Further Characterization of Complement Regulator-Acquiring Surface Proteins of Borrelia burgdorferi

doi:10.1128/IAI.69.12.7800-7809.2001

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Infection and Immunity, December 2001, p. 7800-7809, Vol. 69, No. 12
0019-9567/01/$04.00+0 DOI: 10.1128/IAI.69.12.7800-7809.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Further Characterization of Complement Regulator-Acquiring Surface Proteins of Borrelia burgdorferi

Peter Kraiczy,¹^,^* Christine Skerka,² Volker Brade,¹ and Peter F. Zipfel²

Institute of Medical Microbiology, University Hospital of Frankfurt, D-60596 Frankfurt,¹ and Department of Infection Biology, Hans Knoell Institute for Natural Products Research, D-07745 Jena,² Germany

Received 8 June 2001/Returned for modification 24 July 2001/Accepted 4 September 2001

The three genospecies Borrelia burgdorferi, Borrelia garinii, and Borrelia afzelii, all causative agents of Lyme disease,differ in their susceptibilities to human complement-mediatedlysis. We recently reported that serum resistance of borreliascorrelates largely with their ability to bind the human complementregulators FHL-1/reconectin and factor H. To date, two complementregulator-acquiring-proteins (CRASP-1 and CRASP-2) have been identifiedin serum-resistant B. afzelii isolates (P. Kraiczy, C. Skerka,M. Kirschfink, V. Brade, and P. F. Zipfel, Eur. J. Immunol. 31:1674-1684,2001). Here, we present a comprehensive study of the CRASPs detectablein both serum-resistant and intermediate serum-sensitive B. afzeliiand B. burgdorferi isolates. These CRASPs were designated accordingto the genospecies either as BaCRASPs, when derived from B. afzelii,or as BbCRASPs, for proteins identified in B. burgdorferi isolates.Each borrelial isolate expresses distinct CRASPs that can be differentiatedby their mobility and binding phenotypes. A detailed comparisonreveals overlapping and even identical binding profiles for BaCRASP-1(27.5 kDa), BbCRASP-1 (25.9 kDa), and BbCRASP-2 (23.2 kDa), whichbind FHL-1/reconectin strongly and interact weakly with factorH. In contrast, two B. afzelii proteins (BaCRASP-4 [19.2 kDa]and BaCRASP-5 [22.5 kDa]) and three B. burgdorferi proteins (BbCRASP-3[19.8 kDa], BbCRASP-4 [18.5 kDa], and BbCRASP-5 [17.7 kDa]) bindfactor H but not FHL-1/reconectin. Most CRASPs bind both humanimmune regulators at their C-terminal ends. Temperature-dependentup-regulation of CRASPs (BaCRASP-1, BaCRASP-2, and BaCRASP-5)is detected in low-passage borrelias cultured at 33 or 37°C comparedwith those cultured at 20°C. The characterization of the individualCRASPs on the molecular level is expected to identify new virulencefactors and potential vaccinecandidates.

^* Corresponding author. Mailing address: Institute of Medical Microbiology, University Hospital of Frankfurt, Paul-Ehrlich-Str.40, D-60596 Frankfurt, Germany. Phone: 49 69 6301 7165. Fax: 4969 6301 5767. E-mail: Kraiczy{at}em.uni-frankfurt.de.

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