A naturally occurring antiviral ribonucleotide encoded by the human genome
Viral infections continue to represent major challenges to public health, and an enhanced mechanistic understanding of the processes that contribute to viral life cycles is necessary for the development of new therapeutic strategies 1 . Viperin, a member of the radical S -adenosyl- l -methionine (SA...
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| Published in | Nature (London) Vol. 558; no. 7711; pp. 610 - 614 |
|---|---|
| Main Authors | , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
01.06.2018
Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Viral infections continue to represent major challenges to public health, and an enhanced mechanistic understanding of the processes that contribute to viral life cycles is necessary for the development of new therapeutic strategies
1
. Viperin, a member of the radical
S
-adenosyl-
l
-methionine (SAM) superfamily of enzymes, is an interferon-inducible protein implicated in the inhibition of replication of a broad range of RNA and DNA viruses, including dengue virus, West Nile virus, hepatitis C virus, influenza A virus, rabies virus
2
and HIV
3
,
4
. Viperin has been suggested to elicit these broad antiviral activities through interactions with a large number of functionally unrelated host and viral proteins
3
,
4
. Here we demonstrate that viperin catalyses the conversion of cytidine triphosphate (CTP) to 3ʹ-deoxy-3′,4ʹ-didehydro-CTP (ddhCTP), a previously undescribed biologically relevant molecule, via a SAM-dependent radical mechanism. We show that mammalian cells expressing viperin and macrophages stimulated with IFNα produce substantial quantities of ddhCTP. We also establish that ddhCTP acts as a chain terminator for the RNA-dependent RNA polymerases from multiple members of the Flavivirus genus, and show that ddhCTP directly inhibits replication of Zika virus in vivo. These findings suggest a partially unifying mechanism for the broad antiviral effects of viperin that is based on the intrinsic enzymatic properties of the protein and involves the generation of a naturally occurring replication-chain terminator encoded by mammalian genomes.
Viperin inhibits the replication of various viruses by catalysing the conversion of CTP to ddhCTP, which is a unique nucleotide that functions as replication-chain terminator of RNA-dependent RNA polymerases. |
|---|---|
| AbstractList | Viral infections continue to represent major challenges to public health, and an enhanced mechanistic understanding of the processes that contribute to viral life cycles is necessary for the development of new therapeutic strategies.sup.1. Viperin, a member of the radical S-adenosyl-l-methionine (SAM) superfamily of enzymes, is an interferon-inducible protein implicated in the inhibition of replication of a broad range of RNA and DNA viruses, including dengue virus, West Nile virus, hepatitis C virus, influenza A virus, rabies virus.sup.2 and HIV.sup.3,4. Viperin has been suggested to elicit these broad antiviral activities through interactions with a large number of functionally unrelated host and viral proteins.sup.3,4. Here we demonstrate that viperin catalyses the conversion of cytidine triphosphate (CTP) to 3E-deoxy-3',4E-didehydro-CTP (ddhCTP), a previously undescribed biologically relevant molecule, via a SAM-dependent radical mechanism. We show that mammalian cells expressing viperin and macrophages stimulated with IFN[alpha] produce substantial quantities of ddhCTP. We also establish that ddhCTP acts as a chain terminator for the RNA-dependent RNA polymerases from multiple members of the Flavivirus genus, and show that ddhCTP directly inhibits replication of Zika virus in vivo. These findings suggest a partially unifying mechanism for the broad antiviral effects of viperin that is based on the intrinsic enzymatic properties of the protein and involves the generation of a naturally occurring replication-chain terminator encoded by mammalian genomes. Viral infections continue to represent major challenges to public health, and an enhanced mechanistic understanding of the processes that contribute to viral life cycles is necessary for the development of new therapeutic strategies.sup.1. Viperin, a member of the radical S-adenosyl-l-methionine (SAM) superfamily of enzymes, is an interferon-inducible protein implicated in the inhibition of replication of a broad range of RNA and DNA viruses, including dengue virus, West Nile virus, hepatitis C virus, influenza A virus, rabies virus.sup.2 and HIV.sup.3,4. Viperin has been suggested to elicit these broad antiviral activities through interactions with a large number of functionally unrelated host and viral