Borrelia OspA

Borrelia Burgdorferi Outer Surface Protein A Recombinant
Cat. No.
BT29293
Source
Escherichia Coli.
Synonyms
Appearance
Sterile Filtered clear solution.
Purity

Greater than 95.0% as determined by SDS-PAGE.

Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Recombinant Borrelia Burgdorferi (strain B31) OspA produced in E.coli is a non-glycosylated, full-length polypeptide chain having a calculated molecular mass of 27kDa.
Borrelia OspA is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Borrelia is a genus of bacteria belonging to the spirochete phylum. These bacteria are responsible for causing borreliosis, a zoonotic vector-borne disease primarily transmitted through ticks and, in some cases, lice, depending on the specific species. Among the 36 recognized species of Borrelia, 12 are known to cause Lyme disease or borreliosis and are spread by ticks. The primary Borrelia species responsible for Lyme disease include Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. Members of the Borrelia genus possess a linear chromosome approximately 900 kbp in length, along with numerous linear and circular plasmids ranging in size from 5 to 220 kbp. Unlike typical bacterial plasmids, these plasmids are unique because they contain multiple paralogous sequences, a significant number of pseudogenes, and, in some instances, essential genes. Furthermore, certain plasmids exhibit characteristics suggesting their potential role as prophages.
Description
Recombinant Borrelia Burgdorferi (strain B31) OspA, produced in E.coli, is a full-length polypeptide chain that is not glycosylated and has a calculated molecular mass of 27kDa. This protein is expressed with a -6x His tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
Borrelia OspA is supplied in a buffer solution containing 20mM HEPES (pH 8.0), 200mM NaCl, and 20% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Minimize repeated freeze-thaw cycles.
Purity
Purity exceeds 95.0% as determined by SDS-PAGE analysis.
Source
Escherichia Coli.

Product Science Overview

Introduction

Borrelia burgdorferi is the causative agent of Lyme disease, a tick-borne illness that affects thousands of people annually, particularly in the northern hemisphere. One of the key proteins associated with Borrelia burgdorferi is the Outer Surface Protein A (OspA). This protein has been extensively studied for its role in the pathogenesis of Lyme disease and its potential as a vaccine target.

Structure and Function of OspA

Outer Surface Protein A (OspA) is a lipoprotein found on the surface of Borrelia burgdorferi. It plays a crucial role in the bacterium’s ability to survive and infect its host. OspA is highly expressed when Borrelia burgdorferi resides in the tick vector, Ixodes spp., and is downregulated once the bacterium enters the mammalian host. This stage-specific expression is essential for the bacterium’s adaptation to different environments.

Recombinant OspA

Recombinant OspA refers to the protein produced through recombinant DNA technology. This involves inserting the gene encoding OspA into an expression vector, which is then introduced into a host cell, such as Escherichia coli, to produce the protein. The recombinant OspA can be purified and used for various applications, including vaccine development.

Vaccine Development

The potential of OspA as a vaccine target was first demonstrated in the early 1990s. Studies showed that immunization with recombinant OspA could induce protective antibodies in mice, preventing infection with Borrelia burgdorferi . This led to the development of a human Lyme disease vaccine based on recombinant OspA, known as LYMErix. LYMErix was approved by the FDA in 1998 and was shown to be safe and effective in preventing Lyme disease in adults and adolescents .

However, LYMErix was withdrawn from the market in 2002 due to poor sales and concerns about potential side effects, despite multiple organizations concluding that it was safe . Research on OspA-based vaccines continues, with newer formulations being developed to improve efficacy and safety.

Mechanism of Protection

The protective mechanism of OspA-based vaccines involves the induction of antibodies that target the protein on the surface of Borrelia burgdorferi. These antibodies can neutralize the bacterium, preventing it from establishing an infection in the host. Additionally, passive transfer of OspA-specific antibodies has been shown to protect immunodeficient mice from infection, further supporting the potential of OspA as a vaccine target .

Current Research and Future Directions

Recent research has focused on improving the immunogenicity and safety of OspA-based vaccines. This includes the development of lipidated forms of recombinant OspA, which have been shown to induce stronger immune responses . Additionally, there is a growing interest in developing vaccines that target the tick vector itself, rather than the pathogen, to prevent the transmission of Lyme disease .

In conclusion, Borrelia burgdorferi Outer Surface Protein A (OspA) remains a promising target for Lyme disease vaccine development. Advances in recombinant DNA technology and a better understanding of the protein’s role in the bacterium’s life cycle have paved the way for new and improved vaccines that could significantly reduce the incidence of Lyme disease.

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