HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Supplementary table Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Yin, J. Articles by Paul, A. V. Search for Related Content PubMed PubMed Citation Articles by Yin, J. Articles by Paul, A. V. Agricola Articles by Yin, J. Articles by Paul, A. V.

Complete protein linkage map between the P2 and P3 non-structural proteins of poliovirus

Jiang Yin

Department of Molecular Genetics and Microbiology, School of Medicine, Stony Brook University, Stony Brook, NY 11794, USA

Correspondence
Aniko V. Paul
apaul{at}notes.cc.sunysb.edu

All of the non-structural proteins of poliovirus, including their processing precursors, are involved in the replication of the viral RNA genome. These proteins assemble into a replication complex, which also contains the viral RNA and cellular factors. An understanding of how these viral proteins interact with each other would enhance our understanding of the molecular events occurring during poliovirus infection of the cell. Previously, we have employed the yeast two-hybrid system to construct two separate linkage maps for the polioviral P2 and P3 proteins, respectively. In the present study, we have searched for interacting pairs between the P2 and P3 proteins in a similar inducible yeast two-hybrid system. Although, the primary functions of the proteolytic products of the P2 and P3 domains of the polyprotein in the viral life cycle are different, we observed significant interactions between 2C^ATPase and 3AB; 2A^pro and 3A, 3C^pro or 3D^pol; 2B and 3A or 3AB. All of the interactions were measured in the yeast two-hybrid system by exchanging the interacting pairs on the transcription-activation and DNA-binding constructs. In vitro GST pull-down assay suggested that the 2C^ATPase/3AB interaction involves both ionic and hydrophobic contacts between the two proteins. The possible biological implication of the interactions observed in the yeast two-hybrid system will be discussed.

Present address: Department of Biochemistry, University of Alberta, Canada.

A supplementary table showing primers used to make yeast two-hybrid constructs is available with the online version of this paper.

This article has been cited by other articles:

				P. Adams, E. Kandiah, G. Effantin, A. C. Steven, and E. Ehrenfeld Poliovirus 2C Protein Forms Homo-oligomeric Structures Required for ATPase Activity J. Biol. Chem., August 14, 2009; 284(33): 22012 - 22021. [Abstract] [Full Text] [PDF]

				A. M. De Palma, H. J. Thibaut, L. van der Linden, K. Lanke, W. Heggermont, S. Ireland, R. Andrews, M. Arimilli, T. H. Al-Tel, E. De Clercq, et al. Mutations in the Nonstructural Protein 3A Confer Resistance to the Novel Enterovirus Replication Inhibitor TTP-8307 Antimicrob. Agents Chemother., May 1, 2009; 53(5): 1850 - 1857. [Abstract] [Full Text] [PDF]