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J. Biol. Chem., Vol. 280, Issue 51, 42106-42112, December 23, 2005

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The RNA Binding G-patch Domain in Retroviral Protease Is Important for Infectivity and D-type Morphogenesis of Mason-Pfizer Monkey Virus^*

Helena Bauerová-Zábranská, Jitka Stokrová, Kvido Strísovsk1, Eric Hunter¶, Tomás Ruml||, and Iva Pichová2

From the Centre for New Antivirals and Antineoplastics, Institute of Organic Chemistry and Biochemistry and the Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague 6, Czech Republic, the ^¶Department of Pathology and Laboratory Medicine, Emory Vaccine Center, Emory University, Atlanta, Georgia 30322, the ^||Department of Biochemistry and Microbiology, Institute of Chemical Technology, Prague 6, Czech Republic

Retroviral proteases (PRs) cleave the viral polyprotein precursors into functional mature proteins late during particle release and are essential for viral replication. Unlike most retroviruses, -retroviruses, including Mason-Pfizer monkey virus (M-PMV), assemble immature capsids within the cytoplasm of the cell. The activation of -retroviral proteases must be highly regulated, because processing of the Gag-related polyprotein precursors occurs only after transport of immature capsids to the plasma membrane and budding. Several -retroviral proteases have unique C-terminal extension sequences, containing a glycine-rich motif (G-patch), which specifically binds in vitro to single-stranded nucleic acids. In M-PMV PR the G-patch is removed in vitro as well as in vivo by autoproteolytic processing to yield truncated active forms of PR. To investigate the role of the G-patch domain on the virus life cycle, we introduced mutations within the C-terminal domain of protease. We found that the G-patch domain of M-PMV PR is not required for the processing of viral polyproteins, but it significantly influences the infectivity of M-PMV, the activity of reverse transcriptase, and assembly of immature capsid within the cells. These results demonstrate for the first time that the G-patch domain of M-PMV PR is critical for the life cycle of -retroviruses, and its evolutionary conservation within members of this genus suggests its importance for retroviruses that display D-type morphology.

Received for publication, July 22, 2005 , and in revised form, October 12, 2005.

^* This work was supported by programmes 1M6138896301 and 1M6837805002 of the Czech Ministry of Education and by research projects Z 40550506 AVOZ 505 20514 and MSM 6046137305. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Present address: MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.

² To whom correspondence should be addressed: Dept. of Protein Biochemistry, Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo n. 2, 166 10 Prague 6, Czech Republic. Fax: 420-220183556; E-mail: iva.pichova{at}uochb.cas.cz.

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