Project Details
Projekt Print View

Interference of the viral effector proteins pp71 and IE1 with intrinsic and innate immunity against human cytomegalovirus infections

Subject Area Virology
Term from 2017 to 2022
Project identifier Deutsche Forschungsgemeinschaft (DFG) - Project number 386120716
 
Final Report Year 2023

Final Report Abstract

PML-NBs (nuclear bodies) are subnuclear structures that can be defined as SUMOylation-dependent accumulations of a large number (>140) of cellular proteins. The promyelocytic leukemia protein PML acts as an essential scaffold for these accumulations. The autoantigen Sp100 and the chromatinmodifiers Daxx and ATRX are additional important components. We were able to demonstrate that PML-NBs inhibit viral infections by acting as a cell-intrinsic barrier. Furthermore, we detected coactivation of the interferon-response by PML-NBs. However, during infection with human cytomegalovirus (HCMV) the viral effector proteins pp71 and IE1 counteract these antiviral functions. During this project we were able to solve the crystal structures of the IE1 proteins of human and rat cytomegalovirus. Despite limited amino acid sequence identity of 9% the proteins share a highly conserved fold structure with species-specific adaptations. In addition to species-specific binding of IE1 to PML proteins, we identified the protein FEN-1 (FLAP endonuclease 1) as a novel cellular interaction partner. A further characterization of this interaction revealed a novel mechanism how a viral regulatory protein activates FEN-1 in order to overcome replication barriers. Furthermore, this project revealed that PML-NBs are not only able to entrap and inactivate viral nucleic acids in a reversible manner, but we observed that this is also true for viral proteins (e.g. viral capsids). This could be demonstrated by ultrastructural characterization of giant PML-NBs that form after infection of cells with HCMV exhibiting a deletion of ie1. Finally, we were able to further clarify how IE1 and pp71 are able to inhibit the native immune response: IE1 induces the citrullination of interferonregulated proteins resulting in abrogation of their antiviral function. The PML-NB component ATRX was identified as a broadly acting coactivator of native immune responses which modulates the chromatin structure of distinct interferon-stimulated genes upon IFN treatment. Consequently, mutations in ATRX that are frequently found in human tumors and viral effector proteins that target ATRX are both able to compromise the native immune response.

Publications

 
 

Additional Information

Textvergrößerung und Kontrastanpassung