Complement resistance of Borrelia burgdorferi correlates with the expression of BbCRASP-1, a novel linear plasmid-encoded surface protein that interacts with human factor H and FHL-1 and is unrelated to Erp proteins
The etiologic agent of Lyme disease, Borrelia burgdorferi, is capable of circumventing the immune defense of a variety of potential vertebrate hosts. Previous work has shown that interaction of host-derived complement regulators, factor H and factor H-like protein 1 (FHL-1), with up to five compleme...
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| Hauptverfasser: | , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2004
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| In: |
The journal of biological chemistry
Year: 2004, Jahrgang: 279, Heft: 4, Pages: 2421-2429 |
| ISSN: | 1083-351X |
| DOI: | 10.1074/jbc.M308343200 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1074/jbc.M308343200 Verlag, lizenzpflichtig, Volltext: https://www.jbc.org/article/S0021-9258(18)52604-1/fulltext 
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| Verfasserangaben: | Peter Kraiczy, Jens Hellwage, Christine Skerka, Heiko Becker, Michael Kirschfink, Markus M. Simon, Volker Brade, Peter F. Zipfel, Reinhard Wallich |
MARC
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| 245 | 1 | 0 | |a Complement resistance of Borrelia burgdorferi correlates with the expression of BbCRASP-1, a novel linear plasmid-encoded surface protein that interacts with human factor H and FHL-1 and is unrelated to Erp proteins |c Peter Kraiczy, Jens Hellwage, Christine Skerka, Heiko Becker, Michael Kirschfink, Markus M. Simon, Volker Brade, Peter F. Zipfel, Reinhard Wallich |
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| 520 | |a The etiologic agent of Lyme disease, Borrelia burgdorferi, is capable of circumventing the immune defense of a variety of potential vertebrate hosts. Previous work has shown that interaction of host-derived complement regulators, factor H and factor H-like protein 1 (FHL-1), with up to five complement regulator-acquiring surface proteins (CRASPs) expressed by resistant B. burgdorferi sensu lato isolates conferred complement resistance. In addition expression of CRASP-1 is directly correlated with complement resistance of Borrelia species. This work describes the functional characterization of BbCRASP-1 as the dominant factor H and FHL-1-binding protein of B. burgdorferi. The corresponding gene, zs7.a68, is located on the linear plasmid lp54 and is different from factor H-binding Erp proteins that are encoded by genes localized on circular plasmids (cp32). Deletion mutants of BbCRASP-1 were generated, and a high affinity binding site for factor H and FHL-1 was mapped to the C terminus of BbCRASP-1. Similarly, the predominant binding site of factor H and FHL-1 was localized to the short consensus repeat 7. Factor H and FHL-1 maintain their cofactor activity for factor I-mediated C3b inactivation when bound to BbCRASP-1, and factor H is up to 6-fold more efficient in mediating C3b conversion than FHL-1. In conclusion, BbCRASP-1 (i). binds the host complement regulators factor H and FHL-1 with high affinity, (ii). is the key molecule of the complement resistance of spirochetes, and (iii). is distinct from the Erp protein family. Thus, BbCRASP-1 most likely contributes to persistence of B. burgdorferi and to pathogenesis of Lyme disease. | ||
| 650 | 4 | |a Amino Acid Sequence | |
| 650 | 4 | |a Bacterial Outer Membrane Proteins | |
| 650 | 4 | |a Bacterial Proteins | |
| 650 | 4 | |a Base Sequence | |
| 650 | 4 | |a Blood Proteins | |
| 650 | 4 | |a Borrelia burgdorferi | |
| 650 | 4 | |a Complement Activation | |
| 650 | 4 | |a Complement C3b Inactivator Proteins | |
| 650 | 4 | |a Complement Factor H | |
| 650 | 4 | |a Humans | |
| 650 | 4 | |a Lyme Disease | |
| 650 | 4 | |a Membrane Proteins | |
| 650 | 4 | |a Molecular Sequence Data | |
| 650 | 4 | |a Mutation | |
| 650 | 4 | |a Protein Binding | |
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| 773 | 0 | 8 | |i Enthalten in |t The journal of biological chemistry |d [Amsterdam] : Elsevier B.V., 1905 |g 279(2004), 4, Seite 2421-2429 |h Online-Ressource |w (DE-627)269247025 |w (DE-600)1474604-9 |w (DE-576)077883837 |x 1083-351X |7 nnas |a Complement resistance of Borrelia burgdorferi correlates with the expression of BbCRASP-1, a novel linear plasmid-encoded surface protein that interacts with human factor H and FHL-1 and is unrelated to Erp proteins |
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