AI Article Synopsis
- Immune evasion by Borrelia, which causes diseases like relapsing fever and Lyme disease, is largely facilitated through the acquisition of the host's complement inhibitor Factor H (FH).
- Researchers determined the 2.2 Å crystal structure of FhbA from Borrelia hermsii in complex with FH, uncovering how it helps the bacteria escape immune responses.
- The study also identified a family of FhbA-related proteins across different Borrelia species, which share a conserved mechanism for binding FH, potentially leading to new strategies for combating their virulence and resistance to the immune system.
Article 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.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8967061 | PMC |
| http://dx.doi.org/10.1371/journal.ppat.1010338 | DOI Listing |
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