Functional characterization of Borrelia spielmanii outer surface proteins that interact with distinct members of the human factor H protein family and with plasminogen
Acquisition of complement regulator factor H (CFH) and factor H-like protein 1 (CFHL1) from human serum enables Borrelia spielmanii, one of the etiological agents of Lyme disease, to evade complement-mediated killing by the human host. Up to three distinct complement regulator-acquiring surface prot...
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| Main Authors: | , , , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
2010
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| In: |
Infection and immunity
Year: 2009, Volume: 78, Issue: 1, Pages: 39-48 |
| ISSN: | 1098-5522 |
| DOI: | 10.1128/IAI.00691-09 |
| Online Access: | Verlag, Volltext: https://dx.doi.org/10.1128/IAI.00691-09 Verlag, Volltext: https://iai.asm.org/content/78/1/39 
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| Author Notes: | Annekatrin Seling, Corinna Siegel, Volker Fingerle, Brandon L. Jutras, Catherine A. Brissette, Christine Skerka, Reinhard Wallich, Peter F. Zipfel, Brian Stevenson, and Peter Kraiczy |
| Summary: | Acquisition of complement regulator factor H (CFH) and factor H-like protein 1 (CFHL1) from human serum enables Borrelia spielmanii, one of the etiological agents of Lyme disease, to evade complement-mediated killing by the human host. Up to three distinct complement regulator-acquiring surface proteins (CRASPs) may be expressed by serum-resistant B. spielmanii, each exhibiting an affinity for CFH and/or CFHL1. Here, we describe the functional characterization of the 15-kDa CRASPs of B. spielmanii, members of the polymorphic Erp (OspE/F-related) protein family, that bind two distinct host complement regulators, CFH and factor H-related protein 1 (CFHR1), but not CFHL1. CFH bound to the B. spielmanii CRASPs maintained cofactor activity for factor I-mediated C3b inactivation. Three naturally occurring alleles of this protein bound CFH and CFHR1 while a fourth natural allele could not. Comparative sequence analysis of these protein alleles identified a single amino acid, histidine-79, as playing a significant role in CFH/CFHR1 binding, with substitution by an arginine completely abrogating ligand binding. The mutation of His-79 to Arg did not inhibit binding of plasminogen, another known ligand of this group of borrelial outer-surface proteins. |
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| Item Description: | Published ahead of print on 26 October 2009 Gesehen am 19.05.2021 |
| Physical Description: | Online Resource |
| ISSN: | 1098-5522 |
| DOI: | 10.1128/IAI.00691-09 |