proteins.sup.3,4. Here we demonstrate that viperin catalyses the conversion of cytidine triphosphate (CTP) to 3E-deoxy-3',4E-didehydro-CTP (ddhCTP), a previously undescribed biologically relevant molecule, via a SAM-dependent radical mechanism. We show that mammalian cells expressing viperin and macrophages stimulated with IFN[alpha] produce substantial quantities of ddhCTP. We also establish that ddhCTP acts as a chain terminator for the RNA-dependent RNA polymerases from multiple members of the Flavivirus genus, and show that ddhCTP directly inhibits replication of Zika virus in vivo. These findings suggest a partially unifying mechanism for the broad antiviral effects of viperin that is based on the intrinsic enzymatic properties of the protein and involves the generation of a naturally occurring replication-chain terminator encoded by mammalian genomes. Viperin inhibits the replication of various viruses by catalysing the conversion of CTP to ddhCTP, which is a unique nucleotide that functions as replication-chain terminator of RNA-dependent RNA polymerases. Viral infections continue to represent major challenges to public health, and an enhanced mechanistic understanding of the processes that contribute to viral life cycles is necessary for the development of new therapeutic strategies . Viperin, a member of the radical S-adenosyl-L-methionine (SAM) superfamily of enzymes, is an interferon-inducible protein implicated in the inhibition of replication of a broad range of RNA and DNA viruses, including dengue virus, West Nile virus, hepatitis C virus, influenza A virus, rabies virus and HIV . Viperin has been suggested to elicit these broad antiviral activities through interactions with a large number of functionally unrelated host and viral proteins . Here we demonstrate that viperin catalyses the conversion of cytidine triphosphate (CTP) to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP), a previously undescribed biologically relevant molecule, via a SAM-dependent radical mechanism. We show that mammalian cells expressing viperin and macrophages stimulated with IFNα produce substantial quantities of ddhCTP. We also establish that ddhCTP acts as a chain terminator for the RNA-dependent RNA polymerases from multiple members of the Flavivirus genus, and show that ddhCTP directly inhibits replication of Zika virus in vivo. These findings suggest a partially unifying mechanism for the broad antiviral effects of viperin that is based on the intrinsic enzymatic properties of the protein and involves the generation of a naturally occurring replication-chain terminator encoded by mammalian genomes. Viral infections continue to represent major challenges to public health, and an enhanced mechanistic understanding of the processes that contribute to viral life cycles is necessary for the development of new therapeutic strategies 1 . Viperin, a member of the radical S -adenosyl- l -methionine (SAM) superfamily of enzymes, is an interferon-inducible protein implicated in the inhibition of replication of a broad range of RNA and DNA viruses, including dengue virus, West Nile virus, hepatitis C virus, influenza A virus, rabies virus 2 and HIV 3 , 4 . Viperin has been suggested to elicit these broad antiviral activities through interactions with a large number of functionally unrelated host and viral proteins 3 , 4 . Here we demonstrate that viperin catalyses the conversion of cytidine triphosphate (CTP) to 3ʹ-deoxy-3′,4ʹ-didehydro-CTP (ddhCTP), a previously undescribed biologically relevant molecule, via a SAM-dependent radical mechanism. We show that mammalian cells expressing viperin and macrophages stimulated with IFNα produce substantial quantities of ddhCTP. We also establish that ddhCTP acts as a chain terminator for the RNA-dependent RNA polymerases from multiple members of the Flavivirus genus, and show that ddhCTP directly inhibits replication of Zika virus in vivo. These findings suggest a partially unifying mechanism for the broad antiviral effects of viperin that is based on the intrinsic enzymatic properties of the protein and involves the generation of a naturally occurring replication-chain terminator encoded by mammalian genomes. Viperin inhibits the replication of various viruses by catalysing the conversion of CTP to ddhCTP, which is a unique nucleotide that functions as replication-chain terminator of RNA-dependent RNA polymerases. Viral infections continue to represent major public health challenges, demanding enhanced mechanistic understanding of the processes contributing to viral lifecycles for the realization of new therapeutic strategies 1 . Viperin, a member of the radical S -adenosyl-L-methionine (SAM) superfamily of enzymes, is an interferon inducible