ArticleJournal of bacteriology2005
Putative coiled-coil structural elements of the BBA68 protein of Lyme disease spirochetes are required for formation of its factor H binding site.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed.
- Navigating infection by pathogenic spirochetes: The host-bacteria interface at the atomic level.Protein science : a publication of the Protein Society · 2025Review
- Article
- Complement Evasion inAntibiotics (Basel, Switzerland) · 2019Review
- Polymorphic factor H-binding activity of CspA protects Lyme borreliae from the host complement in feeding ticks to facilitate tick-to-host transmission.PLoS pathogens · 2018Article
- Article
- Structural basis for complement evasion by Lyme disease pathogen Borrelia burgdorferi.The Journal of biological chemistry · 2013Article
- Complement regulator-acquiring surface proteins of Borrelia burgdorferi: Structure, function and regulation of gene expression.Ticks and tick-borne diseases · 2013Review
- The role of Borrelia burgdorferi outer surface proteins.FEMS immunology and medical microbiology · 2012Review
- Structure of factor H-binding protein B (FhbB) of the periopathogen, Treponema denticola: insights into progression of periodontal disease.The Journal of biological chemistry · 2012Article
- Crystallization of the factor H-binding protein, FhbB, from the periopathogen Treponema denticola.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Identification and functional characterisation of Complement Regulator Acquiring Surface Protein-1 of serum resistant Borrelia garinii OspA serotype 4.BMC microbiology · 2010Article
- Comparative analysis of the properties and ligand binding characteristics of CspZ, a factor H binding protein, derived from Borrelia burgdorferi isolates of human origin.Infection and immunity · 2009Article
- Article
- Complement factor H binding by different Lyme disease and relapsing fever Borrelia in animals and human.BMC research notes · 2009Article
- Analysis of a unique interaction between the complement regulatory protein factor H and the periodontal pathogen Treponema denticola.Infection and immunity · 2009Article
- Functional mapping of YadA- and Ail-mediated binding of human factor H to Yersinia enterocolitica serotype O:3.Infection and immunity · 2008Article
- Analysis of a growth-phase-regulated two-component regulatory system in the periodontal pathogen Treponema denticola.Journal of bacteriology · 2008Article
- Borrelia burgdorferi surface-localized proteins expressed during persistent murine infection are conserved among diverse Borrelia spp.Infection and immunity · 2008Article
- Identification of an antiparallel coiled-coil/loop domain required for ligand binding by the Borrelia hermsii FhbA protein: additional evidence for the role of FhbA in the host-pathogen interaction.Infection and immunity · 2008Article
- Delineation of species-specific binding properties of the CspZ protein (BBH06) of Lyme disease spirochetes: evidence for new contributions to the pathogenesis of Borrelia spp.Infection and immunity · 2007Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Factor H and factor H like-protein 1 (FHL-1) are complement regulatory proteins that serve as cofactors for the factor I-mediated cleavage of C3b. Some Lyme disease and relapsing fever spirochete species bind factor H to their surface to facilitate immune evasion. The Lyme disease spirochetes produce several factor H binding proteins (FHBPs) that form two distinct classes. Class I FHBPs (OspE orthologs and paralogs) bind only factor H, while class II FHBPs (BBA68) bind both factor H and FHL-1. BBA68 belongs to a large paralogous protein family, and of these paralogs, BBA69 is the member most closely related to BBA68. To determine if BBA69 can also bind factor H, recombinant protein was generated and tested for factor H binding. BBA69 did not exhibit factor H binding ability, suggesting that among family 54 paralogs, factor H binding is unique to BBA68. To identify the determinants of BBA68 that are involved in factor H binding, truncation and site-directed mutational analyses were performed. These analyses revealed that the factor H binding site is discontinuous and provide strong evidence that coiled-coil structural elements are involved in the formation of the binding site.
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