Anti-Surface Lipoprotein p27

Surface Lipoprotein p27 of Borrelia burgdorferi is a surface-exposed lipoprotein that has been shown (by Western blot and Northern blot) to be expressed in the European B. burgdorferi strain B29, but not in the American strain B31. Cell envelope proteins of bacterial pathogens play important roles in the host-parasite interactions that occur during infection, including cell adherence, cell invasion, and immune cell activation or evasion. p27 is a basic protein of 248 amino acids with a typical prokaryotic leader sequence of 17 amino acid residues at the N-terminus of the proposed translation product. The p27 gene is located on a linear plasmid of a size of approximately 55 kb. Borrelia spirochetes are unique among diderm bacteria in their abundance of surface-displayed lipoproteins, some of which play important roles in the pathogenesis of Lyme disease and relapsing fever. There is evidence that Borrelia lipoproteins are specifically targeted to the bacterial surface, but that they can be retained in the periplasm by sequence-specific signals.