Borrelia DbpB
Description
Borrelia DbpB is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Borrelia burgdorferi is the causative agent of Lyme disease, a tick-borne illness that affects various tissues in the human body. One of the critical factors in the pathogenesis of Borrelia burgdorferi is its ability to adhere to host tissues. This adhesion is mediated by several surface proteins, including the decorin-binding proteins (Dbps) A and B. These proteins play a crucial role in the bacterium’s ability to establish infection and cause disease.
Decorin is a collagen-associated extracellular matrix proteoglycan found in the skin and other tissues. Borrelia burgdorferi expresses two decorin-binding proteins, DbpA and DbpB, which facilitate the bacterium’s attachment to decorin. This interaction is essential for the spirochete’s colonization and persistence in the host.
Recombinant DbpB refers to the decorin-binding protein B that has been produced using recombinant DNA technology. This involves cloning the gene encoding DbpB into an expression vector, which is then introduced into a host organism, such as Escherichia coli, to produce the protein in large quantities. Recombinant DbpB is used in various research applications to study its structure, function, and role in Lyme disease pathogenesis.
DbpB, along with DbpA, mediates the attachment of Borrelia burgdorferi to decorin in the host’s extracellular matrix. This binding is crucial for the bacterium’s ability to establish infection, particularly in the early stages of Lyme disease. Studies have shown that recombinant DbpB can bind to decorin and support the adhesion of Borrelia burgdorferi to decorin-expressing cells . This interaction is vital for the spirochete’s ability to colonize and persist in the host tissues.
The immune response to DbpB has been a subject of interest in Lyme disease research. Infection with Borrelia burgdorferi elicits antibodies against DbpB, indicating that this protein is expressed in vivo and recognized by the host immune system . Passive administration of DbpB antiserum has been shown to protect mice from infection, suggesting that DbpB could be a potential target for immunoprophylaxis .
