Proteins & Peptides

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. Lyme disease proteins are ideal for researchers interested in immunology, neurology

ErpD (ospE/F-Related Protein D), also known as Arp37, is from the spirochete Borrelia burgdorferi, which is carried by Ixodes ticks. Erp proteins from Borrelia burgdorferi are postulated to be lipoproteins, based on their predicted amino acid sequences. 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. Several studies have demonstrated that infected humans and animals produce antibodies directed against Erp proteins within the first 2-4 weeks of infection, indicative of Erp synthesis during the initial stages of vertebrate infec

ErpN (OspE/F-Related Protein N), is from the spirochete Borrelia burgdorferi, which is carried by Ixodes ticks. Erp proteins from Borrelia burgdorferi are postulated to be lipoproteins, based on their predicted amino acid sequences. 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. Several studies have demonstrated that infected humans and animals produce antibodies directed against Erp proteins within the first 2-4 weeks of infection, indicative of Erp synthesis during the initial stages of vertebrate infection. It is postulat

Outer Surface Protein C, or OspC, is a 20.7 kDa immunogenic protein on the outer surface of the spirochete Borrelia burgdorferi. Its function is not known, but it is located with lipid-anchoring sites on the outer cell membrane. Lyme disease proteins are ideal for researchers interested in immunology, neurology, rheumatology, coinfections, autoimmune, and neurodegenerative diseases.

The p35 kDa protein of the spirochete Borrelia burgdorferi is being investigated for use as an early diagnostic marker of Lyme Disease. Borrelia may change its antigenic composition in its need for adaptation to stresses imposed by changes in conditions from cycling between its arthropod and mammalian hosts. This group of B. burgdorferi proteins may be induced in the tick midgut during the feeding event. The p35 protein elicits a protective immunity from wild type B. burgdorferi. It has been shown that p35 expression in B. burgdorferi is upregulated in the stationary growth phase, and that a temperature of 34°C but not 24°C influenced the expression. The expression of a majority of the proteins expressed in early Lyme disease is affected pH, being abundantly expressed at pH 7.0 (resembling the tick midgut pH of 6.8 during feeding) but only sparsely at pH 8.0 (a condition closer to that of the unfed tick midgut pH of 7.4). The encoding genes may be coregulated. The 35-kDa antigen

Outer-Surface Protein A (OspA), a lipoprotein from Borrelia burgdorferi encoded on its Plasmid lp54, is a major component of the spirochete's extracellular matrix. OspA probably serves as a lipid-anchor. The spirochetes migrate 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. Upon transmission of the spirochete from the Ixodes tick to mammalian host, the transcript level of OspA can change. 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. B. burgdorferi can attach to (and also differentially express antigens in) diverse tissues within the vertebrate host and the tick vector, suggesting that physiol

Flagellin is a protein found in the hollow cylinder forming the filament in bacterial flagellum. Its structure is helical, which is important for its function. Studies comparing a flagellate Borrelia to flagellated indicate that the flagella have a role in the invasion of human tissue. The N- and C-termini of flagellin form the inner core of the flagellar filament, and the central portion of the protein makes up the outer surface. While the terminus of the protein is quite similar between all bacterial flagellins, the central portion is variable. The flagellin genes are highly conserved among the different Borrelia species. Mammals often have acquired immune responses (T-cell and antibody responses) to flagellated bacterium. Some bacteria are able to switch between multiple flagellin genes in order to evade this response. Borrelia burgdorferi, the spirochete that is associated with Lyme Disease, may use this tactic when challenging mammals with infection. Borrelia have double-

OspB, is one of the major Outer Surface Proteins of the outer membrane of Borrelia burgdorferi, which is composed of various unique outer surface proteins (Osp) that have been characterized (OspA through OspF). The Osp proteins are lipoproteins anchored by N-terminally attached fatty acid molecules to the membrane. They are presumed to play a role in virulence, transmission, or survival in the tick. Two of the major surface Ag of Borrelia burgdorferi, the 31-kDa OspA and 34-kDa OspB proteins, show a high degree of sequence similarity, are encoded by a 49-kb plasmid and share a common promoter, and are coordinately transcribed. OspA, OspB, and OspD are expressed by B. burgdorferi residing in the gut of unfed ticks, suggesting that they promote the persistence of the spirochete in ticks between blood meals. OspB has a contributing role in the adherence of B. burgdorferi to the tick gut. The C terminus of OspB is important for eliciting a protective immune response to OspB. B. burg

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, tw