6ZH1
Crystal structure of complex between FH19-20 and FhbA protein from Borrelia hermsii
Summary for 6ZH1
Entry DOI | 10.2210/pdb6zh1/pdb |
Descriptor | Factor H-binding protein A, Complement factor H, 1,2-ETHANEDIOL, ... (5 entities in total) |
Functional Keywords | innate immunity, complement, relapsing fever, lyme disease, immune system |
Biological source | Borrelia hermsii YOR More |
Total number of polymer chains | 2 |
Total formula weight | 37961.63 |
Authors | Kogan, K.,Kotila, T.,Meri, T.,Goldman, A. (deposition date: 2020-06-20, release date: 2022-01-12, Last modification date: 2024-01-24) |
Primary citation | Kogan, K.,Haapasalo, K.,Kotila, T.,Moore, R.,Lappalainen, P.,Goldman, A.,Meri, T. Mechanism of Borrelia immune evasion by FhbA-related proteins. Plos Pathog., 18:e1010338-e1010338, 2022 Cited by PubMed Abstract: Immune evasion facilitates survival of Borrelia, leading to infections like relapsing fever and Lyme disease. Important mechanism for complement evasion is acquisition of the main host complement inhibitor, factor H (FH). By determining the 2.2 Å crystal structure of Factor H binding protein A (FhbA) from Borrelia hermsii in complex with FH domains 19-20, combined with extensive mutagenesis, we identified the structural mechanism by which B. hermsii utilizes FhbA in immune evasion. Moreover, structure-guided sequence database analysis identified a new family of FhbA-related immune evasion molecules from Lyme disease and relapsing fever Borrelia. Conserved FH-binding mechanism within the FhbA-family was verified by analysis of a novel FH-binding protein from B. duttonii. By sequence analysis, we were able to group FH-binding proteins of Borrelia into four distinct phyletic types and identified novel putative FH-binding proteins. The conserved FH-binding mechanism of the FhbA-related proteins could aid in developing new approaches to inhibit virulence and complement resistance in Borrelia. PubMed: 35303742DOI: 10.1371/journal.ppat.1010338 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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