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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Winkler, Michael Bogdanow, Boris Hagemeier, Christian Straschewski, Sarah Weisbach, Henry Voigt, Sebastian Wiebusch, Lüder Von Einem, Jens |
| Description | Author Affiliation: Bogdanow B ( Labor für Pädiatrische Molekularbiologie, Charité-Universitätsmedizin Berlin, 13353 Berlin, Germany.); |
| Abstract | Upon cell entry, herpesviruses deliver a multitude of premade virion proteins to their hosts. The interplay between these incoming proteins and cell-specific regulatory factors dictates the outcome of infections at the cellular level. Here, we report a unique type of virion-host cell interaction that is essential for the cell cycle and differentiation state-dependent onset of human cytomegalovirus (HCMV) lytic gene expression. The major tegument 150-kDa phosphoprotein (pp150) of HCMV binds to cyclin A2 via a functional RXL/Cy motif resulting in its cyclin A2-dependent phosphorylation. Alanine substitution of the RXL/Cy motif prevents this interaction and allows the virus to fully escape the cyclin-dependent kinase (CDK)-mediated block of immediate early (IE) gene expression in S/G2 phase that normally restricts the onset of the HCMV replication cycle to G0/G1. Furthermore, the cyclin A2-CDK-pp150 axis is also involved in the establishment of HCMV quiescence in NTera2 cells, showing the importance of this molecular switch for differentiation state-dependent regulation of IE gene expression. Consistent with the known nucleocapsid-binding function of pp150, its RXL/Cy-dependent phosphorylation affects gene expression of the parental virion only, suggesting a cis-acting, virus particle-associated mechanism of control. The pp150 homologs of other primate and mammalian CMVs lack an RXL/Cy motif and accordingly even the nearest relative of HCMV, chimpanzee CMV, starts its lytic cycle in a cell cycle-independent manner. Thus, HCMV has evolved a molecular sensor for cyclin A2-CDK activity to restrict its IE gene expression program as a unique level of self-limitation and adaptation to its human host. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 43 |
| Volume Number | 110 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2013-10-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cell Cycle Cell Differentiation Cyclin A2 Metabolism Cyclin-Dependent Kinases Cytomegalovirus Phosphoproteins Viral Matrix Proteins Amino Acid Motifs Genetics Amino Acid Sequence Cell Line Cell Line, Tumor Physiology Flow Cytometry Gene Expression Regulation, Viral Genes, Immediate-Early HEK293 Cells Host-Pathogen Interactions Immunoblotting Luminescent Proteins Microscopy, Fluorescence Mutation Phosphorylation Protein Binding Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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