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) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted 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 Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lama, J. Articles by Rodrguez, P. L. Search for Related Content PubMed PubMed Citation Articles by Lama, J. Articles by Rodrguez, P. L. Social Bookmarking                      What's this?

Volume 270, Number 24, Issue of June 16, pp. 14430-14438, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Juan Lama , Miguel A. Sanz , Pedro L. Rodrguez

The poliovirus polypeptide 3AB, the precursor of the genome-bound VPg protein, stimulates in vitro the synthesis of poly(U) directed by the viral polymerase 3D (Lama, J., Paul, A., Harris, K., and Wimmer, E. (1994) J. Biol. Chem. 269, 66-70), suggesting that 3AB could be modulating the activity of the viral polymerase in poliovirus-infected cells. To address the exact function of 3AB in the viral replication cycle, a biochemical and molecular genetic analysis of 3AB has been carried out. 3AB protein bound RNA probes in two different assays, and amino acid positions implicated in the RNA binding activity of 3AB were determined. Mutant proteins with reduced RNA binding activity were unable to stimulate 3D polymerase activity. Purified protein 3A showed no RNA binding or 3Dstimulatory activity, but 3A and VPg mutations conferred a synergistic effect on the 3AB functions. Polioviruses encoding for these mutant 3ABs were constructed. These mutant viruses translated their RNA genomes in vitro and processed their polyproteins as wild type virus did. Cells infected with 3AB mutant viruses showed over 90% inhibition in the accumulation of plus and minus viral RNA strands and more than 100-fold reduction of virus yield at 4 h postinfection. Our results suggest that 3AB protein functions in vivo as a co-factor of the viral polymerase and that the activity of 3AB may be regulated by proteolytic processing.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				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]

				H. B. Pathak, H. S. Oh, I. G. Goodfellow, J. J. Arnold, and C. E. Cameron Picornavirus Genome Replication: ROLES OF PRECURSOR PROTEINS AND RATE-LIMITING STEPS IN oriI-DEPENDENT VPg URIDYLYLATION J. Biol. Chem., November 7, 2008; 283(45): 30677 - 30688. [Abstract] [Full Text] [PDF]

				J. J. DeStefano and O. Titilope Poliovirus Protein 3AB Displays Nucleic Acid Chaperone and Helix-Destabilizing Activities J. Virol., February 15, 2006; 80(4): 1662 - 1671. [Abstract] [Full Text] [PDF]

				N. L. Teterina, M. S. Rinaudo, and E. Ehrenfeld Strand-Specific RNA Synthesis Defects in a Poliovirus with a Mutation in Protein 3A J. Virol., December 1, 2003; 77(23): 12679 - 12691. [Abstract] [Full Text] [PDF]

				A. V. Paul, J. Peters, J. Mugavero, J. Yin, J. H. van Boom, and E. Wimmer Biochemical and Genetic Studies of the VPg Uridylylation Reaction Catalyzed by the RNA Polymerase of Poliovirus J. Virol., December 20, 2002; 77(2): 891 - 904. [Abstract] [Full Text] [PDF]

				V. Rodriguez-Wells, S. J. Plotch, and J. J. DeStefano Primer-dependent synthesis by poliovirus RNA-dependent RNA polymerase (3Dpol) Nucleic Acids Res., July 1, 2001; 29(13): 2715 - 2724. [Abstract] [Full Text] [PDF]

				J.-A. Daros, M. C. Schaad, and J. C. Carrington Functional Analysis of the Interaction between VPg-Proteinase (NIa) and RNA Polymerase (NIb) of Tobacco Etch Potyvirus, Using Conditional and Suppressor Mutants J. Virol., October 1, 1999; 73(10): 8732 - 8740. [Abstract] [Full Text] [PDF]

				V. Lohmann, H. Overton, and R. Bartenschlager Selective Stimulation of Hepatitis C Virus and Pestivirus NS5B RNA Polymerase Activity by GTP J. Biol. Chem., April 16, 1999; 274(16): 10807 - 10815. [Abstract] [Full Text] [PDF]

				T. Yamashita, S. Kaneko, Y. Shirota, W. Qin, T. Nomura, K. Kobayashi, and S. Murakami RNA-dependent RNA Polymerase Activity of the Soluble Recombinant Hepatitis C Virus NS5B Protein Truncated at the C-terminal Region J. Biol. Chem., June 19, 1998; 273(25): 15479 - 15486. [Abstract] [Full Text] [PDF]

				O. C. Richards and E. Ehrenfeld Effects of Poliovirus 3AB Protein on 3D Polymerase-catalyzed Reaction J. Biol. Chem., May 22, 1998; 273(21): 12832 - 12840. [Abstract] [Full Text] [PDF]

				J. S. Towner, T. V. Ho, and B. L. Semler Determinants of Membrane Association for Poliovirus Protein 3AB J. Biol. Chem., October 25, 1996; 271(43): 26810 - 26818. [Abstract] [Full Text] [PDF]