6oat: Difference between revisions
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==Structure of the Ganjam virus OTU bound to sheep ISG15== | |||
<StructureSection load='6oat' size='340' side='right'caption='[[6oat]], [[Resolution|resolution]] 3.17Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6oat]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ganjam_virus Ganjam virus] and [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OAT FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.17Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AYE:PROP-2-EN-1-AMINE'>AYE</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6oat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oat OCA], [https://pdbe.org/6oat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oat RCSB], [https://www.ebi.ac.uk/pdbsum/6oat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oat ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A191KWA2_9VIRU A0A191KWA2_9VIRU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Tick-borne nairoviruses (order Bunyavirales) encode an ovarian tumor domain protease (OTU) that suppresses the innate immune response by reversing the post-translational modification of proteins by ubiquitin (Ub) and interferon-stimulated gene product 15 (ISG15). Ub is highly conserved across eukaryotes, whereas ISG15 is only present in vertebrates and shows substantial sequence diversity. Prior attempts to address the effect of ISG15 diversity on viral protein-ISG15 interactions have focused on only a single species' ISG15 or a limited selection of nairovirus OTUs. To gain a more complete perspective of OTU-ISG15 interactions, we biochemically assessed the relative activities of 14 diverse nairovirus OTUs for 12 species' ISG15 and found that ISG15 activity is predominantly restricted to particular nairovirus lineages reflecting, in general, known virus-host associations. To uncover the underlying molecular factors driving OTUs affinity for ISG15, X-ray crystal structures of Kupe virus and Ganjam virus OTUs bound to sheep ISG15 were solved and compared to complexes of Crimean-Congo hemorrhagic fever virus and Erve virus OTUs bound to human and mouse ISG15, respectively. Through mutational and structural analysis seven residues in ISG15 were identified that predominantly influence ISG15 species specificity among nairovirus OTUs. Additionally, OTU residues were identified that influence ISG15 preference, suggesting the potential for viral OTUs to adapt to different host ISG15s. These findings provide a foundation to further develop research methods to trace nairovirus-host relationships and delineate the full impact of ISG15 diversity on nairovirus infection. | |||
Determining the molecular drivers of species-specific interferon-stimulated gene product 15 interactions with nairovirus ovarian tumor domain proteases.,Dzimianski JV, Scholte FEM, Williams IL, Langley C, Freitas BT, Spengler JR, Bergeron E, Pegan SD PLoS One. 2019 Dec 23;14(12):e0226415. doi: 10.1371/journal.pone.0226415., eCollection 2019. PMID:31869347<ref>PMID:31869347</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Dzimianski | <div class="pdbe-citations 6oat" style="background-color:#fffaf0;"></div> | ||
[[Category: Pegan | |||
[[Category: Williams | ==See Also== | ||
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ganjam virus]] | |||
[[Category: Large Structures]] | |||
[[Category: Ovis aries]] | |||
[[Category: Dzimianski JV]] | |||
[[Category: Pegan SD]] | |||
[[Category: Williams IL]] | |||
Latest revision as of 10:07, 11 October 2023
Structure of the Ganjam virus OTU bound to sheep ISG15Structure of the Ganjam virus OTU bound to sheep ISG15
Structural highlights
FunctionPublication Abstract from PubMedTick-borne nairoviruses (order Bunyavirales) encode an ovarian tumor domain protease (OTU) that suppresses the innate immune response by reversing the post-translational modification of proteins by ubiquitin (Ub) and interferon-stimulated gene product 15 (ISG15). Ub is highly conserved across eukaryotes, whereas ISG15 is only present in vertebrates and shows substantial sequence diversity. Prior attempts to address the effect of ISG15 diversity on viral protein-ISG15 interactions have focused on only a single species' ISG15 or a limited selection of nairovirus OTUs. To gain a more complete perspective of OTU-ISG15 interactions, we biochemically assessed the relative activities of 14 diverse nairovirus OTUs for 12 species' ISG15 and found that ISG15 activity is predominantly restricted to particular nairovirus lineages reflecting, in general, known virus-host associations. To uncover the underlying molecular factors driving OTUs affinity for ISG15, X-ray crystal structures of Kupe virus and Ganjam virus OTUs bound to sheep ISG15 were solved and compared to complexes of Crimean-Congo hemorrhagic fever virus and Erve virus OTUs bound to human and mouse ISG15, respectively. Through mutational and structural analysis seven residues in ISG15 were identified that predominantly influence ISG15 species specificity among nairovirus OTUs. Additionally, OTU residues were identified that influence ISG15 preference, suggesting the potential for viral OTUs to adapt to different host ISG15s. These findings provide a foundation to further develop research methods to trace nairovirus-host relationships and delineate the full impact of ISG15 diversity on nairovirus infection. Determining the molecular drivers of species-specific interferon-stimulated gene product 15 interactions with nairovirus ovarian tumor domain proteases.,Dzimianski JV, Scholte FEM, Williams IL, Langley C, Freitas BT, Spengler JR, Bergeron E, Pegan SD PLoS One. 2019 Dec 23;14(12):e0226415. doi: 10.1371/journal.pone.0226415., eCollection 2019. PMID:31869347[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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