Abstract
BBA03 is a Borrelia burgdorferi outer surface lipoprotein encoded on one of the most conserved plasmids in Borrelia genome, linear plasmid 54 (lp54). Although many of its genes have been identified as contributing or essential for spirochete fitness in vivo, the majority of the proteins encoded on this plasmid have no known function and lack homologs in other organisms. In this paper, we report the solution NMR structure of the B. burgdorferi outer surface lipoprotein BBA03, which is known to provide a competitive advantage to the bacteria during the transmission from tick vector to mammalian host. BBA03 shows structural homology to other outer surface lipoproteins reflecting their genetic and evolutionary relatedness. Analysis of the structure reveals a pore in BBA03, which could potentially bind lipids.
Highlights
Lyme disease is the most widespread arthropod-transmitted disease in North America and Europe [1]
Chemical shift assignments for the backbone and the 13 Cβ atoms were obtained through analysis of conventional 3D triple-resonance NMR spectra, while amino acid side chains were assigned using 3D 15 N- and 13 C-resolved nuclear Overhauser enhancement (NOE) spectra
The solution structure of B. burgdorferi outer surface lipoprotein BBA03 was determined revealing a fold with seven α-helices most similar to that of Borrelia turicatae BTA121, which has been shown to bind palmitic acid
Summary
Lyme disease is the most widespread arthropod-transmitted disease in North America and Europe [1]. It is caused by Borrelia burgdorferi sensu lato complex spirochetes, which are transferred to a mammalian host through a bite of an infected tick [2]. Several of its encoded proteins such as OspA that is required for persistence within the tick and DbpA/B decorin binding proteins that are important for dissemination in the mammal have been identified as essential for spirochete survival in vivo [6,7].
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