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PDBsum entry 4j38
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Immune system
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PDB id
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4j38
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References listed in PDB file
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Key reference
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Title
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Structural basis for complement evasion by lyme disease pathogen borrelia burgdorferi.
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Authors
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A.Bhattacharjee,
J.S.Oeemig,
R.Kolodziejczyk,
T.Meri,
T.Kajander,
M.J.Lehtinen,
H.Iwaï,
T.S.Jokiranta,
A.Goldman.
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Ref.
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J Biol Chem, 2013,
288,
18685-18695.
[DOI no: ]
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PubMed id
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Abstract
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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.
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