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Abstract
Lyme disease Borreliae are highly dependent on the uptake of nutrients provided by their hosts. Our study describes the identification of a 36 kDa protein that functions as putative dicarboxylate-specific porin in the outer membrane of Lyme disease Borrelia. The protein was purified by hydroxyapatite chromatography from Borrelia burgdorferi B31 and designated as DipA, for dicarboxylate-specific porin A. DipA was partially sequenced, and corresponding genes were identified in the genomes of B. burgdorferi B31, Borrelia garinii PBi and Borrelia afzelii PKo. DipA exhibits high homology to the Oms38 porins of relapsing fever Borreliae. B. burgdorferi DipA was characterized using the black lipid bilayer assay. The protein has a single-channel conductance of 50 pS in 1 M KCl, is slightly selective for anions with a permeability ratio for cations over anions of 0.57 in KCl and is not voltage-dependent. The channel could be partly blocked by different di- and tricarboxylic anions. Particular high stability constants up to about 28,000 l/mol (in 0.1 M KCl) were obtained among the 11 tested anions for oxaloacetate, 2-oxoglutarate and citrate. The results imply that DipA forms a porin specific for dicarboxylates which may play an important role for the uptake of specific nutrients in different Borrelia species.
Highlights
Lyme disease is a systemic disorder manifested in a wide spectrum of different symptoms such as a circular skin rash around a tick bite and arthritis up to paralysis appearances and other neurological effects [1,2]
The outer membrane fraction (OMF) of B. burgdorferi B31 Dp66 contains a variety of proteins as shown by SDS-PAGE
The results demonstrated that polyclonal anti-DipA serum clearly detected DipA in the total protein fractions (TP) of the Lyme disease species B. burgdorferi, B. afzelii and B. garinii
Summary
Lyme disease is a systemic disorder manifested in a wide spectrum of different symptoms such as a circular skin rash around a tick bite and arthritis up to paralysis appearances and other neurological effects [1,2]. It is caused by infection with Borrelia spirochetes [3,4]. To ensure the survival in this enzootic life cycle, the spirochetes must adapt to a range of diverse host environments and nutrient availability [8,9,10,11,12,13] These parasites need to have an efficient control of the nutrient uptake system across the cell envelope
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