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

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-deriv...

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Main Authors: Dieterich, Roswitha (Author) , Hammerschmidt, Claudia (Author) , Richter, Dania (Author) , Skerka, Christine (Author) , Wallich, Reinhard (Author) , Matuschka, Franz-Rainer (Author) , Zipfel, Peter F. (Author) , Kraiczy, Peter (Author)
Format: Article (Journal)
Language:English
Published: 7 September 2010
In: Infection and immunity
Year: 2010, Volume: 78, Issue: 11, Pages: 4467-4476
ISSN:1098-5522
DOI:10.1128/IAI.00138-10
Online Access:Verlag, lizenzpflichtig, Volltext: https://dx.doi.org/10.1128/IAI.00138-10
Verlag, lizenzpflichtig, Volltext: https://iai.asm.org/content/78/11/4467
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Author Notes:Roswitha Dieterich, Claudia Hammerschmidt, Dania Richter, Christine Skerka, Reinhard Wallich, Franz-Rainer Matuschka, Peter F. Zipfel, and Peter Kraiczy
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Summary: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.
Item Description:Gesehen am 17.05.2021
Physical Description:Online Resource
ISSN:1098-5522
DOI:10.1128/IAI.00138-10

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