Herpes Simplex Virus Tegument ICP0 Is Capsid Associated, and Its E3 Ubiquitin Ligase Domain Is Important for Incorporation into Virions
| Autor: | Carlos R. Siekavizza-Robles, Anthony V. Nicola, Mark G. Delboy |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Ubiquitin-Protein Ligases
viruses Blotting Western Immunology medicine.disease_cause Microbiology Immediate early protein Immediate-Early Proteins Capsid Ubiquitin Cell Line Tumor Virology medicine Humans biology Structure and Assembly Virion Viral tegument biochemical phenomena metabolism and nutrition Ubiquitin ligase RING finger domain Herpes simplex virus Virion assembly Insect Science biology.protein Electrophoresis Polyacrylamide Gel |
| Zdroj: | Journal of Virology. 84:1637-1640 |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.02041-09 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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