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| | ==Solution Structure of Outer surface protein E== | | ==Solution Structure of Outer surface protein E== |
| - | <StructureSection load='2m4f' size='340' side='right'caption='[[2m4f]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2m4f' size='340' side='right'caption='[[2m4f]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2m4f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Borbn Borbn]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M4F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2m4f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi_N40 Borreliella burgdorferi N40]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M4F FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4j38|4j38]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BbuN40_O26 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=521007 BORBN])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2m4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m4f OCA], [https://pdbe.org/2m4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m4f RCSB], [https://www.ebi.ac.uk/pdbsum/2m4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m4f 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=2m4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m4f OCA], [https://pdbe.org/2m4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m4f RCSB], [https://www.ebi.ac.uk/pdbsum/2m4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m4f ProSAT]</span></td></tr> |
| | </table> | | </table> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Borbn]] | + | [[Category: Borreliella burgdorferi N40]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bhattacharjee, A]] | + | [[Category: Bhattacharjee A]] |
| - | [[Category: Goldman, A]] | + | [[Category: Goldman A]] |
| - | [[Category: Iwai, H]] | + | [[Category: Iwai H]] |
| - | [[Category: Jokiranta, T]] | + | [[Category: Jokiranta T]] |
| - | [[Category: Kajander, T]] | + | [[Category: Kajander T]] |
| - | [[Category: Kolodziejczyk, R]] | + | [[Category: Kolodziejczyk R]] |
| - | [[Category: Meri, T]] | + | [[Category: Meri T]] |
| - | [[Category: Oeemig, J S]] | + | [[Category: Oeemig JS]] |
| - | [[Category: Bbcrasp-3]]
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| - | [[Category: Borrelia burgdorferi n40]]
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| - | [[Category: Complement]]
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| - | [[Category: Erp]]
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| - | [[Category: Immune evasion]]
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| - | [[Category: Immune system]]
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| - | [[Category: Innate immunity]]
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| - | [[Category: Ospe]]
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| - | [[Category: Outer surface protein e]]
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| Structural highlights
Publication Abstract from PubMed
Borrelia burgdorferi spirochetes that cause Lyme borreliosis survive for a long time in human serum because they successfully evade the complement system, an important arm of innate immunity. The outer surface protein E (OspE) of B. burgdorferi is needed for this because it recruits complement regulator factor H (FH) onto the bacterial surface to evade complement-mediated cell lysis. To understand this process at the molecular level, we used a structural approach. First, we solved the solution structure of OspE by NMR, revealing a fold that has not been seen before in proteins involved in complement regulation. Next, we solved the x-ray structure of the complex between OspE and the FH C-terminal domains 19 and 20 (FH19-20) at 2.83 A resolution. The structure shows that OspE binds FH19-20 in a way similar to, but not identical with, that used by endothelial cells to bind FH via glycosaminoglycans. The observed interaction of OspE with FH19-20 allows the full function of FH in down-regulation of complement activation on the bacteria. This reveals the molecular basis for how B. burgdorferi evades innate immunity and suggests how OspE could be used as a potential vaccine antigen.
Structural Basis for Complement Evasion by Lyme Disease Pathogen Borrelia burgdorferi.,Bhattacharjee A, Oeemig JS, Kolodziejczyk R, Meri T, Kajander T, Lehtinen MJ, Iwai H, Jokiranta TS, Goldman A J Biol Chem. 2013 Jun 28;288(26):18685-95. doi: 10.1074/jbc.M113.459040. Epub, 2013 May 8. PMID:23658013[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bhattacharjee A, Oeemig JS, Kolodziejczyk R, Meri T, Kajander T, Lehtinen MJ, Iwai H, Jokiranta TS, Goldman A. Structural Basis for Complement Evasion by Lyme Disease Pathogen Borrelia burgdorferi. J Biol Chem. 2013 Jun 28;288(26):18685-95. doi: 10.1074/jbc.M113.459040. Epub, 2013 May 8. PMID:23658013 doi:10.1074/jbc.M113.459040
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