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The cellular RING finger protein PML is not a functional counterpart of the herpes simplex virus type 1 RING finger
1MRC Virology Unit, Glasgow, UK. everett@vir.gla.ac.uk
Abstract:
Herpes simplex virus type 1 (HSV-1) immediate early protein Vmw110 (also known as ICP0) is required for the fully efficient expression of viral genes during onset of lytic growth and for normal reactivation from latency. Both Vmw110 and the cellular protein PML are members of the RING finger family of zinc binding domain proteins, a family which includes an increasing number of examples from a wide evolutionary range. The function of the RING finger domain is unknown, and the question arises whether the RING finger (like several other examples of conserved domains) fulfils similar functions in these diverse proteins. Another link between Vmw110 and PML is that at early times of HSV-1 infection Vmw110 migrates to distinct nuclear structures which contain the PML protein. In order to test the possibility that PML and Vmw110, or their RING finger domains, fulfill similar functions, we have constructed recombinant viruses that express either intact PML, or a chimeric Vmw110 protein which contains the PML RING finger in place of its own. The results indicate that the PML and Vmw110 RING fingers are not functionally interchangeable, and that PML is not a cellular functional counterpart of Vmw110.
Insights
Herpes simplex virus type 1 protein Vmw110 (ICP0) and cellular PML protein share a RING finger domain. Their domains are not interchangeable, indicating PML is not a functional counterpart to Vmw110.
Area of Science:
- Virology
- Molecular Biology
- Cellular Biology
Background:
- Herpes simplex virus type 1 (HSV-1) immediate early protein Vmw110 (ICP0) is crucial for viral gene expression and reactivation from latency.
- Vmw110 and the cellular protein PML belong to the RING finger family of zinc-binding proteins.
- The function of the RING finger domain is not fully understood, prompting investigation into conserved domain functions.
Purpose of the Study:
- To investigate the functional similarity between the RING finger domains of HSV-1 Vmw110 (ICP0) and cellular PML protein.
- To determine if the PML protein serves as a cellular functional counterpart to Vmw110.
- To test the interchangeability of the RING finger domains of Vmw110 and PML.
Main Methods:
- Construction of recombinant viruses expressing intact PML or a chimeric Vmw110 protein with the PML RING finger.
- Analysis of viral gene expression and reactivation from latency in the presence of engineered proteins.
- Comparative study of Vmw110 and PML protein functions and their respective RING finger domains.
Main Results:
- The RING finger domains of PML and Vmw110 (ICP0) were found to be non-interchangeable.
- Recombinant viruses expressing chimeric proteins did not exhibit functional equivalence.
- The cellular PML protein does not act as a functional counterpart to the viral Vmw110 protein.
Conclusions:
- The RING finger domains of Vmw110 and PML possess distinct functional specificities.
- PML protein is not a cellular functional equivalent of HSV-1 Vmw110 (ICP0).
- This study clarifies the specific roles of these proteins in viral replication and cellular interactions.