scholarly journals C-Terminal Region of Outer Surface Protein C Binds Borreliacidal Antibodies in Sera from Patients with Lyme Disease

2003 ◽  
Vol 10 (4) ◽  
pp. 573-578 ◽  
Author(s):  
Dean A. Jobe ◽  
Steven D. Lovrich ◽  
Ronald F. Schell ◽  
Steven M. Callister
Keyword(s):  
Lyme Disease ◽  
Outer Surface ◽  
Protein C ◽  
Surface Protein ◽  
Immunoglobulin M ◽  
Enzyme Linked Immunosorbent Assay ◽  
Carboxy Terminus ◽  
Outer Surface Protein ◽  
Serum Titer ◽  
High Concentrations

ABSTRACT Borreliacidal antibodies specific for outer surface protein C (OspC) are induced shortly after infection with Borrelia burgdorferi. In this study, we identified the region of OspC recognized by immunoglobulin M (IgM) and IgG borreliacidal antibodies. Sera from patients with early Lyme disease were screened for borreliacidal activity specific for B. burgdorferi 50772 and OspC antibodies. Seven sera that contained similarly high titers of each response were then chosen randomly and adsorbed with OspC or a truncated OspC (OspC-Dra) containing the 50 amino acids nearest the carboxy terminus. Adsorption with OspC or OspC-Dra completely eliminated the borreliacidal activity in six (86%) of seven sera and significantly decreased the activity in the remaining serum (titer of 10,240 to 1,280). Moreover, OspC antibodies were no longer detected by OspC enzyme-linked immunosorbent assay or in a Western blot that contained native OspC. The findings confirmed that sera from patients with early Lyme disease contain high concentrations of IgM or IgG borreliacidal antibodies that bind a conserved region of OspC.

scholarly journals Antibody response to OspC-I synthetic peptide derived from outer surface protein C of Borrelia burgdorferi in sera from Japanese forestry workers

1999 ◽  
Vol 122 (3) ◽  
pp. 429-433 ◽  
Author(s):  
M. IKUSHIMA ◽  
F. YAMADA ◽  
S. KAWAHASHI ◽  
Y. OKUYAMA ◽  
K. MATSUI
Keyword(s):  
Lyme Disease ◽  
Borrelia Burgdorferi ◽  
Outer Surface ◽  
Synthetic Peptide ◽  
Protein C ◽  
Surface Protein ◽  
Enzyme Linked Immunosorbent Assay ◽  
Igg Antibody ◽  
Forestry Workers ◽  
Outer Surface Protein

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.

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

2020 ◽  
Vol 16 (5) ◽  
pp. e1008516 ◽  
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

Recombinant Outer Surface Protein C Elisa For The Diagnosis Of Early Lyme Disease

1995 ◽  
Vol 171 (3) ◽  
pp. 724-727 ◽  
Author(s):  
M. A. Gerber ◽  
E. D. Shapiro ◽  
G. L. Bell ◽  
A. Sampieri ◽  
S. J. Padula
Keyword(s):  
Lyme Disease ◽  
Outer Surface ◽  
Protein C ◽  
Surface Protein ◽  
Outer Surface Protein

scholarly journals Crystal Structure of Lyme Disease Antigen Outer Surface Protein C fromBorrelia burgdorferi

2001 ◽  
Vol 276 (13) ◽  
pp. 10010-10015 ◽  
Author(s):  
Christoph Eicken ◽  
Vivek Sharma ◽  
Thomas Klabunde ◽  
Rick T. Owens ◽  
Dagmar S. Pikas ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Lyme Disease ◽  
Outer Surface ◽  
Protein C ◽  
Surface Protein ◽  
Outer Surface Protein ◽  
Disease Antigen

scholarly journals Identification and quantification of Lyme pathogen strains by deep sequencing of outer surface protein C (ospC) amplicons

2018 ◽  
Author(s):  
Lia Di ◽  
Zhenmao Wan ◽  
Saymon Akther ◽  
Chunxiao Ying ◽  
Amanda Larracuente ◽  
...  
Keyword(s):  
Lyme Disease ◽  
Deep Sequencing ◽  
Outer Surface ◽  
Protein C ◽  
Surface Protein ◽  
Unique Challenge ◽  
Outer Surface Protein ◽  
Intergenic Sequences ◽  
Pathogen Strains ◽  
Identification And Quantification

AbstractMixed infection of a single tick or host by Lyme disease spirochetes is common and a unique challenge for diagnosis, treatment, and surveillance of Lyme disease. Here we describe a novel protocol for differentiating Lyme strains based on deep sequencing of the hypervariable outer-surface protein C locus (ospC). Improving upon the traditional DNA-DNA hybridization method, the next-generation sequencing-based protocol is high-throughput, quantitative, and able to detect new pathogen strains. We applied the method to over one hundred infectedIxodes scapularisticks collected from New York State, USA in 2015 and 2016. Analysis of strain distributions within individual ticks suggests an overabundance of multiple infections by five or more strains, inhibitory interactions among co-infecting strains, and presence of a new strain closely related toBorreliella bissettiae. A supporting bioinformatics pipeline has been developed. With the newly designed pair of universalospCprimers targeting intergenic sequences conserved among all known Lyme pathogens, the protocol could be used for culture-free identification and quantification of Lyme pathogens in wildlife and clinical specimens across the globe.

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