Immunological characterization of the complement regulator factor H-binding CRASP and Erp proteins of Borrelia burgdorferi

• Verfasst von: Kraiczy, Peter [VerfasserIn]
• Verfasst von: Hartmann, Kristina [VerfasserIn]
• Verfasst von: Hellwage, Jens [VerfasserIn]
• Verfasst von: Skerka, Christine [VerfasserIn]
• Verfasst von: Kirschfink, Michael [VerfasserIn]
• Verfasst von: Brade, Volker [VerfasserIn]
• Verfasst von: Zipfel, Peter F. [VerfasserIn]
• Verfasst von: Wallich, Reinhard [VerfasserIn]
• Verfasst von: Stevenson, Brian [VerfasserIn]
• Titel: Immunological characterization of the complement regulator factor H-binding CRASP and Erp proteins of Borrelia burgdorferi
• Verf.angabe: Peter Kraiczy, Kristina Hartmann, Jens Hellwage, Christine Skerka, Michael Kirschfink, Volker Brade, Peter F. Zipfel, Reinhard Wallich, Brian Stevenson
• E-Jahr: 2005
• Jahr: 24 August 2005
• Jahr des Originals: 2004
• Umfang: 6 S.
• Fussnoten: Available online 24 August 2005 ; Gesehen am 22.02.2021
• Titel Quelle: Enthalten in: International journal of medical microbiology / Supplement
• Ort Quelle: Amsterdam [u.a.] : Elsevier, 2003
• Jahr Quelle: 2004
• Band/Heft Quelle: 293(2004), Seite 152-157
• ISSN Quelle: 2214-8108
• DOI: doi:10.1016/S1433-1128(04)80029-9
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: complement
• Sach-SW: Erp proteins
• Sach-SW: factor H
• Sach-SW: innate immunity
• K10plus-PPN: 1749103850

Abstract

Complement activation plays an important role in the elimination of invading microorganisms. Borrelia (B.) burgdorferi sensu lato the etiological agent of Lyme borreliosis, can resist complement-mediated killing. The mechanism of complement resistance of B. burgdorferi sensu stricto apparently depends on the expression of several outer surface proteins described as CRASPs (complement regulator-acquiring surface proteins). These borrelial surface proteins are able to bind components of the complement regulatory system, factor H and/or factor H-like protein 1 (FHL-1), two crucial fluid-phase negative regulators of the alternative pathway of complement. It was previously demonstrated that one CRASP is encoded by a member of the erp gene family. The purpose of the study was to use a set of monoclonal antibodies (mAb) and polyclonal antisera to characterize the relatedness of factor H-binding CRASP and Erp proteins among several B. burgdorferi sensu stricto and B. afzelii strains. Based on the observed cross-reactivities between B. burgdorferi sensu stricto strains LW2 and PKa-1, it is concluded that BbCRASP-3 is similar to ErpP, BbCRASP-4 is structurally related to ErpC, and BbCRASP-5 is similar to ErpA. The BaCRASP-2 and BaCRASP-4 proteins of B. afzelii strain EB1 reacted with both anti-ErpA and anti-ErpP antibodies whereas BaCRASP-5 of B. afzelii strain FEM1-D15 exclusively reacted with BbCRASP-3/ErpP specific antibodies. Together, these data indicate that most of the factor H-binding CRASPs are members of the Erp protein family, which represents a polymorphic class of proteins with similar or identical immunological reactivities.