the number of PML bodies per cell, including six that were shown to be SUMO-modified. These results have provided the first functional insights into over 120 previously unstudied proteins and suggest that herpesviruses employ multiple strategies for manipulating nuclear bodies that control key cellular processes.

【 授权许可】

CC BY