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DbpA, or Decorin Binding Protein A, is from the spirochete Borrelia burgdorferi, which is carried by Ixodes ticks. DbpA from other microbial organisms such as E. coli (ATP-dependent RNA helicase DbpA) are significantly different. The spirochete migrates from the tick midgut during tick feeding to tick salivary glands and are thus transmitted to the mammal host. This transition may be facilitated by changes in expression of some B. burgdorferi genes. Spirochetal surface adhesions mediate attachment to decorin, a major component of the host extracellular matrix, enabling bacteria to colonize in mammalian tissues. 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.
cold shock domain protein A; cold shock domain-containing protein A; cold-shock domain containing A1; cold-shock domain protein A; CSDA; CSDA1; DBPA; DNA-binding protein A; Single-strand DNA-binding protein NF-GMB; Y box binding protein 3; Y-box binding protein 3; Y-box-binding protein 3; YBX3; ZO-1-associated nucleic acid-binding protein; ZONAB
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