Journal article
Herpes Simplex Virus Tegument ICP0 Is Capsid Associated, and Its E3 Ubiquitin Ligase Domain Is Important for Incorporation into Virions
Journal of virology, Vol.84(3), pp.1637-1640
02/2010
Handle:
https://hdl.handle.net/2376/105636
PMCID: PMC2812315
PMID: 19906912
Abstract
Herpes simplex virus (HSV) immediate-early (IE) protein ICP0 is a multifunctional regulator of HSV infection. ICP0 that is present in the tegument layer has not been well characterized. Protein compositions of wild-type and ICP0 null virions were similar, suggesting that the absence of ICP0 does not grossly impair virion assembly. ICP0 has a RING finger domain with E3 ubiquitin ligase activity that is necessary for IE functions. Virions with mutations in this domain contained greatly reduced levels of tegument ICP0, suggesting that the domain influences the incorporation of ICP0. Virion ICP0 was resistant to removal by detergent and salt and was associated with capsids, features common to inner tegument proteins.
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Details
- Title
- Herpes Simplex Virus Tegument ICP0 Is Capsid Associated, and Its E3 Ubiquitin Ligase Domain Is Important for Incorporation into Virions
- Creators
- Mark G Delboy - Department of Microbiology and Immunology, School of Medicine, Virginia Commonwealth University, Richmond, Virginia 23298-0678Carlos R Siekavizza-Robles - Department of Microbiology and Immunology, School of Medicine, Virginia Commonwealth University, Richmond, Virginia 23298-0678Anthony V Nicola - Department of Microbiology and Immunology, School of Medicine, Virginia Commonwealth University, Richmond, Virginia 23298-0678
- Publication Details
- Journal of virology, Vol.84(3), pp.1637-1640
- Academic Unit
- Veterinary Microbiology and Pathology, Department of
- Publisher
- American Society for Microbiology (ASM)
- Identifiers
- 99900546928201842
- Language
- English
- Resource Type
- Journal article