Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

28LK

Crystal structure of complement-inhibiting protein ChiB of Borrelia recurrentis

Summary for 28LK
Entry DOI10.2210/pdb28lk/pdb
Descriptorcomplement-inhibiting protein ChiB, 2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE, GLYCEROL, ... (4 entities in total)
Functional Keywordsborrelia recurrentis, louse-borne relapsing fever, surface protein, complement targeting and host interacting protein, complement-inhibiting protein, protein binding
Biological sourceBorrelia recurrentis
Total number of polymer chains1
Total formula weight32553.98
Authors
Fritz-Wolf, K.,Rahlfs, S.,Przyborski, J.M.,Stumpf, M.,Roettgerding, F.,Kraiczy, P. (deposition date: 2026-02-05, release date: 2026-05-06)
Primary citationRottgerding, F.,Reyer, F.,Gerlach, E.,Amborn, M.,Duschek, N.,Schultze, T.G.,Fingerle, V.,Roome, C.M.,Stumpf, M.,Becker, K.,Rahlfs, S.,Przyborski, J.M.,Kraiczy, P.,Fritz-Wolf, K.
Complement inhibition by a unique cluster of immunomodulatory outer surface proteins of Borrelia recurrentis.
Nat Commun, 17:-, 2026
Cited by
PubMed Abstract: Borrelia recurrentis, the agent of louse-borne relapsing fever, causes a poverty-associated, infectious disease of high mortality. Here, we identified and characterized five Complement targeting and Host Interacting proteins, ChiA to ChiE displaying immunomodulatory functions. Almost all Chi homologs inhibit complement activation by direct binding of key components, block membrane attack complex formation, and interact with plasminogen. Borrelia proteins protect susceptible spirochetes from complement-mediated killing and ChiB, ChiC, and ChiD facilitate serum resistance. X-ray structures of ChiA and ChiB, along with AlphaFold models of ChiC, ChiD, and ChiE, reveal a conserved, compact eight-helix fold with a central hydrophobic pocket and a unique S-domain-feature distinct from all known Borrelia proteins. Notably, ChiC and ChiE harbor conserved cysteines forming a reversible disulfide bridge, indicating redox-responsive function. Our findings identify a protein family of functionally related immune evasion factors, advancing our understanding of the underlying mechanisms of complement resistance in this neglected, human pathogenic microorganism.
PubMed: 42050325
DOI: 10.1038/s41467-026-72359-y
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

253795

PDB entries from 2026-05-20

PDB statisticsPDBj update infoContact PDBjnumon