protein implicated in inhibiting the replication of a remarkable range of RNA and DNA viruses, including dengue virus, West Nile virus, hepatitis C virus, influenza A virus, rabies virus 2 and HIV 3 , 4 . Viperin has been suggested to elicit these broad antiviral activities through interactions with a large number of functionally unrelated host and viral proteins 3 , 4 . In contrast, herein, we demonstrate that viperin catalyzes the conversion of cytidine triphosphate (CTP) to 3′-deoxy-3′,4′-didehydro-CTP (ddhCTP), a previously undescribed biologically relevant molecule, via a SAM-dependent radical mechanism. We show that mammalian cells expressing viperin, and macrophages stimulated with IFN-α, produce substantial quantities of ddhCTP. We also establish that ddhCTP acts as a chain terminator for the RNA-dependent RNA-polymerases from multiple members of the flavivirus family, and present evidence that ddhCTP directly inhibits in vivo replication of ZIKA virus. These findings suggest a partially unifying mechanism, based on intrinsic catalytic/enzymatic properties, for the broad antiviral effects of viperin, which involves the generation of a naturally occurring replication chain terminator encoded by mammalian genomes. Viral infections continue to represent major challenges to public health, and an enhanced mechanistic understanding of the processes that contribute to viral life cycles is necessary for the development of new therapeutic strategies1. Viperin, a member of the radical S-adenosyl-L-methionine (SAM) superfamily of enzymes, is an interferon-inducible protein implicated in the inhibition of replication of a broad range of RNA and DNA viruses, including dengue virus, West Nile virus, hepatitis C virus, influenza A virus, rabies virus2 and HIV3,4. Viperin has been suggested to elicit these broad antiviral activities through interactions with a large number of functionally unrelated host and viral proteins3,4. Here we demonstrate that viperin catalyses the conversion of cytidine triphosphate (CTP) to 3′-deoxy-3′,4′-didehydro-CTP (ddhCTP), a previously undescribed biologically relevant molecule, via a SAM-dependent radical mechanism. We show that mammalian cells expressing viperin and macrophages stimulated with IFNα produce substantial quantities of ddhCTP. We also establish that ddhCTP acts as a chain terminator for the RNA-dependent RNA polymerases from multiple members of the Flavivirus genus, and show that ddhCTP directly inhibits replication of Zika virus in vivo. These findings suggest a partially unifying mechanism for the broad antiviral effects of viperin that is based on the intrinsic enzymatic properties of the protein and involves the generation of a naturally occurring replication-chain terminator encoded by mammalian genomes. Viral infections continue to represent major challenges to public health, and an enhanced mechanistic understanding of the processes that contribute to viral life cycles is necessary for the development of new therapeutic strategies 1 . Viperin, a member of the radical S-adenosyl-L-methionine (SAM) superfamily of enzymes, is an interferon-inducible protein implicated in the inhibition of replication of a broad range of RNA and DNA viruses, including dengue virus, West Nile virus, hepatitis C virus, influenza A virus, rabies virus 2 and HIV3,4. Viperin has been suggested to elicit these broad antiviral activities through interactions with a large number of functionally unrelated host and viral proteins3,4. Here we demonstrate that viperin catalyses the conversion of cytidine triphosphate (CTP) to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP), a previously undescribed biologically relevant molecule, via a SAM-dependent radical mechanism. We show that mammalian cells expressing viperin and macrophages stimulated with IFNα produce substantial quantities of ddhCTP. We also establish that ddhCTP acts as a chain terminator for the RNA-dependent RNA polymerases from multiple members of the Flavivirus genus, and show that ddhCTP directly inhibits replication of Zika virus in vivo. These findings suggest a partially unifying mechanism for the broad antiviral effects of viperin that is based on the intrinsic enzymatic properties of the protein and involves the generation of a naturally occurring replication-chain terminator encoded by mammalian genomes.Viral infections continue to represent major challenges to public health, and an enhanced mechanistic understanding of the processes that contribute to viral life cycles is necessary for the development of new therapeutic strategies 1 . Viperin, a member of the radical S-adenosyl-L-methionine (SAM) superfamily of enzymes, is an interferon-inducible protein implicated in the inhibition