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Originally published In Press as doi:10.1074/jbc.M203595200 on June 11, 2002

J. Biol. Chem., Vol. 277, Issue 34, 30606-30613, August 23, 2002
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Specific Cleavage of Hepatitis C Virus RNA Genome by Human RNase P*

Anna NadalDagger , María MartellDagger , J. Robin Lytle§, Alita J. Lyons§, Hugh D. Robertson§, Beatriz CabotDagger , Juan I. EstebanDagger , Rafael EstebanDagger , Jaime GuardiaDagger , and Jordi GómezDagger

From the Dagger  Servicio de Medicina Interna-Hepatología, Area de Investigación Básica, Hospital Valle de Hebrón, Barcelona 08035, Spain and the § Department of Biochemistry, Weill Medical College of Cornell University, New York, New York 10021

We have found that RNase P from HeLa cells specifically and efficiently cleaves hepatitis C virus (HCV) transcripts in vitro. The evidence includes identification of the 5'-phosphate polarity of the newly generated termini at position A2860 as well as immunological and biochemical assays. Active cleavage has been shown in five dominant sequences of HCV "quasispecies" differing at or near the position of cleavage, demonstrating that this is a general property of HCV RNA. During the analysis, a second cleavage event was found in the 3' domain of the internal ribosome entry site. We have found that HCV RNA competitively inhibits pre-tRNA cleavage by RNase P, suggesting that HCV RNA has structural similarities to tRNA. This finding sets HCV apart from other pathogens causing serious human diseases and represents the first description of human RNase P-viral RNA cleavage. Here we discuss the possible meaning of these RNase P-accessible structures built into the viral genome and their possible role in vivo. Moreover, such structures within the viral genome might be vulnerable to attack by therapeutic strategies.

* Work in New York was supported by National Institutes of Health Grant DK-56424. Work in Barcelona was funded by Ministerio de Ciencia y Tecnología Grants SAF1999-0108 and BIO00-0347, Ministerio de Sanidad y Consumo Grant FISS-01/1351, and the Hospital Vall d'Hebron.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence and requests for materials should be addressed: Laboratorio de Medicina Interna-Hepatología, Area de Investigación Básica (B), Hospital Vall d'Hebron, Paseo Vall d'Hebrón 119-129, Barcelona 08035, Spain. Tel.: 34-93-4894034; Fax: 34-93-4894032; E-mail: jgomez@hg.vhebron.es.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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