Characterization of Borrelia burgdorferi Associated Antigens by Monoclonal Antibodies

Kramer, Michael D.; Schaible, U. E.; Wallich, Reinhard; Moter, S E; Petzoldt, D; Simon, Markus M.

doi:10.1016/s0171-2985(11)80504-8

Cited by 64 publications

(53 citation statements)

References 24 publications

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“…On the other hand, the comparison of our isolates with the strain B31 showed that only two isolates presented exactly the same reactivity with the MoAbs described by Barbour and colleagues [8], Kramer and colleagues [15] and Wallich and colleagues [12]. In view of this, it is suggested that European isolates could elicit specific antibody responses during infection, which differ from one site to another site and which is different from that induced by the strain B31.…”

Section: Discussionsupporting

confidence: 65%

“…The monoclonal antibodies (MoAbs): H5332, LA-2, LA-4, LA-31 (anti-OspA) [8,15], LA-25, LA-27 (anti-OspB) [15], LA-7 (anti-20 kDa protein) [15], and polyclonal antibodies (PoAbs): anti-22 kDa/NE4 [14] and anti-B31, produced by immunizing a New Zealand white rabbit with strain B31 [9], were used for immuno-blotting. Bound antibodies were visualized by using peroxidase labelled anti-rabbit IgG or anti-mouse IgG antibodies (1: 1000, Nordic Immunological Laboratories, The Netherlands).…”

Section: Sds-page and Immunoblot Analysismentioning

confidence: 99%

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Comparison in the immunological properties ofBorrelia burgdorferiisolates fromIxodes ricinusderived from three endemic areas in Switzerland

Leuba-Garcia

Kramer

et al. 1994

Epidemiol. Infect.

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SUMAIMARYBorrelia burgdorferi isolates were obtained from Ixodes ricinus from three sites in Switzerland. They were examined by SDS-PAGE and immunoblotting. The phenotypes, in respect of three outer surface proteins (Osp), differed between the sites of collection. In site 1, most isolates had an OspA of 31 kDa and an OspB of 34 kDa; in site 2, isolates presenting an OspA of 33 kDa dominated and in site 3, the isolates with an OspA of 32 kDa and an OspB of 35 kDa were most frequent. This distribution differed significantly. About half of the isolates from sites 1 and 3 reacted with anti-OspA monoclonal antibody H5332 compared to 29 % from site 2. Site 1 isolates reacted significantly more frequently (81 %) with another antiOspA monoclonal antibody LA-31 than isolates from site 3 (P < 0 0001). These findings have implications for the epidemiology of Lyme borreliosis, for the further development of serodiagnostic reagents and for the development of a vaccine.

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Section: Discussionsupporting

confidence: 65%

Section: Sds-page and Immunoblot Analysismentioning

confidence: 99%

Comparison in the immunological properties ofBorrelia burgdorferiisolates fromIxodes ricinusderived from three endemic areas in Switzerland

Leuba-Garcia

Kramer

et al. 1994

Epidemiol. Infect.

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“…Generation of Monoclonal BBA70 Antiserum-Monoclonal antibody 70-11/10.17 directed against BBA70 was generated by immunization of BALB/c mice with recombinant ZSA70 protein according to a method described elsewhere (45). Animal research was approved in advance by the Laboratory Animal Committee of the University of Heidelberg (RP Karlsruhe 35-9185.82/A-25/07).…”

Section: Methodsmentioning

confidence: 99%

BBA70 of Borrelia burgdorferi Is a Novel Plasminogen-binding Protein

Koenigs

Hammerschmidt

Jutras

et al. 2013

Journal of Biological Chemistry

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Background: Recruitment of plasminogen is important for efficient dissemination of Borrelia burgdorferi. Results: BBA70 of B. burgdorferi binds plasminogen, and following activation, bound plasmin can cleave fibrinogen and inactivate the key complement components C3b and C5. Conclusion: BBA70 is a potent plasminogen-binding protein.Significance: Investigation suggests that binding of plasminogen may aid in pathogen dissemination and inhibit bacteriolytic effects of the host complement system.

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“…Generation of mAb LA3 against Hsp70, LA22.1 against flagellin, LA27 against OspA, and LA28.1 OspB were described elsewhere (46).…”

Section: Construction Of Expression Plasmids and Purification Of Recomentioning

confidence: 99%

Complement Resistance of Borrelia burgdorferi Correlates with the Expression of BbCRASP-1, a Novel Linear Plasmid-encoded Surface Protein That Interacts with Human Factor H and FHL-1 and Is Unrelated to Erp Proteins

Kraiczy

Hellwage

Skerka

et al. 2004

Journal of Biological Chemistry

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215

217

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The etiologic agent of Lyme disease, Borrelia burgdorferi, is capable of circumventing the immune defense of a variety of potential vertebrate hosts. Previous work has shown that interaction of host-derived complement regulators, factor H and factor H-like protein 1 (FHL-1), with up to five complement regulator-acquiring surface proteins (CRASPs) expressed by resistant B. burgdorferi sensu lato isolates conferred complement resistance. In addition expression of CRASP-1 is directly correlated with complement resistance of Borrelia species. This work describes the functional characterization of BbCRASP-1 as the dominant factor H and FHL-1-binding protein of B. burgdorferi. The corresponding gene, zs7.a68, is located on the linear plasmid lp54 and is different from factor H-binding Erp proteins that are encoded by genes localized on circular plasmids (cp32). Deletion mutants of BbCRASP-1 were generated, and a high affinity binding site for factor H and FHL-1 was mapped to the C terminus of BbCRASP-1. Similarly, the predominant binding site of factor H and FHL-1 was localized to the short consensus repeat 7. Factor H and FHL-1 maintain their cofactor activity for factor I-mediated C3b inactivation when bound to BbCRASP-1, and factor H is up to 6-fold more efficient in mediating C3b conversion than FHL-1. In conclusion, BbCRASP-1 (i) binds the host complement regulators factor H and FHL-1 with high affinity, (ii) is the key molecule of the complement resistance of spirochetes, and (iii) is distinct from the Erp protein family. Thus, BbCRASP-1 most likely contributes to persistence of B. burgdorferi and to pathogenesis of Lyme disease.

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Characterization of Borrelia burgdorferi Associated Antigens by Monoclonal Antibodies

Cited by 64 publications

References 24 publications

Comparison in the immunological properties ofBorrelia burgdorferiisolates fromIxodes ricinusderived from three endemic areas in Switzerland

Comparison in the immunological properties ofBorrelia burgdorferiisolates fromIxodes ricinusderived from three endemic areas in Switzerland

BBA70 of Borrelia burgdorferi Is a Novel Plasminogen-binding Protein

Complement Resistance of Borrelia burgdorferi Correlates with the Expression of BbCRASP-1, a Novel Linear Plasmid-encoded Surface Protein That Interacts with Human Factor H and FHL-1 and Is Unrelated to Erp Proteins

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