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Evidence that vaccinia virulence factor E3L binds to Z-DNA in vivo : Implications for development of a therapy for poxvirus infection
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
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| Personen und Körperschaften: | , , , , |
| In: | Proceedings of the National Academy of Sciences, 101, 2004, 6, S. 1514-1518 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
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| Schlagwörter: |
| author_facet |
Kim, Yang-Gyun Lowenhaupt, Ky Oh, Doo-Byoung Kim, Kyeong Kyu Rich, Alexander Kim, Yang-Gyun Lowenhaupt, Ky Oh, Doo-Byoung Kim, Kyeong Kyu Rich, Alexander |
|---|---|
| author |
Kim, Yang-Gyun Lowenhaupt, Ky Oh, Doo-Byoung Kim, Kyeong Kyu Rich, Alexander |
| spellingShingle |
Kim, Yang-Gyun Lowenhaupt, Ky Oh, Doo-Byoung Kim, Kyeong Kyu Rich, Alexander Proceedings of the National Academy of Sciences Evidence that vaccinia virulence factor E3L binds to Z-DNA in vivo : Implications for development of a therapy for poxvirus infection Multidisciplinary |
| author_sort |
kim, yang-gyun |
| spelling |
Kim, Yang-Gyun Lowenhaupt, Ky Oh, Doo-Byoung Kim, Kyeong Kyu Rich, Alexander 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.0308260100 <jats:p> The E3L gene product found in all poxviruses is required for the lethality of mice in vaccinia virus infection. Both the C-terminal region, consisting of a double-stranded RNA-binding motif, and the N-terminal region (vZ <jats:sub>E3L</jats:sub> ), which is similar to the Zα family of Z-DNA-binding proteins, are required for infection. It has recently been demonstrated that the function of the N-terminal domain depends on its ability to bind Z-DNA; Z-DNA-binding domains from unrelated mammalian proteins fully complement an N-terminal deletion of E3L. Mutations that decrease affinity for Z-DNA have similar effects in decreasing pathogenicity. Compounds that block the Z-DNA-binding activity of E3L may also limit infection by the poxvirus. Here we show both an <jats:italic>in vitro</jats:italic> and an <jats:italic>in vivo</jats:italic> assay with the potential to be used in screening for such compounds. Using a conformation-specific yeast one-hybrid assay, we compared the results for Z-DNA binding of vZ <jats:sub>E3L</jats:sub> with those for human Zβ <jats:sub>ADAR1</jats:sub> , a peptide that has similarity to the Zα motif but does not bind Z-DNA, and with a mutant of hZβ <jats:sub>ADAR1</jats:sub> , which binds Z-DNA. The results suggest that this system can be used for high-throughput screening. </jats:p> Evidence that vaccinia virulence factor E3L binds to Z-DNA <i>in vivo</i> : Implications for development of a therapy for poxvirus infection Proceedings of the National Academy of Sciences |
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| title |
Evidence that vaccinia virulence factor E3L binds to Z-DNA in vivo : Implications for development of a therapy for poxvirus infection |
| title_unstemmed |
Evidence that vaccinia virulence factor E3L binds to Z-DNA in vivo : Implications for development of a therapy for poxvirus infection |
| title_full |
Evidence that vaccinia virulence factor E3L binds to Z-DNA in vivo : Implications for development of a therapy for poxvirus infection |
| title_fullStr |
Evidence that vaccinia virulence factor E3L binds to Z-DNA in vivo : Implications for development of a therapy for poxvirus infection |
| title_full_unstemmed |
Evidence that vaccinia virulence factor E3L binds to Z-DNA in vivo : Implications for development of a therapy for poxvirus infection |
| title_short |
Evidence that vaccinia virulence factor E3L binds to Z-DNA in vivo : Implications for development of a therapy for poxvirus infection |
| title_sort |
evidence that vaccinia virulence factor e3l binds to z-dna
<i>in vivo</i>
: implications for development of a therapy for poxvirus infection |
| topic |
Multidisciplinary |
| url |
http://dx.doi.org/10.1073/pnas.0308260100 |
| publishDate |
2004 |
| physical |
1514-1518 |
| description |
<jats:p>
The E3L gene product found in all poxviruses is required for the lethality of mice in vaccinia virus infection. Both the C-terminal region, consisting of a double-stranded RNA-binding motif, and the N-terminal region (vZ
<jats:sub>E3L</jats:sub>
), which is similar to the Zα family of Z-DNA-binding proteins, are required for infection. It has recently been demonstrated that the function of the N-terminal domain depends on its ability to bind Z-DNA; Z-DNA-binding domains from unrelated mammalian proteins fully complement an N-terminal deletion of E3L. Mutations that decrease affinity for Z-DNA have similar effects in decreasing pathogenicity. Compounds that block the Z-DNA-binding activity of E3L may also limit infection by the poxvirus. Here we show both an
<jats:italic>in vitro</jats:italic>
and an
<jats:italic>in vivo</jats:italic>
assay with the potential to be used in screening for such compounds. Using a conformation-specific yeast one-hybrid assay, we compared the results for Z-DNA binding of vZ
<jats:sub>E3L</jats:sub>
with those for human Zβ
<jats:sub>ADAR1</jats:sub>
, a peptide that has similarity to the Zα motif but does not bind Z-DNA, and with a mutant of hZβ
<jats:sub>ADAR1</jats:sub>
, which binds Z-DNA. The results suggest that this system can be used for high-throughput screening.
