PDBsum entry 4j38

Immune system

PDB id: 4j38

Contents

Protein chains

132 a.a.

123 a.a.

Ligands

SO4

Waters ×15

PDB id:

4j38

Name:

Immune system

Title:

Structure of borrelia burgdorferi outer surface protein e in complex with factor h domains 19-20

Structure:

Outer surface protein e. Chain: a. Fragment: unp residues 21-171. Engineered: yes. Complement factor h. Chain: b. Fragment: fh domains 19-20, unp residues 1103-1231. Synonym: h factor 1. Engineered: yes.

Source:

Borrelia burgdorferi. Organism_taxid: 521007. Strain: n40. Gene: ospe. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human. Organism_taxid: 9606.

Resolution:

2.83Å R-factor: 0.196 R-free: 0.255

Authors:

A.Bhattacharjee,R.Kolodziejczyk,T.Kajander,A.Goldman,T.S.Jokiranta

Key ref:

A.Bhattacharjee et al. (2013). Structural basis for complement evasion by Lyme disease pathogen Borrelia burgdorferi. J Biol Chem, 288, 18685-18695. PubMed id: 23658013 DOI: 10.1074/jbc.M113.459040

Date:

05-Feb-13 Release date: 15-May-13

Protein chain

No UniProt id for this chain

Struc: 132 a.a.

Protein chain

P08603  (CFAH_HUMAN) -  Complement factor H from Homo sapiens

Seq: 1231 a.a.

Struc: 123 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.1074/jbc.M113.459040

J Biol Chem 288:18685-18695 (2013)

PubMed id: 23658013

Structural basis for complement evasion by Lyme disease pathogen Borrelia burgdorferi.

A.Bhattacharjee, J.S.Oeemig, R.Kolodziejczyk, T.Meri, T.Kajander, M.J.Lehtinen, H.Iwaï, T.S.Jokiranta, A.Goldman.

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.