P39, Strain B31, Recombinant, Borrelia burgdorferi, MBP-Tag

P39 is encoded by the spirochete B. burgdorferi, which is carried by Ixodes ticks. Strain B31 is the type strain (ATCC 35210) for this organism and was derived by limited dilutional cloning from the original Lyme-disease tick isolate obtained by A. Barbour (Johnson, et al., 1984). The p39 protein, or Basic membrane protein A (BmpA), is one of the immunogenic cell membrane components displayed on the outer surface of B. burgdorferi, the spirochete carried by Ixodes ticks and is an important antigen for serodiagnosis of human infection. BmpA is involved in borrelial pathogenicity and participates in the development of borrelial arthritis. It is a member of the chromosomally-located paralogous family 36 which also includes BmpB, BmpC and BmpD. Its expression is co-regulated with that of BmpC and BmpB and may be subject to global regulation (Bryksin, et al., 2010). The spirochete migrates from the tick mid-gut during feeding to its salivary glands and is then transmitted to the mammal host. This transition may be facilitated by changes in expression of some B. burgdorferi genes (Aron, et al., 1996). It is believed that expression of the various proteins associated with the spirochete may be regulated by the changes in tick life cycle, changes in conditions during tick feeding (such as temperature, pH, and nutrients) and/or in coordination with the course of infection of the mammal host. BmpA and its three paralogous proteins, BmpB, C and D, all bind to mammalian laminin and BmpA-directed antibodies, significantly inhibiting the adherence of live B. burgdorferi to laminin. The laminin-binding domain of BmpA was mapped to the 80 C-terminal residues. Solubilized collagen inhibited BmpA-laminin binding, suggesting interactions through the collagen-binding domains of laminin. BmpA does not bind mammalian type I or type IV collagens or fibronectin (Verma, et al., 2009). BmpA is expressed during the invasion of the spirochete and in the evolution of the arthritis of Lyme disease in mammals. The major products of the B. burgdorferi basic membrane protein (bmp) A/B operon that are induced in murine and human joints possess inflammatory properties. Non-lipidated and lipidated versions of BmpA have been shown to induce the pro-inflammatory cytokines TNF-alpha and IL-1beta in human synovial cells. The induction of cytokine responses in synovial cells via activation of the NF-kappaB and p38 MAP kinase pathways could potentially contribute to the pathogenesis of Lyme arthritis (Yang, et al., 2008). Recombinant protein corresponding to Borrelia burgdorferi P39, strain B31, fused to MBP-Tag, expressed in E. coli. , Molecular Weight:, ~77.8kD, Storage and Stability: Aliquot to avoid repeated freezing and thawing and store at -70°C. Aliquots are stable for 6 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.