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Preparation and purification of recombinant outer surface protein A (rOspA) of Borrelia burgdorferi sensu stricto and Borrelia afzelii
J. Bĕláková, M. Krupka, M. Sebestová, J. Tuhácková, V. Vrzal, M. Raska, E. Weigl
Language English Country Czech Republic
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Directory of Open Access Journals
from 2001
Free Medical Journals
from 1998
ROAD: Directory of Open Access Scholarly Resources
from 2001
PubMed
16601765
DOI
10.5507/bp.2005.035
Knihovny.cz E-resources
- MeSH
- Antigens, Surface biosynthesis isolation & purification MeSH
- Bacterial Vaccines biosynthesis isolation & purification MeSH
- Borrelia burgdorferi Group immunology MeSH
- Borrelia burgdorferi immunology MeSH
- Vaccines, DNA biosynthesis isolation & purification MeSH
- Escherichia coli MeSH
- Genetic Vectors MeSH
- Lipoproteins biosynthesis isolation & purification MeSH
- Bacterial Outer Membrane Proteins biosynthesis isolation & purification MeSH
- Lyme Disease Vaccines biosynthesis MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
The recombinant Outer surface protein A (rOspA) from Borrelia burgdorferi is a possible immunogen for protection of infected humans and animals against development of Lyme borreliosis (Lyme disease), a chronic tick-borne disease characterised by diverse dermatologic, neurologic, rheumatic, and cardiac manifestations. For several years, research and development have been directed towards a vaccine for the prevention of this debilitating disease. Numerous animal studies demonstrate that pre-existing antibodies against the outer surface proteins of B. burgdorferi can prevent infection and disease caused by this organism. In this communication, using recombinant DNA technology, genes from B. burgdorferi sensu stricto and B. afzelii were inserted into E. coli-expression vectors and the rOspA were produced. Our aim was to obtain rOspA protein in a purity and quantity desirable for immunization of experimental animals. rOspA is currently the most developed, molecularly-defined vaccine candidate for the prevention of Lyme borreliosis.
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