Article

Viral serine/threonine protein kinases.

Department of Virology, Parasitology, and Immunology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, 9820 Merelbeke, Belgium.
Journal of Virology (Impact Factor: 4.65). 11/2010; 85(3):1158-73. DOI: 10.1128/JVI.01369-10
Source: PubMed

ABSTRACT Phosphorylation represents one the most abundant and important posttranslational modifications of proteins, including viral proteins. Virus-encoded serine/threonine protein kinases appear to be a feature that is unique to large DNA viruses. Although the importance of these kinases for virus replication in cell culture is variable, they invariably play important roles in virus virulence. The current review provides an overview of the different viral serine/threonine protein kinases of several large DNA viruses and discusses their function, importance, and potential as antiviral drug targets.

Full-text

Available from: Thary Jacob, Jun 12, 2015
1 Follower
 · 
124 Views
  • [Show abstract] [Hide abstract]
    ABSTRACT: Phosphorylation is a common protein modification by which a cell or virus regulates protein activity, and subsequently cellular and viral functions. Herpesviruses commonly encode protein kinases that regulate their own replicative processes and modify host cellular machinery, by phosphorylating target proteins. Although numerous studies have revealed the multiple downstream effects of viral protein kinases and their potential molecular mechanisms, it remains unknown whether herpes viral protein kinases are involved in viral replication and pathogenicity in vivo. This review focuses on Us3 protein kinase encoded by herpes simplex virus 1 and provides a current overview of its functions in infected cells, with a special focus on their relevancy in vivo.
    Cornea 01/2013; 32:S22-S27. DOI:10.1097/ICO.0b013e3182a0a320 · 2.36 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Phosphorylation is one of the major mechanisms by which the activities of protein factors can be regulated. Such regulation impacts multiple key-functions of mammalian cells, including signal transduction, nucleo-cytoplasmic shuttling, macromolecular complexes assembly, DNA binding and regulation of enzymatic activities to name a few. To ensure their capacities to replicate and propagate efficiently in their hosts, viruses may rely on the phosphorylation of viral proteins to assist diverse steps of their life cycle. It has been known for several decades that particles from diverse virus families contain some protein kinase activity. While large DNA viruses generally encode for viral kinases, RNA viruses and more precisely retroviruses have acquired the capacity to hijack the signaling machinery of the host cell and to embark cellular kinases when budding. Such property was demonstrated for HIV-1 more than a decade ago. This review summarizes the knowledge acquired in the field of HIV-1-associated kinases and discusses their possible function in the retroviral life cycle.
    Retrovirology 09/2011; 8:71. DOI:10.1186/1742-4690-8-71 · 4.77 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: To effectively respond to viral infections, mammals rely on the innate and adaptive immune systems. Additionally, host cellular responses, such as apoptosis also play a vital role in the host defense mechanisms. To accomplish a successful replicative strategy in vivo, animal viruses have evolved a variety of molecular mechanisms that interfere with host responses. Poxviruses in particular, represents a prime example of where animal viruses encode a wide variety of proteins necessary for replication and subversion of the host's immune and single cell responses. Several proteins that inhibit host immmunomodulatory cytokines and apoptosis of infected cells have been characterized in vaccinia virus (VV). Here, we describe the identification of a protein encoded by the tanapox virus genome (142R open reading frame) that is orthologous to the B1R protein from VV. We demonstrate that like B1R, TPV142R encodes a serine threonine kinase that can phosphorylate the tumor suppressor p53 and therefore has the potential for inhibiting apoptosis of infected cells.
    The Open Virology Journal 01/2013; 7:1-4. DOI:10.2174/1874357901307010001