</jats:p> |
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| author | Kim, Yang-Gyun, Lowenhaupt, Ky, Oh, Doo-Byoung, Kim, Kyeong Kyu, Rich, Alexander |
| author_facet | Kim, Yang-Gyun, Lowenhaupt, Ky, Oh, Doo-Byoung, Kim, Kyeong Kyu, Rich, Alexander, Kim, Yang-Gyun, Lowenhaupt, Ky, Oh, Doo-Byoung, Kim, Kyeong Kyu, Rich, Alexander |
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| description | <jats:p> The E3L gene product found in all poxviruses is required for the lethality of mice in vaccinia virus infection. Both the C-terminal region, consisting of a double-stranded RNA-binding motif, and the N-terminal region (vZ <jats:sub>E3L</jats:sub> ), which is similar to the Zα family of Z-DNA-binding proteins, are required for infection. It has recently been demonstrated that the function of the N-terminal domain depends on its ability to bind Z-DNA; Z-DNA-binding domains from unrelated mammalian proteins fully complement an N-terminal deletion of E3L. Mutations that decrease affinity for Z-DNA have similar effects in decreasing pathogenicity. Compounds that block the Z-DNA-binding activity of E3L may also limit infection by the poxvirus. Here we show both an <jats:italic>in vitro</jats:italic> and an <jats:italic>in vivo</jats:italic> assay with the potential to be used in screening for such compounds. Using a conformation-specific yeast one-hybrid assay, we compared the results for Z-DNA binding of vZ <jats:sub>E3L</jats:sub> with those for human Zβ <jats:sub>ADAR1</jats:sub> , a peptide that has similarity to the Zα motif but does not bind Z-DNA, and with a mutant of hZβ <jats:sub>ADAR1</jats:sub> , which binds Z-DNA. The results suggest that this system can be used for high-throughput screening. </jats:p> |
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| imprint | Proceedings of the National Academy of Sciences, 2004 |
| imprint_str_mv | Proceedings of the National Academy of Sciences, 2004 |
| institution | DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161 |
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| language | English |
| last_indexed | 2024-03-01T15:17:50.152Z |
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| physical | 1514-1518 |
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| spelling | Kim, Yang-Gyun Lowenhaupt, Ky Oh, Doo-Byoung Kim, Kyeong Kyu Rich, Alexander 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.0308260100 <jats:p> The E3L gene product found in all poxviruses is required for the lethality of mice in vaccinia virus infection. Both the C-terminal region, consisting of a double-stranded RNA-binding motif, and the N-terminal region (vZ <jats:sub>E3L</jats:sub> ), which is similar to the Zα family of Z-DNA-binding proteins, are required for infection. It has recently been demonstrated that the function of the N-terminal domain depends on its ability to bind Z-DNA; Z-DNA-binding domains from unrelated mammalian proteins fully complement an N-terminal deletion of E3L. Mutations that decrease affinity for Z-DNA have similar effects in decreasing pathogenicity. Compounds that block the Z-DNA-binding activity of E3L may also limit infection by the poxvirus. Here we show both an <jats:italic>in vitro</jats:italic> and an <jats:italic>in vivo</jats:italic> assay with the potential to be used in screening for such compounds. Using a conformation-specific yeast one-hybrid assay, we compared the results for Z-DNA binding of vZ <jats:sub>E3L</jats:sub> with those for human Zβ <jats:sub>ADAR1</jats:sub> , a peptide that has similarity to the Zα motif but does not bind Z-DNA, and with a mutant of hZβ <jats:sub>ADAR1</jats:sub> , which binds Z-DNA. The results suggest that this system can be used for high-throughput screening. </jats:p> Evidence that vaccinia virulence factor E3L binds to Z-DNA <i>in vivo</i> : Implications for development of a therapy for poxvirus infection Proceedings of the National Academy of Sciences |
| spellingShingle | Kim, Yang-Gyun, Lowenhaupt, Ky, Oh, Doo-Byoung, Kim, Kyeong Kyu, Rich, Alexander, Proceedings of the National Academy of Sciences, Evidence that vaccinia virulence factor E3L binds to Z-DNA in vivo : Implications for development of a therapy for poxvirus infection, Multidisciplinary |
| title | Evidence that vaccinia virulence factor E3L binds to Z-DNA in vivo : Implications for development of a therapy for poxvirus infection |
| title_full | Evidence that vaccinia virulence factor E3L binds to Z-DNA in vivo : Implications for development of a therapy for poxvirus infection |
| title_fullStr | Evidence that vaccinia virulence factor E3L binds to Z-DNA in vivo : Implications for development of a therapy for poxvirus infection |
| title_full_unstemmed | Evidence that vaccinia virulence factor E3L binds to Z-DNA in vivo : Implications for development of a therapy for poxvirus infection |
| title_short | Evidence that vaccinia virulence factor E3L binds to Z-DNA in vivo : Implications for development of a therapy for poxvirus infection |
| title_sort | evidence that vaccinia virulence factor e3l binds to z-dna <i>in vivo</i> : implications for development of a therapy for poxvirus infection |
| title_unstemmed | Evidence that vaccinia virulence factor E3L binds to Z-DNA in vivo : Implications for development of a therapy for poxvirus infection |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.0308260100 |