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The leader proteinase of foot-and-mouth disease virus: structure-function relationships in a proteolytic virulence factor

  • Jutta Steinberger and Tim Skern EMAIL logo
Published/Copyright: March 26, 2014

Abstract

The leader proteinase (Lpro) of the foot-and-mouth disease virus inhibits the host innate immune response by at least three different mechanisms. The most well-characterised of these is the prevention of the synthesis of cytokines such as interferons immediately after infection, brought about by specific proteolytic cleavage of the eukaryotic initiation factor 4G. This prevents the recruitment of capped cellular mRNA; however, the viral RNA can be translated under these conditions. The two other mechanisms are the induction of NF-κB cleavage and the deubiquitination of immune signalling molecules. This review focuses on the structure-function relationships in Lpro responsible for these widely divergent activities.


Corresponding author: Tim Skern, Max F. Perutz Laboratories, Medical University of Vienna, Department of Medical Biochemistry, Dr. Bohr-Gasse 9/3, A-1030 Vienna, Austria, e-mail:

Acknowledgments

This work was supported by grants P20889 and P24038 from the Austrian Science Foundation to T.S.

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Received: 2014-2-28
Accepted: 2014-3-24
Published Online: 2014-3-26
Published in Print: 2014-10-1

©2014 by De Gruyter

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