Borrelia Garinii DbpA
Description
Recombinant Borrelia Garinii Decorin Binding Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 19kDa.
Borrelia Garinii DbpA is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Borrelia garinii is one of the causative agents of Lyme borreliosis, a tick-borne infectious disease. This bacterium, along with Borrelia afzelii and Borrelia burgdorferi sensu stricto, belongs to the Borrelia burgdorferi sensu lato complex. Decorin-binding protein A (DbpA) is a surface-exposed lipoprotein expressed by Borrelia species during mammalian infection. The recombinant form of this protein, Borrelia garinii Decorin Binding Protein A Recombinant, is produced in laboratory settings for research purposes.
DbpA is a helical, surface-displayed lipoprotein with a molecular mass of approximately 19 kDa . It promotes the attachment of Borrelia species to connective tissues and components of the extracellular matrix (ECM), including glycosaminoglycans (GAGs) such as decorin, dermatan sulfate, and heparin . This binding is crucial for the bacterium’s ability to disseminate and persist within the host.
The ability of Borrelia garinii to bind to decorin is significant in the pathogenesis of Lyme borreliosis. Decorin is a proteoglycan associated with collagen fibers in the ECM. By binding to decorin, DbpA facilitates the adherence of Borrelia to host tissues, aiding in the colonization and dissemination of the bacterium . This interaction is particularly important for Borrelia garinii, which has a tendency to cause neuroborreliosis, a form of Lyme disease that affects the nervous system .
Recombinant Borrelia garinii Decorin Binding Protein A is produced in Escherichia coli (E. coli) as a non-glycosylated polypeptide chain . The recombinant protein retains the typical lipid anchor and decorin/glycosaminoglycan binding properties of native DbpA . This recombinant form is used in various research applications, including studies on the molecular mechanisms of Borrelia infection and the development of potential therapeutic interventions.
Research on recombinant DbpA has provided valuable insights into the role of this protein in Borrelia infection. Studies have shown that DbpA and its counterpart, DbpB, are expressed during mammalian infection and mediate bacterial attachment to decorin . Recombinant DbpA has been used to study the binding properties of Borrelia species to decorin and other ECM components, as well as to investigate the potential of DbpA as a target for therapeutic interventions .
