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PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication
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| Zeitschriftentitel: | Journal of Cell Science |
|---|---|
| Personen und Körperschaften: | , , , , , , , , |
| In: | Journal of Cell Science, 124, 2011, 2, S. 280-291 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
The Company of Biologists
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| Schlagwörter: |
| author_facet |
Cuchet, Delphine Sykes, Amanda Nicolas, Armel Orr, Anne Murray, Jill Sirma, Hüseyin Heeren, Joerg Bartelt, Alexander Everett, Roger D. Cuchet, Delphine Sykes, Amanda Nicolas, Armel Orr, Anne Murray, Jill Sirma, Hüseyin Heeren, Joerg Bartelt, Alexander Everett, Roger D. |
|---|---|
| author |
Cuchet, Delphine Sykes, Amanda Nicolas, Armel Orr, Anne Murray, Jill Sirma, Hüseyin Heeren, Joerg Bartelt, Alexander Everett, Roger D. |
| spellingShingle |
Cuchet, Delphine Sykes, Amanda Nicolas, Armel Orr, Anne Murray, Jill Sirma, Hüseyin Heeren, Joerg Bartelt, Alexander Everett, Roger D. Journal of Cell Science PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication Cell Biology |
| author_sort |
cuchet, delphine |
| spelling |
Cuchet, Delphine Sykes, Amanda Nicolas, Armel Orr, Anne Murray, Jill Sirma, Hüseyin Heeren, Joerg Bartelt, Alexander Everett, Roger D. 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.075390 <jats:p>Intrinsic antiviral resistance mediated by constitutively expressed cellular proteins is one arm of defence against virus infection. Promyelocytic leukaemia nuclear bodies (PML-NBs, also known as ND10) contribute to host restriction of herpes simplex virus type 1 (HSV-1) replication via mechanisms that are counteracted by viral regulatory protein ICP0. ND10 assembly is dependent on PML, which comprises several different isoforms, and depletion of all PML isoforms decreases cellular resistance to ICP0-null mutant HSV-1. We report that individual expression of PML isoforms I and II partially reverses the increase in ICP0-null mutant HSV-1 plaque formation that occurs in PML-depleted cells. This activity of PML isoform I is dependent on SUMO modification, its SUMO interaction motif (SIM), and each element of its TRIM domain. Detailed analysis revealed that the punctate foci formed by individual PML isoforms differ subtly from normal ND10 in terms of composition and/or Sp100 modification. Surprisingly, deletion of the SIM motif from PML isoform I resulted in increased colocalisation with other major ND10 components in cells lacking endogenous PML. Our observations suggest that complete functionality of PML is dependent on isoform-specific C-terminal sequences acting in concert.</jats:p> PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication Journal of Cell Science |
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The Company of Biologists, 2011 |
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The Company of Biologists, 2011 |
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Journal of Cell Science |
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| title |
PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication |
| title_unstemmed |
PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication |
| title_full |
PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication |
| title_fullStr |
PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication |
| title_full_unstemmed |
PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication |
| title_short |
PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication |
| title_sort |
pml isoforms i and ii participate in pml-dependent restriction of hsv-1 replication |
| topic |
Cell Biology |
| url |
http://dx.doi.org/10.1242/jcs.075390 |
| publishDate |
2011 |
| physical |
280-291 |
| description |
<jats:p>Intrinsic antiviral resistance mediated by constitutively expressed cellular proteins is one arm of defence against virus infection. Promyelocytic leukaemia nuclear bodies (PML-NBs, also known as ND10) contribute to host restriction of herpes simplex virus type 1 (HSV-1) replication via mechanisms that are counteracted by viral regulatory protein ICP0. ND10 assembly is dependent on PML, which comprises several different isoforms, and depletion of all PML isoforms decreases cellular resistance to ICP0-null mutant HSV-1. We report that individual expression of PML isoforms I and II partially reverses the increase in ICP0-null mutant HSV-1 plaque formation that occurs in PML-depleted cells. This activity of PML isoform I is dependent on SUMO modification, its SUMO interaction motif (SIM), and each element of its TRIM domain. Detailed analysis revealed that the punctate foci formed by individual PML isoforms differ subtly from normal ND10 in terms of composition and/or Sp100 modification. Surprisingly, deletion of the SIM motif from PML isoform I resulted in increased colocalisation with other major ND10 components in cells lacking endogenous PML. Our observations suggest that complete functionality of PML is dependent on isoform-specific C-terminal sequences acting in concert.</jats:p> |
