Decorin-binding protein B, or DbpB, binds to decorin, which may mediate the adherence of B.burgdorferi to collagen fibers in skin and other tissues. Spirochetal surface adhesions mediate attachment to decorin, a major component of the host extracellular matrix enabling bacteria to colonize in mammalian tissues. The spirochete migrates from the tick midgut during feeding to its salivary glands and are thus transmitted to the mammal host. This transition may be facilitated by changes in expression of some B. burgdorferi genes. 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. Borrelia burgdorferi can colonize multiple tissues, and is capable of attachment to diverse cell types. The expression of decorin-binding protein (Dbp) A and/or DbpB, two B. burgdorferi surface proteins that bind GAGs, is sufficient to convert a high-passage nonadherent B. burgdorferi strain into one that efficiently binds 293 epithelial cells. Lyme disease proteins are ideal for researchers interested in immunology, neurology, and rheumatology, coinfections , autoimmune, and neurodegenerative diseases.