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http://purl.uniprot.org/citations/23658013http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23658013http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23658013http://www.w3.org/2000/01/rdf-schema#comment"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 Å 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."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m113.459040"xsd:string
http://purl.uniprot.org/citations/23658013http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m113.459040"xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Iwai H."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Iwai H."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Goldman A."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Goldman A."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Kajander T."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Kajander T."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Bhattacharjee A."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Bhattacharjee A."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Oeemig J.S."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Oeemig J.S."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Jokiranta T.S."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Jokiranta T.S."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Kolodziejczyk R."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Kolodziejczyk R."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Lehtinen M.J."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Lehtinen M.J."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Meri T."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/author"Meri T."xsd:string
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23658013http://purl.uniprot.org/core/date"2013"xsd:gYear