84-5136-45　［取扱停止］DbpA, Borrelia burgdorferi 100ug　516579

特徴

• B.
• burgdorferi sensu stricto has a linear plasmid (lp54) which carries a two-gene operon encoding two surface lipoproteins, DbpA and DbpB, both of which bind Decorin Binding Protein A (DbpA).
• It should be noted that other microbial DbpA’s, such as E.
• coli (ATP-dependent RNA helicase DbpA), are significantly different to Borrelia DbpA (Guo, et al., 1995).
• DbpA and DbpB are surface-exposed outer membrane lipoproteins that mediate the attachment of Borrelia to decorin, a major component of the host extracellular matrix, enabling bacteria to colonize mammalian tissues (Roberts, et al., 1998).
• Both can mediate interaction with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (Guo, et al., 1998), but only DbpB binds chondroitin sulfate (Fischer, et al., 2003).
• The spirochete travels from the tick mid-gut during tick feeding, to the tick salivary glands and into the mammal host, and it is believed that this migration is facilitated by changes in expression of different B.
• burgdorferi genes.
• It is thought 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.
• While not expressed in the unfed tick, DbpA (and possibly DbpB) are quickly upregulated, either during feeding or after entry, into the host.
• The location of DbpA and DbpB in the outer membrane of B.
• burgdorferi allows exposure of these proteins to the host immune system.
• DbpA has also been used to show high levels of genetic diversity in B.
• afzelii-infected rodent hosts, by qPCR (Coipan, et al., 2018).
• NMR and a crystal structure of a DbpA monomer (resolution of 1.60 Å) confirmed three lysines co-localize with decorin to a common basic patch near the C-terminal of the protein (Wang & Feng, 2015; Fortune, et al., 2014).
• Knockout strains confirmed that the lysine residues are required for binding and infection in mice (Fortune, et al., 2014).
• Strain-specific variations of Borrelia surface proteins also affect tissue tropism (Lin, et al., 2014) as well as differences in GAG binding affinities which is correlated with differences in GAG-binding pocket location and epitope number (Morgan & Wang, 2015).
• Applications:Suitable for use in ELISA.
• Other applications not tested.
• Recommended Dilution:Optimal dilutions to be determined by the researcher.
• Storage and Stability:May be stored at 4°C for short-term only.
• Aliquot to avoid repeated freezing and thawing.
• Store at -20°C.
• Aliquots are stable for 12 months after receipt.
• For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.