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6ZH1

Crystal structure of complex between FH19-20 and FhbA protein from Borrelia hermsii

Summary for 6ZH1
Entry DOI10.2210/pdb6zh1/pdb
DescriptorFactor H-binding protein A, Complement factor H, 1,2-ETHANEDIOL, ... (5 entities in total)
Functional Keywordsinnate immunity, complement, relapsing fever, lyme disease, immune system
Biological sourceBorrelia hermsii YOR
More
Total number of polymer chains2
Total formula weight37961.63
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 citationKogan, 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: 35303742
DOI: 10.1371/journal.ppat.1010338
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

226707

數據於2024-10-30公開中

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