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

Peter Kraiczy; Kristina Hartmann; Jens Hellwage; Christine Skerka; Michael Kirschfink; Volker Brade; Peter F. Zipfel; Reinhard Wallich; Brian Stevenson

doi:10.1016/S1433-1128(04)80029-9

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

Peter Kraiczy, Kristina Hartmann, Jens Hellwage, Christine Skerka, Michael Kirschfink, Volker Brade, Peter F. Zipfel, Reinhard Wallich, Brian Stevenson

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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.

Original language	English
Pages (from-to)	152-157
Number of pages	6
Journal	International Journal of Medical Microbiology, Supplement
Volume	293
Issue number	37
DOIs	https://doi.org/10.1016/S1433-1128(04)80029-9
State	Published - Apr 2004

Bibliographical note

Funding Information:
Acknowledgements. We thank Christiane Brenner, Chris-ta Hanssen-Hiibner, and Andrea H6nes for their skilful and expert technical assistance. This work was funded by the Thiiringer Ministerium fiir Wissenschaft, Forschung und Kultur, US National Institutes of Health grant RO1-AI44254, and the Deutsche Forschungsgemeinschaft, Project Zi 342/5 and Br 446/11-3.

Keywords

Borrelia burgdorferi
Complement
Erp proteins
Factor H
Innate immunity

ASJC Scopus subject areas

Microbiology
Microbiology (medical)

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10.1016/S1433-1128(04)80029-9

Cite this

Kraiczy, P., Hartmann, K., Hellwage, J., Skerka, C., Kirschfink, M., Brade, V., Zipfel, P. F., Wallich, R., & Stevenson, B. (2004). Immunological characterization of the complement regulator factor H-binding CRASP and Erp proteins of Borrelia burgdorferi. International Journal of Medical Microbiology, Supplement, 293(37), 152-157. https://doi.org/10.1016/S1433-1128(04)80029-9

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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.",

keywords = "Borrelia burgdorferi, Complement, Erp proteins, Factor H, Innate immunity",

author = "Peter Kraiczy and Kristina Hartmann and Jens Hellwage and Christine Skerka and Michael Kirschfink and Volker Brade and Zipfel, {Peter F.} and Reinhard Wallich and Brian Stevenson",

note = "Funding Information: Acknowledgements. We thank Christiane Brenner, Chris-ta Hanssen-Hiibner, and Andrea H6nes for their skilful and expert technical assistance. This work was funded by the Thiiringer Ministerium fiir Wissenschaft, Forschung und Kultur, US National Institutes of Health grant RO1-AI44254, and the Deutsche Forschungsgemeinschaft, Project Zi 342/5 and Br 446/11-3.",

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Kraiczy, P, Hartmann, K, Hellwage, J, Skerka, C, Kirschfink, M, Brade, V, Zipfel, PF, Wallich, R & Stevenson, B 2004, 'Immunological characterization of the complement regulator factor H-binding CRASP and Erp proteins of Borrelia burgdorferi', International Journal of Medical Microbiology, Supplement, vol. 293, no. 37, pp. 152-157. https://doi.org/10.1016/S1433-1128(04)80029-9

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AU - Kraiczy, Peter

AU - Hartmann, Kristina

AU - Hellwage, Jens

AU - Skerka, Christine

AU - Kirschfink, Michael

AU - Brade, Volker

AU - Zipfel, Peter F.

AU - Wallich, Reinhard

AU - Stevenson, Brian

N1 - Funding Information: Acknowledgements. We thank Christiane Brenner, Chris-ta Hanssen-Hiibner, and Andrea H6nes for their skilful and expert technical assistance. This work was funded by the Thiiringer Ministerium fiir Wissenschaft, Forschung und Kultur, US National Institutes of Health grant RO1-AI44254, and the Deutsche Forschungsgemeinschaft, Project Zi 342/5 and Br 446/11-3.

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N2 - 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.

AB - 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.

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KW - Complement

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KW - Factor H

KW - Innate immunity

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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