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Flavivirus RNA cap methyltransferase: structure,
function, and inhibition |
| Lihui LIU1,Hui CHEN1,Jing ZHANG1,Hua LING1,Zhong LI1,Hongping DONG2,Pei-Yong SHI2,Hongmin LI3, |
| 1.Wadsworth Center, New
York State Department of Health, 120 New Scotland Ave, Albany, NY
12208, USA; 2.Wadsworth Center, New
York State Department of Health, 120 New Scotland Ave, Albany, NY
12208, USA；Current address Novartis
Institute for Tropical Diseases, 10 Biopolis Road, Singapore 138670; 3.Wadsworth Center, New
York State Department of Health, 120 New Scotland Ave, Albany, NY
12208, USA；Department of Biomedical
Sciences, School of Public Health, State University of New York, Albany,
New York 12201-0509, USA; |
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Abstract Many flaviviruses are significant human pathogens. The plus-strand RNA genome of a flavivirus contains a 5′ terminal cap 1 structure (m7GpppAmG). The flavivirus encodes one methyltransferase (MTase), located at the N-terminal portion of the NS5 RNA-dependent RNA polymerase (RdRp). Here we review recent advances in our understanding of flaviviral capping machinery and the implications for drug development. The NS5 MTase catalyzes both guanine N7 and ribose 2’-OH methylations during viral cap formation. Representative flavivirus MTases, from dengue, yellow fever, and West Nile virus (WNV), sequentially generate GpppA→m7GpppA→m7GpppAm. Despite the existence of two distinct methylation activities, the crystal structures of flavivirus MTases showed a single binding site for S-adenosyl-L-methionine (SAM), the methyl donor. This finding indicates that the substrate GpppA-RNA must be repositioned to accept the N7 and 2’-O methyl groups from SAM during the sequential reactions. Further studies demonstrated that distinct RNA elements are required for the methylations of guanine N7 on the cap and of ribose 2’-OH on the first transcribed nucleotide. Mutant enzymes with different methylation defects can trans complement one another in vitro, demonstrating that separate molecules of the enzyme can independently catalyze the two cap methylations in vitro. In the context of the infectious virus, defects in both methylations, or a defect in the N7 methylation alone, are lethal to WNV. However, viruses defective solely in 2’-O methylation are attenuated and can protect mice from later wild-type WNV challenge. The results demonstrate that the N7 methylation activity is essential for the WNV life cycle and, thus, methyltransferase represents a novel and promising target for flavivirus therapy.
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| Keywords
Flavivirus NS5
RNA cap methylation
methyltransferase
structure and function
inhibitor
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Issue Date: 01 August 2010
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