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7sej
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7sej is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | The entry | + | ==Structure-based design of prefusion-stabilized human metapneumovirus fusion proteins== |
| + | <StructureSection load='7sej' size='340' side='right'caption='[[7sej]], [[Resolution|resolution]] 2.51Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7sej]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_metapneumovirus Human metapneumovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SEJ 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]] 2.51Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=7sej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sej OCA], [https://pdbe.org/7sej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sej RCSB], [https://www.ebi.ac.uk/pdbsum/7sej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sej ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/H6X1Z0_9MONO H6X1Z0_9MONO] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The human metapneumovirus (hMPV) fusion (F) protein is essential for viral entry and is a key target of neutralizing antibodies and vaccine development. The prefusion conformation is thought to be the optimal vaccine antigen, but previously described prefusion F proteins expressed poorly and were not well stabilized. Here, we use structures of hMPV F to guide the design of 42 variants containing stabilizing substitutions. Through combinatorial addition of disulfide bonds, cavity-filling substitutions, and improved electrostatic interactions, we describe a prefusion-stabilized F protein (DS-CavEs2) that expresses at 15 mg/L and has a melting temperature of 71.9 degrees C. Crystal structures of two prefusion-stabilized hMPV F variants reveal that antigenic surfaces are largely unperturbed. Importantly, immunization of mice with DS-CavEs2 elicits significantly higher neutralizing antibody titers against hMPV A1 and B1 viruses than postfusion F. The improved properties of DS-CavEs2 will advance the development of hMPV vaccines and the isolation of therapeutic antibodies. | ||
| - | + | Structure-based design of prefusion-stabilized human metapneumovirus fusion proteins.,Hsieh CL, Rush SA, Palomo C, Chou CW, Pickens W, Mas V, McLellan JS Nat Commun. 2022 Mar 14;13(1):1299. doi: 10.1038/s41467-022-28931-3. PMID:35288548<ref>PMID:35288548</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7sej" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human metapneumovirus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hsieh C-L]] | ||
| + | [[Category: McLellan JS]] | ||
| + | [[Category: Rush SA]] | ||
Current revision
Structure-based design of prefusion-stabilized human metapneumovirus fusion proteins
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