Navigation überspringen
Universitätsbibliothek Heidelberg
Status: Bibliographieeintrag

Verfügbarkeit
Standort: ---
Exemplare: ---
heiBIB
 Online-Ressource
Verfasst von:Hartmann, Kristina [VerfasserIn]   i
 Corvey, Carsten [VerfasserIn]   i
 Skerka, Christine [VerfasserIn]   i
 Kirschfink, Michael [VerfasserIn]   i
 Karas, Michael [VerfasserIn]   i
 Brade, Volker [VerfasserIn]   i
 Miller, Jennifer C. [VerfasserIn]   i
 Stevenson, Brian [VerfasserIn]   i
 Wallich, Reinhard [VerfasserIn]   i
 Zipfel, Peter F. [VerfasserIn]   i
 Kraiczy, Peter [VerfasserIn]   i
Titel:Functional characterization of BbCRASP-2, a distinct outer membrane protein of Borrelia burgdorferi that binds host complement regulators factor H and FHL-1
Verf.angabe:Kristina Hartmann, Carsten Corvey, Christine Skerka, Michael Kirschfink, Michael Karas, Volker Brade, Jennifer C. Miller, Brian Stevenson, Reinhard Wallich, Peter F. Zipfel and Peter Kraiczy
E-Jahr:2006
Jahr:01 August 2006
Umfang:17 S.
Fussnoten:Gesehen am 15.02.2021
Titel Quelle:Enthalten in: Molecular microbiology
Ort Quelle:Oxford [u.a.] : Wiley-Blackwell, 1987
Jahr Quelle:2006
Band/Heft Quelle:61(2006), 5, Seite 1220-1236
ISSN Quelle:1365-2958
Abstract:Borrelia burgdorferi, the aetiological agent of Lyme disease, employs sophisticated means to survive in diverse mammalian hosts. Recent studies demonstrated that acquisition of complement regulators factor H and factor H-like protein-1 (FHL-1) allows spirochetes to resist complement-mediated killing. Serum-resistant B. burgdorferi express up to five distinct complement regulator-acquiring surface proteins (CRASPs) that bind factor H and/or FHL-1. In this study we have identified and characterized one of those B. burgdorferi proteins, named BbCRASP-2. BbCRASP-2 is distinct from the four previously identified factor H/FHL-1-binding CRASPs of B. burgdorferi strains. The single copy of the gene encoding BbCRASP-2, cspZ, is located on the linear plasmid lp28-3. BbCRASP-2 is highly divergent from the factor H/FHL-1-binding protein BbCRASP-1 and from members of the factor H-binding Erp (OspE/F-related) protein family. Peptide mapping analysis revealed that the factor H/FHL-1 binding site is discontinuous and it was found that C-terminal truncations abrogate factor H and FHL-1 binding. The predominant BbCRASP-2 binding site of both host complement regulators was mapped to the short consensus repeat 7 (SCR 7). Factor H and FHL-1 bound to BbCRASP-2 maintain cofactor activity for factor I-mediated C3b inactivation and accelerate the decay of the C3 convertase. Expression of BbCRASP-2 in serum-sensitive B. burgdorferi mutant B313 increased resistance to complement-mediated lysis. The characterization of BbCRASP-2 now provides a complete picture of the three diverse complement regulator-binding protein families of B. burgdorferi yielding new insights into the pathogenesis of Lyme disease.
DOI:doi:10.1111/j.1365-2958.2006.05318.x
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: https://doi.org/10.1111/j.1365-2958.2006.05318.x
 Volltext: https://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2006.05318.x
 DOI: https://doi.org/10.1111/j.1365-2958.2006.05318.x
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Amino Acid Sequence
 Animals
 Bacterial Proteins
 Blotting, Western
 Borrelia burgdorferi
 Complement Factor H
 Electrophoresis, Polyacrylamide Gel
 Humans
 Intracellular Signaling Peptides and Proteins
 LIM Domain Proteins
 Lyme Disease
 Mass Spectrometry
 Membrane Proteins
 Mice
 Mice, Inbred BALB C
 Microscopy, Fluorescence
 Molecular Sequence Data
 Muscle Proteins
 Protein Binding
 Surface Plasmon Resonance
K10plus-PPN:1748290371
Verknüpfungen:→ Zeitschrift

Permanenter Link auf diesen Titel (bookmarkfähig):  https://katalog.ub.uni-heidelberg.de/titel/68699016   QR-Code
zum Seitenanfang