Key result
Human RNase P from HeLa cells specifically and efficiently cleaves hepatitis C virus transcripts in vitro, representing the first description of human RNase P-viral RNA cleavage.
Human RNase P specifically cleaves HCV RNA, suggesting structural similarities to tRNA and identifying a potential vulnerability for therapeutic strategies.
Hypothesis-generating for RNase P as HCV antiviral target; leaves open in vivo efficacy and clinical translation.
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 A(2860) 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.
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Nadal et al. (2002) studied Hepatitis C Virus. Human RNase P was evaluated on Cleavage of HCV transcripts. Human RNase P from HeLa cells specifically and efficiently cleaves hepatitis C virus transcripts in vitro, representing the first description of human RNase P-viral RNA cleavage.
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