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Status: Bibliographieeintrag

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Verfasst von:Siegel, Corinna [VerfasserIn]   i
 Hallström, Teresia [VerfasserIn]   i
 Skerka, Christine [VerfasserIn]   i
 Eberhardt, Hannes [VerfasserIn]   i
 Uzonyi, Barbara [VerfasserIn]   i
 Beckhaus, Tobias [VerfasserIn]   i
 Karas, Michael [VerfasserIn]   i
 Wallich, Reinhard [VerfasserIn]   i
 Stevenson, Brian [VerfasserIn]   i
 Zipfel, Peter F. [VerfasserIn]   i
 Kraiczy, Peter [VerfasserIn]   i
Titel:Complement factor H-related proteins CFHR2 and CFHR5 represent novel ligands for the infection-associated CRASP proteins of Borrelia burgdorferi
Verf.angabe:Corinna Siegel, Teresia Hallström, Christine Skerka, Hannes Eberhardt, Barbara Uzonyi, Tobias Beckhaus, Michael Karas, Reinhard Wallich, Brian Stevenson, Peter F. Zipfel, Peter Kraiczy
E-Jahr:2010
Jahr:October 20, 2010
Umfang:14 S.
Fussnoten:Gesehen am 17.05.2021
Titel Quelle:Enthalten in: PLOS ONE
Ort Quelle:San Francisco, California, US : PLOS, 2006
Jahr Quelle:2010
Band/Heft Quelle:5(2010), 10, Artikel-ID e13519, Seite 1-14
ISSN Quelle:1932-6203
Abstract:BACKGROUND: One virulence property of Borrelia burgdorferi is its resistance to innate immunity, in particular to complement-mediated killing. Serum-resistant B. burgdorferi express up to five distinct complement regulator-acquiring surface proteins (CRASP) which interact with complement regulator factor H (CFH) and factor H-like protein 1 (FHL1) or factor H-related protein 1 (CFHR1). In the present study we elucidate the role of the infection-associated CRASP-3 and CRASP-5 protein to serve as ligands for additional complement regulatory proteins as well as for complement resistance of B. burgdorferi. METHODOLOGY/PRINCIPAL FINDINGS: To elucidate whether CRASP-5 and CRASP-3 interact with various human proteins, both borrelial proteins were immobilized on magnetic beads. Following incubation with human serum, bound proteins were eluted and separated by Glycine-SDS-PAGE. In addition to CFH and CFHR1, complement regulators CFHR2 and CFHR5 were identified as novel ligands for both borrelial proteins by employing MALDI-TOF. To further assess the contributions of CRASP-3 and CRASP-5 to complement resistance, a serum-sensitive B. garinii strain G1 which lacks all CFH-binding proteins was used as a valuable model for functional analyses. Both CRASPs expressed on the B. garinii outer surface bound CFH as well as CFHR1 and CFHR2 in ELISA. In contrast, live B. garinii bound CFHR1, CFHR2, and CFHR5 and only miniscute amounts of CFH as demonstrated by serum adsorption assays and FACS analyses. Further functional analysis revealed that upon NHS incubation, CRASP-3 or CRASP-5 expressing borreliae were killed by complement. CONCLUSIONS/SIGNIFICANCE: In the absence of CFH and the presence of CFHR1, CFHR2 and CFHR5, assembly and integration of the membrane attack complex was not efficiently inhibited indicating that CFH in co-operation with CFHR1, CFHR2 and CFHR5 supports complement evasion of B. burgdorferi.
DOI:doi:10.1371/journal.pone.0013519
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: https://doi.org/10.1371/journal.pone.0013519
 Volltext: https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0013519
 DOI: https://doi.org/10.1371/journal.pone.0013519
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Bacterial Proteins
 Blood Proteins
 Borrelia burgdorferi
 Complement Factor H
 Ligands
 Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
K10plus-PPN:1757910069
Verknüpfungen:→ Zeitschrift

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