Identification of a highly cross-reactive outer surface protein B epitope among diverse geographic isolates of Borrelia spp. causing Lyme disease
| Autor: | D. Denee Thomas, M Jonsson, A Sadziene, S Bergström, R J Shoberg |
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| Rok vydání: | 1994 |
| Předmět: |
DNA
Bacterial Microbiology (medical) medicine.drug_class Sequence analysis Molecular Sequence Data Context (language use) Spirochaetaceae Cross Reactions Monoclonal antibody complex mixtures Epitope Microbiology Epitopes Borrelia burgdorferi Group Species Specificity Borrelia medicine Humans Amino Acid Sequence Borrelia burgdorferi DNA Primers Antigens Bacterial Lyme Disease Base Sequence Sequence Homology Amino Acid biology Nucleic acid sequence Antibodies Monoclonal biology.organism_classification Genes Bacterial Mutagenesis Antigens Surface Bacterial Vaccines Bacterial Outer Membrane Proteins Research Article |
| Zdroj: | Journal of Clinical Microbiology. 32:489-500 |
| ISSN: | 1098-660X 0095-1137 |
| DOI: | 10.1128/jcm.32.2.489-500.1994 |
| Popis: | The outer surface lipoprotein B (OspB) of Borrelia burgdorferi is a major component of the borrelial protein profile and has been shown to be highly immunogenic in experimentally immunized and infected mammals. However, the ospB loci of different strains show considerable heterology at the nucleic acid sequence level, and the progeny of a clonal strain of B. burgdorferi exhibited OspB polymorphisms with respect to apparent molecular weights and reactivities with monoclonal antibodies. These data suggest that OspB is not a good candidate for vaccination or diagnostic purposes. The present study describes a monoclonal antibody, designated 84C, directed against a very highly conserved domain of the OspB lipoprotein. Western immunoblot analysis with 84C demonstrated reactivity in 84.2% of human, tick, and other vertebrate isolate strains examined from widely diverse geographic regions, including strains of B. burgdorferi sensu stricto and two closely related species, B. garinii and B. afzelii. The 84C-binding region was delimited to a highly conserved 11-amino-acid region in the carboxyl terminus of OspB as demonstrated by (i) DNA sequence analysis of wild-type and 84C-resistant mutant ospB alleles and (ii) deletion mutagenesis of a recombinant ospB gene in Escherichia coli. Finally, the 84C epitope was demonstrated to be exposed on the borrelial surface in situ as (i) the monoclonal antibody 84C was able to agglutinate borrelias in culture and (ii) 84C-resistant escape variants were isolated. These data suggest that the potential value of OspB as a vaccine candidate or diagnostic tool be examined more closely, in the context of the 84C-reactive domain. |
| Databáze: | OpenAIRE |
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