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Journal of Biomedicine and Biotechnology
Volume 2011, Article ID 369648, 23 pages
Review Article

The Multifaceted Poliovirus 2A Protease: Regulation of Gene Expression by Picornavirus Proteases

1European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, 69117 Heidelberg, Germany
2Centro de Biología Molecular Severo Ochoa (CSIC-UAM), C/ Nicolas Cabrera 1, Universidad Autónoma de Madrid, Cantoblanco. 28049 Madrid, Spain

Received 28 October 2010; Revised 18 January 2011; Accepted 17 February 2011

Academic Editor: Decheng Yang

Copyright © 2011 Alfredo Castelló et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


After entry into animal cells, most viruses hijack essential components involved in gene expression. This is the case of poliovirus, which abrogates cellular translation soon after virus internalization. Abrogation is achieved by cleavage of both eIF4GI and eIF4GII by the viral protease 2A. Apart from the interference of poliovirus with cellular protein synthesis, other gene expression steps such as RNA and protein trafficking between nucleus and cytoplasm are also altered. Poliovirus 2 A p r o is capable of hydrolyzing components of the nuclear pore, thus preventing an efficient antiviral response by the host cell. Here, we compare in detail poliovirus 2 A p r o with other viral proteins (from picornaviruses and unrelated families) as regard to their activity on key host factors that control gene expression. It is possible that future analyses to determine the cellular proteins targeted by 2 A p r o will uncover other cellular functions ablated by poliovirus infection. Further understanding of the cellular proteins hydrolyzed by 2 A p r o will add further insight into the molecular mechanism by which poliovirus and other viruses interact with the host cell.