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| author | Cuchet, Delphine, Sykes, Amanda, Nicolas, Armel, Orr, Anne, Murray, Jill, Sirma, Hüseyin, Heeren, Joerg, Bartelt, Alexander, Everett, Roger D. |
| author_facet | Cuchet, Delphine, Sykes, Amanda, Nicolas, Armel, Orr, Anne, Murray, Jill, Sirma, Hüseyin, Heeren, Joerg, Bartelt, Alexander, Everett, Roger D., Cuchet, Delphine, Sykes, Amanda, Nicolas, Armel, Orr, Anne, Murray, Jill, Sirma, Hüseyin, Heeren, Joerg, Bartelt, Alexander, Everett, Roger D. |
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| description | <jats:p>Intrinsic antiviral resistance mediated by constitutively expressed cellular proteins is one arm of defence against virus infection. Promyelocytic leukaemia nuclear bodies (PML-NBs, also known as ND10) contribute to host restriction of herpes simplex virus type 1 (HSV-1) replication via mechanisms that are counteracted by viral regulatory protein ICP0. ND10 assembly is dependent on PML, which comprises several different isoforms, and depletion of all PML isoforms decreases cellular resistance to ICP0-null mutant HSV-1. We report that individual expression of PML isoforms I and II partially reverses the increase in ICP0-null mutant HSV-1 plaque formation that occurs in PML-depleted cells. This activity of PML isoform I is dependent on SUMO modification, its SUMO interaction motif (SIM), and each element of its TRIM domain. Detailed analysis revealed that the punctate foci formed by individual PML isoforms differ subtly from normal ND10 in terms of composition and/or Sp100 modification. Surprisingly, deletion of the SIM motif from PML isoform I resulted in increased colocalisation with other major ND10 components in cells lacking endogenous PML. Our observations suggest that complete functionality of PML is dependent on isoform-specific C-terminal sequences acting in concert.</jats:p> |
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| imprint | The Company of Biologists, 2011 |
| imprint_str_mv | The Company of Biologists, 2011 |
| institution | DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3 |
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| spelling | Cuchet, Delphine Sykes, Amanda Nicolas, Armel Orr, Anne Murray, Jill Sirma, Hüseyin Heeren, Joerg Bartelt, Alexander Everett, Roger D. 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.075390 <jats:p>Intrinsic antiviral resistance mediated by constitutively expressed cellular proteins is one arm of defence against virus infection. Promyelocytic leukaemia nuclear bodies (PML-NBs, also known as ND10) contribute to host restriction of herpes simplex virus type 1 (HSV-1) replication via mechanisms that are counteracted by viral regulatory protein ICP0. ND10 assembly is dependent on PML, which comprises several different isoforms, and depletion of all PML isoforms decreases cellular resistance to ICP0-null mutant HSV-1. We report that individual expression of PML isoforms I and II partially reverses the increase in ICP0-null mutant HSV-1 plaque formation that occurs in PML-depleted cells. This activity of PML isoform I is dependent on SUMO modification, its SUMO interaction motif (SIM), and each element of its TRIM domain. Detailed analysis revealed that the punctate foci formed by individual PML isoforms differ subtly from normal ND10 in terms of composition and/or Sp100 modification. Surprisingly, deletion of the SIM motif from PML isoform I resulted in increased colocalisation with other major ND10 components in cells lacking endogenous PML. Our observations suggest that complete functionality of PML is dependent on isoform-specific C-terminal sequences acting in concert.</jats:p> PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication Journal of Cell Science |
| spellingShingle | Cuchet, Delphine, Sykes, Amanda, Nicolas, Armel, Orr, Anne, Murray, Jill, Sirma, Hüseyin, Heeren, Joerg, Bartelt, Alexander, Everett, Roger D., Journal of Cell Science, PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication, Cell Biology |
| title | PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication |
| title_full | PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication |
| title_fullStr | PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication |
| title_full_unstemmed | PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication |
| title_short | PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication |
| title_sort | pml isoforms i and ii participate in pml-dependent restriction of hsv-1 replication |
| title_unstemmed | PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication |
| topic | Cell Biology |
| url | http://dx.doi.org/10.1242/jcs.075390 |