of replication of a broad range of RNA and DNA viruses, including dengue virus, West Nile virus, hepatitis C virus, influenza A virus, rabies virus 2 and HIV3,4. Viperin has been suggested to elicit these broad antiviral activities through interactions with a large number of functionally unrelated host and viral proteins3,4. Here we demonstrate that viperin catalyses the conversion of cytidine triphosphate (CTP) to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP), a previously undescribed biologically relevant molecule, via a SAM-dependent radical mechanism. We show that mammalian cells expressing viperin and macrophages stimulated with IFNα produce substantial quantities of ddhCTP. We also establish that ddhCTP acts as a chain terminator for the RNA-dependent RNA polymerases from multiple members of the Flavivirus genus, and show that ddhCTP directly inhibits replication of Zika virus in vivo. These findings suggest a partially unifying mechanism for the broad antiviral effects of viperin that is based on the intrinsic enzymatic properties of the protein and involves the generation of a naturally occurring replication-chain terminator encoded by mammalian genomes. |
| Audience | Academic |
| Author | Gizzi, Anthony S. Cameron, Craig E. Love, James D. Garforth, Scott J. Arnold, Jamie J. Jangra, Rohit K. Bresnick, Anne R. Grove, Tyler L. Dulyaninova, Natalya G. Almo, Steven C. Du, Quan Jose, Joyce Cahill, Sean M. Chandran, Kartik |
| AuthorAffiliation | 1 Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA 4 Institute for Protein Innovation. Boston. MA, USA 2 Department Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA 5 Department of Department of Microbiology & Immunology, Albert Einstein College of Medicine, Bronx, NY 10461, USA |
| AuthorAffiliation_xml | – name: 2 Department Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA – name: 4 Institute for Protein Innovation. Boston. MA, USA – name: 5 Department of Department of Microbiology & Immunology, Albert Einstein College of Medicine, Bronx, NY 10461, USA – name: 1 Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA |
| Author_xml | – sequence: 1 givenname: Anthony S. surname: Gizzi fullname: Gizzi, Anthony S. organization: Department of Biochemistry, Albert Einstein College of Medicine – sequence: 2 givenname: Tyler L. surname: Grove fullname: Grove, Tyler L. email: tyler.grove@einstein.yu.edu organization: Department of Biochemistry, Albert Einstein College of Medicine – sequence: 3 givenname: Jamie J. surname: Arnold fullname: Arnold, Jamie J. organization: Department of Biochemistry and Molecular Biology, The Pennsylvania State University – sequence: 4 givenname: Joyce surname: Jose fullname: Jose, Joyce organization: Department of Biochemistry and Molecular Biology, The Pennsylvania State University – sequence: 5 givenname: Rohit K. surname: Jangra fullname: Jangra, Rohit K. organization: Department of Microbiology and Immunology, Albert Einstein College of Medicine – sequence: 6 givenname: Scott J. surname: Garforth fullname: Garforth, Scott J. organization: Department of Biochemistry, Albert Einstein College of Medicine – sequence: 7 givenname: Quan surname: Du fullname: Du, Quan organization: Department of Biochemistry, Albert Einstein College of Medicine – sequence: 8 givenname: Sean M. surname: Cahill fullname: Cahill, Sean M. organization: Department of Biochemistry, Albert Einstein College of Medicine – sequence: 9 givenname: Natalya G. surname: Dulyaninova fullname: Dulyaninova, Natalya G. organization: Department of Biochemistry, Albert Einstein College of Medicine – sequence: 10 givenname: James D. surname: Love fullname: Love, James D. organization: Institute for Protein Innovation – sequence: 11 givenname: Kartik surname: Chandran fullname: Chandran, Kartik organization: Department of Microbiology and Immunology, Albert Einstein College of Medicine – sequence: 12 givenname: Anne R. surname: Bresnick fullname: Bresnick, Anne R. organization: Department of Biochemistry, Albert Einstein College of Medicine – sequence: 13 givenname: Craig E. surname: Cameron fullname: Cameron, Craig E. organization: Department of Biochemistry and Molecular Biology, The Pennsylvania State University – sequence: 14 givenname: Steven C. surname: Almo fullname: Almo, Steven C. email: steve.almo@einstein.yu.edu organization: Department of Biochemistry, Albert Einstein College of Medicine, Institute for Protein Innovation |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29925952$$D View this record in MEDLINE/PubMed |
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| Title | A naturally occurring antiviral ribonucleotide encoded by the human genome |
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