White spot syndrome virus protein ICP11: A histone-binding DNA mimic that disrupts nucleosome assembly
- 30 December 2008
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 105 (52) , 20758-20763
- https://doi.org/10.1073/pnas.0811233106
Abstract
White spot syndrome virus (WSSV) is a large (≈300 kbp), double-stranded DNA eukaryotic virus that has caused serious disease in crustaceans worldwide. ICP11 is the most highly expressed WSSV nonstructural gene/protein, which strongly suggests its importance in WSSV infection; but until now, its function has remained obscure. We show here that ICP11 acts as a DNA mimic. In crystal, ICP11 formed a polymer of dimers with 2 rows of negatively charged spots that approximated the duplex arrangement of the phosphate groups in DNA. Functionally, ICP11 prevented DNA from binding to histone proteins H2A, H2B, H3, and H2A.x, and in hemocytes from WSSV-infected shrimp, ICP11 colocalized with histone H3 and activated-H2A.x. These observations together suggest that ICP11 might interfere with nucleosome assembly and prevent H2A.x from fulfilling its critical function of repairing DNA double strand breaks. Therefore, ICP11 possesses a functionality that is unique among the handful of presently known DNA mimic proteins.Keywords
This publication has 37 references indexed in Scilit:
- HU-α binds to the putative double-stranded DNA mimic HI1450 from Haemophilus influenzaeProtein Science, 2009
- Histone modifications induced by a family of bacterial toxinsProceedings of the National Academy of Sciences, 2007
- Identification of a Novel Nonstructural Protein, VP9, from White Spot Syndrome Virus: Its Structure Reveals a Ferredoxin Fold with Specific Metal Binding SitesJournal of Virology, 2006
- PmRab7 Is a VP28-Binding Protein Involved in White Spot Syndrome Virus Infection inShrimpJournal of Virology, 2006
- DNA mimicry by proteins and the control of enzymatic activity on DNATrends in Biotechnology, 2006
- Genomic and Proteomic Analysis of Thirty-Nine Structural Proteins of Shrimp White Spot Syndrome VirusJournal of Virology, 2004
- Solution structure of the highly acidic protein HI1450 from Haemophilus influenzae, a putative double‐stranded DNA mimicProteins-Structure Function and Bioinformatics, 2003
- Bovine Herpesvirus 1 Tegument Protein VP22 Interacts with Histones, and the Carboxyl Terminus of VP22 Is Required for Nuclear LocalizationJournal of Virology, 2001
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994