2M4F

Solution Structure of Outer surface protein E

Summary for 2M4F

• Entry DOI: 10.2210/pdb2m4f/pdb
• Related: 4J38
• NMR Information: BMRB: 19001
• Descriptor: Outer surface protein E (1 entity in total)
• Functional Keywords: ospe, outer surface protein e, borrelia burgdorferi n40, bbcrasp-3, erp, complement, innate immunity, immune evasion, immune system
• Biological source: Borrelia burgdorferi
• Total number of polymer chains: 1
• Total formula weight: 16941.97

Authors

Bhattacharjee, A.,Oeemig, J.S.,Kolodziejczyk, R.,Meri, T.,Kajander, T.,Iwai, H.,Jokiranta, T.,Goldman, A. (deposition date: 2013-02-05, release date: 2013-05-15, Last modification date: 2024-05-15)

Primary citation

Bhattacharjee, A.,Oeemig, J.S.,Kolodziejczyk, R.,Meri, T.,Kajander, T.,Lehtinen, M.J.,Iwai, H.,Jokiranta, T.S.,Goldman, A.
Structural Basis for Complement Evasion by Lyme Disease Pathogen Borrelia burgdorferi
J.Biol.Chem., 288:18685-18695, 2013

PubMed Abstract: 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.

PubMed: 23658013
DOI: 10.1074/jbc.M113.459040

Experimental method

SOLUTION NMR