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| | ==GP1 receptor-binding domain from Whitewater Arroyo mammarenavirus== | | ==GP1 receptor-binding domain from Whitewater Arroyo mammarenavirus== |
| - | <StructureSection load='5nsj' size='340' side='right' caption='[[5nsj]], [[Resolution|resolution]] 2.25Å' scene=''> | + | <StructureSection load='5nsj' size='340' side='right'caption='[[5nsj]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nsj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Wwav Wwav]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NSJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NSJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nsj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mammarenavirus_whitewaterense Mammarenavirus whitewaterense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NSJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.249Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GPC, GP-C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46919 WWAV])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nsj OCA], [http://pdbe.org/5nsj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nsj RCSB], [http://www.ebi.ac.uk/pdbsum/5nsj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nsj ProSAT]</span></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=5nsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nsj OCA], [https://pdbe.org/5nsj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nsj RCSB], [https://www.ebi.ac.uk/pdbsum/5nsj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nsj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLYC_WWAVU GLYC_WWAVU]] Stable signal peptide (SSP) is cleaved but is apparently retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational cleavage of GP1 and GP2, glycoprotein transport to the cell plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion (By similarity). Glycoprotein G1 mediates virus attachment to host receptor. This interaction leads to virion entry into the host cell through the endosomal pathway (By similarity). Glycoprotein G2 is a class I viral fusion protein, that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversable conformational changes induced upon acidification in the endosome (By similarity). | + | [https://www.uniprot.org/uniprot/GLYC_WWAVU GLYC_WWAVU] Stable signal peptide (SSP) is cleaved but is apparently retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational cleavage of GP1 and GP2, glycoprotein transport to the cell plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion (By similarity). Glycoprotein G1 mediates virus attachment to host receptor. This interaction leads to virion entry into the host cell through the endosomal pathway (By similarity). Glycoprotein G2 is a class I viral fusion protein, that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversable conformational changes induced upon acidification in the endosome (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5nsj" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5nsj" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Glycoprotein GP 3D structures|Glycoprotein GP 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Wwav]] | + | [[Category: Large Structures]] |
| - | [[Category: Diskin, R]] | + | [[Category: Mammarenavirus whitewaterense]] |
| - | [[Category: Shani, O]] | + | [[Category: Diskin R]] |
| - | [[Category: Shimon, A]] | + | [[Category: Shani O]] |
| - | [[Category: Receptor binding domain]] | + | [[Category: Shimon A]] |
| - | [[Category: Viral glycoprotein]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
GLYC_WWAVU Stable signal peptide (SSP) is cleaved but is apparently retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational cleavage of GP1 and GP2, glycoprotein transport to the cell plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion (By similarity). Glycoprotein G1 mediates virus attachment to host receptor. This interaction leads to virion entry into the host cell through the endosomal pathway (By similarity). Glycoprotein G2 is a class I viral fusion protein, that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversable conformational changes induced upon acidification in the endosome (By similarity).
Publication Abstract from PubMed
Whitewater Arroyo virus belongs to the "New World" group of mammarenaviruses that reside in rodent reservoirs and are prevalent in North and South Americas. Clades B and A/B of New World mammarenaviruses use transferrin receptor 1 (TfR1) for entry. While all of these viruses use rodent-derived TfR1 orthologs, some can also use the human-TfR1 and thereby infect humans. Although we have structural information for TfR1 recognition by pathogenic virus, we do not know what the structural differences are between the receptor-binding domains of pathogenic and non-pathogenic viruses that allow some but not all viruses to utilize the human receptor for entry. The poor understanding of the molecular determinants of mammarenavirus host range, and thus pathogenicity, is partly due to the low sequence similarity between the receptor-binding domains from these viruses and the limited available structural information that preclude the use of modeling approaches. Here we present the first crystal structure of a receptor-binding domain of a non-pathogenic clade A/B mammarenavirus. This structure reveals the magnitude of structural differences within the receptor-binding domains of TfR1-tropic viruses. Our structural and sequence analyses indicate that the same structural incompatibilities with the human receptor equally affect both pathogenic and non-pathogenic mammarenaviruses. Non-pathogenic viruses do not have specific structural elements that prevent them from using the human receptor. Instead, the ability to utilize the human receptor directly depends on the extent of weak interactions throughout the receptor-binding site that in some viruses are sufficiently strong to overcome the structural incompatibilities.
Structural Basis for Receptor Selectivity by the Whitewater Arroyo Mammarenavirus.,Shimon A, Shani O, Diskin R J Mol Biol. 2017 Jul 21. pii: S0022-2836(17)30348-0. doi:, 10.1016/j.jmb.2017.07.011. PMID:28736175[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shimon A, Shani O, Diskin R. Structural Basis for Receptor Selectivity by the Whitewater Arroyo Mammarenavirus. J Mol Biol. 2017 Jul 21. pii: S0022-2836(17)30348-0. doi:, 10.1016/j.jmb.2017.07.011. PMID:28736175 doi:http://dx.doi.org/10.1016/j.jmb.2017.07.011
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