In Vitro Inhibition of Borrelia burgdorferi Growth by Antibodies

Sadziene, A; Thompson, Patricia A.; Barbour, Alan G.

doi:10.1093/infdis/167.1.165

Cited by 129 publications

(152 citation statements)

References 36 publications

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“…Therefore, OspA-ACA-1 or OspA-ZQ-1 antisera effectively bound to, but did not kill, B. burgdorferi N40. Moreover, in a standard agglutination assay (34), neither of these OspA antisera resulted in appreciable agglutination of N40 spirochetes (data not shown). .…”

Section: Characterization Of Ospa Absmentioning

confidence: 88%

Inhibition of Borrelia burgdorferi-Tick Interactions In Vivo by Outer Surface Protein A Antibody

Pal

Montgomery

Lusitani

et al. 2001

The Journal of Immunology

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Borrelia burgdorferi outer surface protein (Osp) A is preferentially expressed by spirochetes in the Ixodes scapularis gut and facilitates pathogen-vector adherence in vitro. Here we examined B. burgdorferi-tick interactions in vivo by using Abs directed against OspA from each of the three major B. burgdorferi sensu lato genospecies: B. burgdorferi sensu stricto, Borrelia afzelii, and Borrelia garinii. Abs directed against B. burgdorferi sensu stricto (isolate N40) destroy the spirochete and can protect mice from infection. In contrast, antisera raised against OspA from B. afzelii (isolate ACA-1) and B. garinii (isolate ZQ-1) bind to B. burgdorferi N40 but are not borreliacidal against the N40 isolate. Our present studies assess whether these selected OspA Abs interfere with B. burgdorferi-tick attachment in a murine model of Lyme disease with I. scapularis. We examined engorged ticks that had fed on B. burgdorferi N40-infected scid mice previously treated with OspA (N40, ACA-1, ZQ-1, or mAb C3.78) or control Abs. OspA-N40 antisera or mAb C3.78 destroyed B. burgdorferi N40 within the engorged ticks. In contrast, treatment of mice with OspA-ACA-1 and OspA-ZQ-1 antisera did not kill B. burgdorferi N40 within the ticks but did effectively interfere with B. burgdorferi-I. scapularis adherence, thereby preventing efficient colonization of the vector. These studies show that nonborreliacidal OspA Abs can inhibit B. burgdorferi attachment to the tick gut, highlighting the importance of OspA in spirochete-arthropod interactions in vivo.

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Section: Characterization Of Ospa Absmentioning

confidence: 88%

Inhibition of Borrelia burgdorferi-Tick Interactions In Vivo by Outer Surface Protein A Antibody

Pal

Montgomery

Lusitani

et al. 2001

The Journal of Immunology

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“…In the current study, we assessed cell binding by B. burgdorferi strain B314, a high-passage strain that has lost the linear plasmid that encodes DbpA and DbpB (28). Several other (putative) B. burgdorferi adhesins, such as Bgp or p66 could potentially promote cell attachment, and in fact, immunoblot analysis revealed that Bgp is expressed by B314 (N.P., unpublished observation).…”

Section: Discussionmentioning

confidence: 99%

“…B314, a high-passage derivative of the B. burgdorferi B31 strain, has lost several plasmids including lp54, which encodes the dbp operon (28,47), and preliminary experiments showed that B314 spirochetes do not adhere to cultured mammalian cells (see Fig. 4 below).…”

Section: Expression Of Dbpa and Dbpb Is Sufficient To Convert A Nonadmentioning

confidence: 99%

“…First, the traditional approach of testing antibodies directed against bacterial surface molecules for the ability to block attachment activity is problematic because many such antibodies, including some directed against DbpA, are lethal to B. burgdorferi (28)(29)(30). Second, B. burgdorferi encodes a number of potential adhesins that could contribute to cell attachment, including another GAG-binding protein, Bgp, which binds to dermatan sulfate and heparin (31), the integrin-binding protein p66 (32), and the fibronectin-binding protein BBK032 (33).…”

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confidence: 99%

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Decorin-binding proteins A and B confer distinct mammalian cell type-specific attachment by Borrelia burgdorferi , the Lyme disease spirochete

Fischer

Parveen

Magoun

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

110

149

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Host cell binding is an essential step in colonization by many bacterial pathogens, and the Lyme disease agent, Borrelia burgdorferi, which colonizes multiple tissues, is capable of attachment to diverse cell types. Glycosaminoglycans (GAGs) are ubiquitously expressed on mammalian cells and are recognized by multiple B. burgdorferi surface proteins. We previously showed that B. burgdorferi strains differ in the particular spectrum of GAGs that they recognize, leading to differences in the cultured mammalian cell types that they efficiently bind. The molecular basis of these binding specificities remains undefined, due to the difficulty of analyzing multiple, potentially redundant cell attachment pathways and to the paucity of genetic tools for this pathogen. In the current study, we show that the expression of decorin-binding protein (

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“…Many studies in experimental animals demonstrated that humoral immunity protects against infection with B. burgdorferi (Johnson et al, 1986;Barthold and Bockenstedt, 1993;Fikrig et al, 1996;Sadziene et al, 1993;Schaible et al, 1990). These observations generated much interest in the development of a LD vaccine.…”

Section: E Vaccinementioning

confidence: 99%

Characterization of secA-sod operon in Borrellia burgdorferi.

Nichols¹

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Borrelia burgdorferi, the causative agent of Lyme disease, has been characterized as a microaerophilic spirochete. O2 consumption and utilization potentially yield reactive oxygen intermediates, such as superoxide, hydroxyl radicals, and hydrogen peroxide. This study investigated the expression of the sod gene, which encodes the only, identified oxidative defense mechanism in B. burgdorferi. Using primer extension analysis and RT-PCR, it was found that sod and secA are organized as a single transcriptional unit under the control of σ 70 -like promoter upstream of the secA open reading frame. Generally, gene expression decreases with increased distance from the promoter; however, secA expression was observed to be relatively lower amounts than sod. Both genes were expressed in all phases of growth, with greatest expression observed in stationary phase. Because transcription of most sod genes is tightly regulated by iron concentration, the secA-sod gene expression was analyzed in borrelial cells grown in varying amounts of metal. Ironrestriction did not significantly affect growth nor did it affect transcription of secA or sod.Likewise, no major differences in transcription were observed with restricting or supplementing media with manganese. To test the possibility that the borrelial SOD may function with either iron or manganese as a cofactor as in cambialistic SODs, SOD activity was assayed and the highest activity was observed in increased manganese concentrations.Protein expression profiles of Sh-2-82 cultured in metal-defined media were investigated by one-and two-dimensional gel electrophoresis. Approximately 15 proteins were differentially expressed in response to metal concentration. iv ACKNOWLEDGMENTS

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In Vitro Inhibition of Borrelia burgdorferi Growth by Antibodies

Cited by 129 publications

References 36 publications

Inhibition of Borrelia burgdorferi-Tick Interactions In Vivo by Outer Surface Protein A Antibody

Inhibition of Borrelia burgdorferi-Tick Interactions In Vivo by Outer Surface Protein A Antibody

Decorin-binding proteins A and B confer distinct mammalian cell type-specific attachment by Borrelia burgdorferi , the Lyme disease spirochete

Characterization of secA-sod operon in Borrellia burgdorferi.

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