Serologic response to the Borrelia burgdorferi flagellin demonstrates an epitope common to a neuroblastoma cell line.

Fikrig, Erol; Berland, Robert; Chen, Manchuan; Williams, Stephanie; Sigal, Leonard H.; Flavell, Richard A.

doi:10.1073/pnas.90.1.183

Cited by 37 publications

(16 citation statements)

References 21 publications

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“…Which part of the flagellin provides the highest degree of sensitivity and specificity and, therefore, should be used as diagnostic antigen has been discussed by a number of authors [7,14,21,25,29,30,32]. It was clear from these studies (which used flagellin fragments derived from B. burgdorferi sensu stricto strains) that increasing the size of the fragments resulted in a gain of sensitivity but also in a loss of specificity.…”

Section: Igg Antibody Detectionmentioning

confidence: 93%

Immunoblot using recombinant antigens derived from different genospecies of Borrelia burgdorferi sensu lato

Wilske

Fingerle

Preac-Mursic

et al. 1994

Med Microbiol Immunol

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Immunodominant proteins are variable in molecular and antigenic structure among different genospecies of Borrelia burgdorferi sensu lato. We have recently developed an immunoblot using five recombinant antigens: the chromosomal-encoded B. burgdorferi proteins p100, the flagellin and an internal flagellin fragment thereof, and the plasmid-encoded outersurface proteins A (OspA) and C (OspC). In the present study the same antigens (derived from strain PKo, genospecies B. afzelii) were compared with the homologous recombinant proteins from strain B31 (genospecies B. burgdorferi sensu stricto) and with OspA, OspC and the internal flagellin fragment from strain PBi (genospecies B. garinii). Patients with neuroborreliosis (n = 28) and patients with acrodermatitis chronica atrophicans (n = 20) were investigated in the IgG immunoblot; the IgM immunoblot was performed only in patients with neuroborreliosis. There was a small increase in the detection rate of OspA-specific IgG or IgM antibodies using the different variants of recombinant OspA; however, OspA remained an insensitive antigen for antibody detection in Lyme borreliosis. The same was true to OspC-specific IgG antibodies. The sensitivity of OspC, which is the immunodominant antigen for IgM antibody detection, could not be increased using recombinant antigens derived from different strains. However, some sera which were negative in the recombinant immunoblot reacted with OspC in the conventional immunoblot using B. burgdorferi whole cell lysate as antigen. The most unexpected finding was the high degree of immunological heterogeneity of the internal flagellin fragments: IgG antibodies were detected in 18 of 48 patients using B31 fragments, in 25 of 48 using PKo fragments, in 23 of 48 using PBi fragments versus 33 of 48 when the three recombinant proteins were combined. PKo-derived fragments were more sensitive for antibody detection in patients with acrodermatitis chronica atrophicans, B31- and PBi-derived fragments for antibody detection in patients with neuroborreliosis. This is in agreement with the fact that isolates from patients with neuroborreliosis are predominantly belonging to the genospecies B. burgdorferi sensu stricto and B. garinii. For detection of IgM antibodies in sera from patients with neuroborreliosis, recombinant internal fragments derived from strains B31 and PBi were more sensitive than the PKo-derived fragment. The best discrimination between neuroborreliosis sera and control sera was achieved when the IgM blot was performed using recombinant internal flagellin fragments derived from strains PKo and PBi and OspC derived from B31 or PKo.

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Section: Igg Antibody Detectionmentioning

confidence: 93%

Immunoblot using recombinant antigens derived from different genospecies of Borrelia burgdorferi sensu lato

Wilske

Fingerle

Preac-Mursic

et al. 1994

Med Microbiol Immunol

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“…B. burgdorferi N40 whole cell lysates or recombinant OspA or B was used as the substrate for ELISA (27 24,27). Proteins were transferred to nitrocellulose paper and the resulting strips were blocked in 5% bovine serum albumin (BSA) for 90 min and then incubated with murine serum (1:1,000 dilution) in 5% BSA for 1 h. The strips were washed three times with PBS and bound antibody was detected by incubation with goat anti-mouse IgG or IgM secondary antibody-conjugated to horseradish peroxidase using the enhanced chemiluminescence immunoblotting detection system (Amersham, Arlington Heights, IL).…”

Section: Introductionmentioning

confidence: 99%

Lyme borreliosis in transgenic mice tolerant to Borrelia burgdorferi OspA or B.

et al. 1995

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“…B. burgdorferi lysates, murine tissue, or epitopes of flagellin expressed as glutathione transferase fusion proteins were resolved by SDS‐PAGE [7]. The fusion proteins expressed flagellin fragment F (aa 197–241), the central region that reacts with B. burgdorferi antibodies, and F5 (flagellin aa 212–25), the epitope that includes the region that binds with cross‐reactive antibodies [7].…”

Section: Methodsmentioning

confidence: 99%

“…Antibodies to the B. burgdorferi flagellin, elicited during the course of infection, have been shown to bind to human axons and therefore may be implicated in the pathogenesis of neurologic disease [1, 2, 6]. The specificity of these cross‐reactive antibodies has been mapped to a 12‐amino acid (aa) epitope (aa 213–24) in the central region of the B. burgdorferi flagellin [7]. Moreover, the antigen to which these antibodies bind in human tissue has been identified as an endogenously expressed 60‐kDa heat shock protein [8, 9].…”

Section: Introductionmentioning

confidence: 99%

Lyme disease in transgenic mice expressing the Borrelia burgdorferi flagellin epitope implicated in human neuroborreliosis

Fikrig

Barthold

2006

FEMS Microbiology Letters

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Because of an association of human neuroborreliosis with the development of an antibody response against an antigen in neural tissue that cross-reacts with an epitope on the flagellin protein of Borrelia burgdorferi, C3H transgenic mice were created that expressed the flagellin epitope (amino acids 213-224) as a fusion protein with myelin basic protein. The transgenic mice expressed the flagellin epitope selectively in myelinated regions of the nervous system. Both transgenic and non-transgenic mice developed an antibody response to the flagellin epitope during B. burgdorferi infection and both developed arthritis and carditis. However, no lesions were found in the central nervous system of either type of mouse for up to 8 weeks after infection. The data indicate that expression of the flagellin 213-24 epitope in mice does not result in neurologic disease, suggesting that B. burgdorferi flagellin antibodies may not be directly implicated in neuroborreliosis.

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Serologic response to the Borrelia burgdorferi flagellin demonstrates an epitope common to a neuroblastoma cell line.

Cited by 37 publications

References 21 publications

Immunoblot using recombinant antigens derived from different genospecies of Borrelia burgdorferi sensu lato

Immunoblot using recombinant antigens derived from different genospecies of Borrelia burgdorferi sensu lato

Lyme borreliosis in transgenic mice tolerant to Borrelia burgdorferi OspA or B.

Lyme disease in transgenic mice expressing the Borrelia burgdorferi flagellin epitope implicated in human neuroborreliosis

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