A new specific serodiagnosis system for Lyme disease: use of synthetic peptides derived from outer surface protein C of Borrelia burgdorferi

The prevalence of antibodies against Lyme disease spirochaetes in serum samples from 80 forestry workers at high occupational risk of Lyme disease was surveyed by enzyme-linked immunosorbent assay (ELISA) with the OspC-I synthetic peptide. The peptide is part of the outer surface protein C (OspC) amino acid sequence located in the region conserved among Borrelia burgdorferi sensu stricto or sensu lato. Positivity for antibodies against OspC-I was observed in 25 (31·3%) of the forestry workers. Of these positive cases, 12 (15·0%) and 19 (23·8%) were positive for immunoglobulin M (IgM) and IgG antibody, respectively. Among 62 workers who were negative for IgG antibody against B. garinii or B. japonica in our previous study, 9 (14·5%) and 4 (6·5%) were positive for IgM and IgG antibody, respectively, in OspC-I ELISA. These results demonstrate for the first time that Lyme disease in forestry workers can be revealed using OspC-I ELISA. We conclude that forestry workers who show positive results for antibodies against OspC-I have very likely been exposed to Lyme disease spirochaetes, and that those who show positivity for IgM antibody against OspC-I may be in the early stage of Lyme disease.

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Faculty Opinions recommendation of Outer-surface protein C of the Lyme disease spirochete: a protein induced in ticks for infection of mammals.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1018462.209504 ◽

2004 ◽

Author(s):

Daniel Dykhuizen

Keyword(s):

Lyme Disease ◽

Outer Surface ◽

Protein C ◽

Surface Protein ◽

Outer Surface Protein

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Strain-specific joint invasion and colonization by Lyme disease spirochetes is promoted by outer surface protein C

PLoS Pathogens ◽

10.1371/journal.ppat.1008516 ◽

2020 ◽

Vol 16 (5) ◽

pp. e1008516 ◽

Cited By ~ 2

Author(s):

Yi-Pin Lin ◽

Xi Tan ◽

Jennifer A. Caine ◽

Mildred Castellanos ◽

George Chaconas ◽

...

Keyword(s):

Lyme Disease ◽

Outer Surface ◽

Protein C ◽

Surface Protein ◽

Outer Surface Protein

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Vaccination against Lyme Disease with recombinant Borrelia burgdorferi outer-surface protein A (rOspA) in horses

Vaccine ◽

10.1016/s0264-410x(99)00187-5 ◽

1999 ◽

Vol 18 (5-6) ◽

pp. 540-548 ◽

Cited By ~ 25

Author(s):

Y Chang

Keyword(s):

Lyme Disease ◽

Borrelia Burgdorferi ◽

Outer Surface ◽

Protein A ◽

Surface Protein ◽

Outer Surface Protein A ◽

Outer Surface Protein

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Constitutive Expression of Outer Surface Protein C Diminishes the Ability of Borrelia burgdorferi To Evade Specific Humoral Immunity

Infection and Immunity ◽

10.1128/iai.00713-06 ◽

2006 ◽

Vol 74 (9) ◽

pp. 5177-5184 ◽

Cited By ~ 55

Author(s):

Qilong Xu ◽

Sunita V. Seemanapalli ◽

Kristy McShan ◽

Fang Ting Liang

Keyword(s):

Borrelia Burgdorferi ◽

Outer Surface ◽

Protein C ◽

Severe Combined Immunodeficiency ◽

Constitutive Expression ◽

Surface Protein ◽

Start Codon ◽

Chronic Infections ◽

Translational Initiation ◽

Outer Surface Protein

ABSTRACT The Lyme disease spirochete Borrelia burgdorferi reduces the expression of outer surface protein C (OspC) in response to the development of an anti-OspC humoral response, leading to the hypothesis that the ability to repress OspC expression is critical for the pathogen to proceed to chronic infection. B. burgdorferi was genetically modified to constitutively express OspC by introducing an extra ospC copy fused with the borrelial flagellar gene (flaB) promoter. Such a genetic modification did not reduce infectivity or pathogenicity in severe combined immunodeficiency mice but resulted in clearance of infection by passively transferred OspC antibody. Spirochetes with constitutive ospC expression were unable to establish chronic infections in immunocompetent mice unless they had undergone very destructive mutations in the introduced ospC copy. Two escape mutants were identified; one had all 7 bp deleted between the putative ribosome-binding site and the start codon, ATG, causing a failure in translational initiation, and the other mutant had an insertion of 2 bp between nucleotides 315 and 316, resulting in a nonsense mutation at codon 108. Thus, the ability of B. burgdorferi to repress ospC expression during mammalian infection allows the pathogen to avoid clearance and to preserve the integrity of the important gene for subsequent utilization during its enzootic life cycle.

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