Unknown

Dataset Information

0

The Tanapoxvirus 142R Protein is a Serine-Threonine Kinase that Phosphorylates the Tumor Suppressor p53.


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.

SUBMITTER: Seibert KN 

PROVIDER: S-EPMC3553498 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

altmetric image

Publications

The Tanapoxvirus 142R Protein is a Serine-Threonine Kinase that Phosphorylates the Tumor Suppressor p53.

Seibert Krystal N KN   Essani Karim K   Bejcek Bruce E BE  

The open virology journal 20130121


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 replicat  ...[more]

Similar Datasets

| S-EPMC6480182 | biostudies-literature
| S-EPMC4785400 | biostudies-other
| S-EPMC6521941 | biostudies-literature
| S-EPMC2192163 | biostudies-other
| S-EPMC5494665 | biostudies-other
| S-EPMC4423074 | biostudies-literature