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Status: Bibliographieeintrag

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Verfasst von:Herzberger, Pia [VerfasserIn]   i
 Siegel, Corinna [VerfasserIn]   i
 Skerka, Christine [VerfasserIn]   i
 Fingerle, Volker [VerfasserIn]   i
 Schulte-Spechtel, Ulrike [VerfasserIn]   i
 Wilske, Bettina [VerfasserIn]   i
 Brade, Volker [VerfasserIn]   i
 Zipfel, Peter F. [VerfasserIn]   i
 Wallich, Reinhard [VerfasserIn]   i
 Kraiczy, Peter [VerfasserIn]   i
Titel:Identification and characterization of the factor H and FHL-1 binding complement regulator-acquiring surface protein 1 of the Lyme disease spirochete Borrelia spielmanii sp. nov
Verf.angabe:Pia Herzberger, Corinna Siegel, Christine Skerka, Volker Fingerle, Ulrike Schulte-Spechtel, Bettina Wilske, Volker Brade, Peter F. Zipfel, Reinhard Wallich, Peter Kraiczy
Jahr:2009
Umfang:14 S.
Fussnoten:Gesehen am 04.06.2021
Titel Quelle:Enthalten in: International journal of medical microbiology
Ort Quelle:München : Elsevier, 2000
Jahr Quelle:2009
Band/Heft Quelle:299(2009), 2, Seite 141-154
ISSN Quelle:1618-0607
Abstract:Borrelia spielmanii, one of the etiological agents of Lyme disease found in Europe, evades host complement-mediated killing by recruitment of the immune regulators factor H and FHL-1 from human serum. Serum-resistant and intermediate serum-resistant isolates express up to 3 distinct complement regulator-acquiring surface proteins (CRASPs) that bind factor H and/or FHL-1. The present study describes identification and functional characterization of BsCRASP-1 as the dominant factor H and FHL-1 binding protein of B. spielmanii. BsCRASP-1 is a 27.7kDa outer surface lipoprotein, which after processing has a predicted mass of 24.9kDa. BsCRASP-1 is encoded by a single copy gene, cspA, that maps to a linear plasmid of approximately 55kb. Ligand affinity blot techniques revealed that both native and recombinant BsCRASP-1 from different isolates can strongly bind FHL-1, but only weakly factor H. Deletion mutants of recombinant BsCRASP-1 were generated and a high-affinity binding site for factor H and FHL-1 was mapped to its carboxy-terminal 10-amino-acid residue domain. Similarly, the dominant binding site of factor H and FHL-1 was localized to short consensus repeats (SCRs) 5-7. Factor H and FHL-1 maintained cofactor activity for factor I-mediated C3b inactivation when bound to full-length BsCRASP-1 but not to a deletion mutant lacking the carboxy-terminal 10-amino-acid residue domain. In conclusion, BsCRASP-1 binds the host immune regulators factor H and FHL-1, and is suggested to represent a key molecule of B. spielmanii for complement resistance. Thus, BsCRASP-1 most likely contributes to persistence of B. spielmanii and to pathogenesis of Lyme disease.
DOI:doi:10.1016/j.ijmm.2008.06.005
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext ; Verlag: http://dx.doi.org/10.1016/j.ijmm.2008.06.005
 Volltext: https://www.sciencedirect.com/science/article/abs/pii/S1438422108000817
 DOI: https://doi.org/10.1016/j.ijmm.2008.06.005
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Bacterial Outer Membrane Proteins
 Bacterial Proteins
 Binding Sites
 Borrelia
 Complement Factor H
 DNA, Bacterial
 Europe
 Gene Deletion
 Humans
 Intracellular Signaling Peptides and Proteins
 LIM Domain Proteins
 Lyme Disease
 Molecular Sequence Data
 Molecular Weight
 Muscle Proteins
 Plasmids
 Protein Binding
 Protein Interaction Domains and Motifs
 Protein Interaction Mapping
 Sequence Analysis, DNA
 Virulence Factors
K10plus-PPN:1759783102
Verknüpfungen:→ Zeitschrift

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