Comparison of Two Laboratory Methods for the Determination of Serum Resistance in Borrelia burgdorferi Isolates

Kraiczy, Peter; Hunfeld, Klaus-Peter; Breitner-Ruddock, S.; Würzner, Reinhard; Acker, Georg; Brade, Volker

doi:10.1016/s0171-2985(00)80094-7

Cited by 59 publications

(73 citation statements)

References 19 publications

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“…Group I proteins (e.g., CRASP-1 Bb ) are related to the gbb54 orthologous family and bind to both factor H and FHL-1, whereas group III proteins (e.g., CRASP-3 Bb to CRASP-5 Bb ) are members of the polymorphic Erp protein family and bind to only factor H. Previous work indicated that serum-sensitive B. garinii strains lack CRASP molecules and are unable to bind FHL-1 or factor H for survival in the infected host (3,4,14,15,21,33). However, the present study shows that B. garinii ZQ1 also expresses a protein homologous to CRASP-1 Bb and CRASP-1 Ba , termed CRASP-1 Bg .…”

Section: Discussionmentioning

confidence: 99%

Identification and Functional Characterization of Complement Regulator-Acquiring Surface Protein 1 of the Lyme Disease SpirochetesBorrelia afzeliiandBorrelia garinii

et al. 2005

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Section: Discussionmentioning

confidence: 99%

Identification and Functional Characterization of Complement Regulator-Acquiring Surface Protein 1 of the Lyme Disease SpirochetesBorrelia afzeliiandBorrelia garinii

et al. 2005

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“…The serum susceptibility of B. hermsii HS1 mutants B313 and B313 containing shuttle vector pBH was assessed using a growth inhibition assay (42). Briefly, cells grown to mid-logarithmic phase were harvested, washed, and resuspended in fresh Barbour-Stoenner-Kelly medium.…”

Section: Serum Susceptibility Testing For Borrelia Strainsmentioning

confidence: 99%

“…9B, B. hermsii HS1 and the transformant B313/pBH, but not the mutant strain B313, showed a specific band. Furthermore, a growth inhibition assay (42) was used to compare the susceptibility of B. hermsii HS1, B313, and B313/pBH to human serum. Resistance to complement-mediated killing was indicated by a continuous growth of spirochetes in the presence of human serum and a subsequent reduction of A562/A630 ratios, whereas the inhibition of sensitive cells was indicated by lack of changes in absorbance.…”

Section: Bhcrasp-1 Increases Resistance To Complement-mediated Killingmentioning

confidence: 99%

Dual Binding Specificity of a Borrelia hermsii-Associated Complement Regulator-Acquiring Surface Protein for Factor H and Plasminogen Discloses a Putative Virulence Factor of Relapsing Fever Spirochetes

Rossmann

Kraiczy

Herzberger

et al. 2007

The Journal of Immunology

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Tick-borne relapsing fever in North America is primarily caused by the spirochete Borrelia hermsii. The pathogen employs multiple strategies, including the acquisition of complement regulators and antigenic variation, to escape innate and humoral immunity. In this study we identified in B. hermsii a novel member of the complement regulator-acquiring surface protein (CRASP) family, designated BhCRASP-1, that binds the complement regulators factor H (FH) and FH-related protein 1 (FHR-1) but not FH-like protein 1 (FHL-1). BhCRASP-1 specifically interacts with the short consensus repeat 20 of FH, thereby maintaining FH-associated cofactor activity for factor I-mediated C3b inactivation. Furthermore, ectopic expression of BhCRASP- 1 converted the serum-sensitive Borrelia burgdorferi B313 strain into an intermediate complement-resistant strain. Finally, we report for the first time that BhCRASP-1 binds plasminogen/plasmin in addition to FH via, however, distinct nonoverlapping domains. The fact that surface-bound plasmin retains its proteolytic activity suggest that the dual binding specificity of BhCRASP-1 for FH and plasminogen/plasmin contributes to both the dissemination/invasion of B. hermsii and its resistance to innate immunity.

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“…Deposition of complement components C3, C6 and C9 (neoantigen) on borrelial cells after incubation with immune sera was investigated by an indirect immunouorescence assay (IFA) as described previously [15]. Borrelial cells (1:25 3 10 7 ) were incubated in veronalbuffered saline (VBS; supplemented with 1 mM Mg 2 , 0.15 mM Ca 2 , gelatin 0.1%, pH 7.3±7.4) 200 ìl containing immune serum 50% at 378C with gentle agitation.…”

Section: Detection Of Deposited Complement Components On the Surfacesmentioning

confidence: 99%

Borreliacidal activity of early Lyme disease sera against complement-resistant Borrelia afzelii FEM1 wild-type and an OspC-lacking FEM1 variant

Kraiczy¹,

Hunfeld

Peters³

et al. 2000

Journal of Medical Microbiology

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Sera obtained from 14 Lyme borreliosis patients at early stages (stages I and II) of the disease were examined for their borreliacidal properties against Borrelia afzelii isolate FEM1 by use of a growth inhibition assay. Five of 14 immune sera exhibited borreliacidal activity against isolate FEM1. Heat-inactivated immune sera failed to kill the spirochaetes. Immunoblotting experiments with outer-membrane preparations showed that OspC and 11 additional proteins of 14.0, 16.0, 17.7, 19.3, 21.7, 27.5, 32.7, 40.7, 48.9, 51.3 and 53.6 kDa were recognised by borreliacidal immune sera. To analyse the borreliacidal properties of anti-OspC antibodies, two sera (EM4 and EM5), which beside antibodies against a 51.3-kDa protein contained exclusively anti-OspC antibodies, were further investigated by comparative analysis with a FEM1 wild-type and a FEM1 variant lacking OspC in a growth inhibition assay. Only FEM1 wild-type and not variant FEM1OspC(2) was killed by immune sera EM4 and EM5. Complementdependent killing of FEM1 wild-type was mediated by formation of the terminal complement complex that was found to be attached directly to the outer membrane as con®rmed by immuno-electron microscopy. No complement deposition was observed on the surface of variant FEM1OspC(2) after incubation with immune sera EM4 and EM5, thereby suggesting that only anti-OspC antibodies in these two immune sera were responsible for borreliacidal activity. These results provide direct evidence that antiOspC antibodies, once developed during the immune response, are of critical importance for ef®cient killing of borreliae in the early phase of infection.

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Comparison of Two Laboratory Methods for the Determination of Serum Resistance in Borrelia burgdorferi Isolates

Cited by 59 publications

References 19 publications

Identification and Functional Characterization of Complement Regulator-Acquiring Surface Protein 1 of the Lyme Disease SpirochetesBorrelia afzeliiandBorrelia garinii

Identification and Functional Characterization of Complement Regulator-Acquiring Surface Protein 1 of the Lyme Disease SpirochetesBorrelia afzeliiandBorrelia garinii

Dual Binding Specificity of a Borrelia hermsii-Associated Complement Regulator-Acquiring Surface Protein for Factor H and Plasminogen Discloses a Putative Virulence Factor of Relapsing Fever Spirochetes

Borreliacidal activity of early Lyme disease sera against complement-resistant Borrelia afzelii FEM1 wild-type and an OspC-lacking FEM1 variant

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