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Inadequate binding of immune regulator factor H is associated with sensitivity of Borrelia lusitaniae to human complement.

Abstract

Spirochetes belonging to the Borrelia burgdorferi sensu lato complex differ in resistance to complement-mediated killing by human serum. Here, we characterize complement sensitivity of a panel of B. lusitaniae isolates derived from ticks collected in Germany and Portugal as well as one patient-derived isolate, PoHL. All isolates are highly susceptible to complement-mediated lysis in human serum and activate complement predominantly by the alternative pathway, leading to an increased deposition of complement components C3, C6, and the terminal complement complex. Interestingly, serum-sensitive B. lusitaniae isolates were able to bind immune regulator factor H (CFH), and some strains also bound CFH-related protein 1 (CFHR1) and CFHR2. Moreover, CFH bound to the surface of B. lusitaniae was inefficient in mediating C3b conversion. Furthermore, the identification and characterization of a potential CFH-binding protein, OspE, revealed that this molecule possesses a significantly reduced binding capacity for CFH compared to that of CFH-binding OspE paralogs expressed by various serum-resistant Borrelia species. This finding suggests that a reduced binding capability of CFH is associated with an increased serum sensitivity of B. lusitaniae to human complement.

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    Source

    Infection and immunity 78:11 2010 Nov pg 4467-76

    MeSH

    Animals
    Bacterial Outer Membrane Proteins
    Blood Bactericidal Activity
    Blood Proteins
    Borrelia
    Borrelia Infections
    Complement Activation
    Complement C3b Inactivator Proteins
    Complement Factor H
    Complement Pathway, Alternative
    Germany
    Humans
    Ixodes
    Molecular Sequence Data
    Portugal
    Sequence Analysis, DNA

    Pub Type(s)

    Journal Article
    Research Support, Non-U.S. Gov't

    Language

    eng

    PubMed ID

    20823202