The Alphaherpesvirus Serine/Threonine Kinase Us3 Disrupts Promyelocytic Leukemia Protein Nuclear Bodies▿†
| Autor: | Masany Jung, Bruce W. Banfield, Renée L. Finnen, Casey E. Neron |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
viruses
Herpesvirus 2 Human Immunology Intranuclear Inclusion Bodies Promyelocytic Leukemia Protein Protein Serine-Threonine Kinases medicine.disease_cause Microbiology Virus Cell Line Promyelocytic leukemia protein chemistry.chemical_compound Viral Proteins Virology MG132 medicine Animals Humans Nuclear protein Serine/threonine-specific protein kinase biology Tumor Suppressor Proteins virus diseases Nuclear Proteins Transfection Cell biology Virus-Cell Interactions Herpes simplex virus chemistry Insect Science embryonic structures biology.protein Vero cell Transcription Factors |
| Popis: | Us3, a serine/threonine kinase encoded by all alphaherpesviruses, plays diverse roles during virus infection, including preventing virus-induced apoptosis, facilitating nuclear egress of capsids, stimulating mRNA translation and promoting cell-to-cell spread of virus infection. Given this diversity, the full spectrum of Us3 function may not yet be recognized. We noted, in transiently transfected cells, that herpes simplex virus type 2 (HSV-2) Us3 disrupted promyelocytic leukemia protein nuclear bodies (PML-NBs). However, PML-NB disruption was not observed in cells expressing catalytically inactive HSV-2 Us3. Analysis of PML-NBs in Vero cells transfected with pseudorabies virus (PRV) Us3 and those in Vero cells infected with Us3-null or -repaired PRV strains indicated that PRV Us3 expression also leads to the disruption of PML-NBs. While loss of PML-NBs in response to Us3 expression was prevented by the proteasome inhibitor MG132, Us3-mediated degradation of PML was not observed in infected cells or in transfected cells expressing enhanced green fluorescent protein (EGFP)-tagged PML isoform IV. These findings demonstrate that Us3 orthologues derived from distantly related alphaherpesviruses cause a disruption of PML-NBs in a kinase- and proteasome-dependent manner but, unlike the alphaherpesvirus ICP0 orthologues, do not target PML for degradation. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|