Disease relevance of BB0363

• Borrelia burgdorferi is a motile spirochete with multiple internal periplasmic flagella (PFs) attached near each end of the cell cylinder; these PFs overlap in the cell center [1].
• Borrelia burgdorferi periplasmic flagella have both skeletal and motility functions [2].
• The Lyme disease spirochete Borrelia burgdorferi has bundles of periplasmic flagella subpolarly located at each cell end [3].
• This periplasmic enzyme may prevent the accumulation of proteins damaged by the innate immune response and contribute to the ability of the relapsing fever spirochaetes to achieve high cell densities in blood [4].
• We recently characterized the three-dimensional shape of Treponema phagedenis periplasmic flagella (PFs) [5].

High impact information on BB0363

• Our results indicate that the periplasmic flagella of B. burgdorferi have a skeletal function [2].
• Using targeted mutagenesis, we inactivated the gene encoding the major periplasmic flagellar filament protein FlaB [2].
• Wild-type cells poisoned with the protonophore carbonyl cyanide-m-chlorophenylhydrazone retained their flat-wave morphology, indicating that the periplasmic flagella do not need to be energized for the cell to maintain this shape [2].
• Protease treatment of intact spirochetes cleaved P66 and Osp proteins but not the periplasmic flagellin or the BmpA protein of the cytoplasmic membrane [6].
• Fourteen chromosomal genes involved in energy metabolism, substrate transport, and signal transduction and 10 (4 chromosomal and 6 plasmid) genes encoding putative lipoproteins and periplasmic proteins were preferentially expressed in engorging ticks [7].

Chemical compound and disease context of BB0363

• Uptake of B. burgdorferi by BMM phi, which mainly occurs by coiling phagocytosis, generation of NO and O2- radicals as well as killing of spirochetes were significantly enhanced by pre-opsonization of spirochetes with monoclonal antibodies (mAb) to the outer surface proteins A and B but not with those to the periplasmic flagellin [8].

Associations of BB0363 with chemical compounds

• Wheat germ agglutinin bound weakly to the surface of borreliae; however, alterations of the outer membrane by preincubation in 100 ppm Triton X-100 or boiling uncovered numerous periplasmic sites recognized by the lectin [9].
• No surface-exposed or periplasmic epitopes for the lectins from Glycine max, Dolichos biflorus or Helix pomatia were detected [9].

Analytical, diagnostic and therapeutic context of BB0363

• Western blot analysis indicated that FlaB was no longer synthesized, and electron microscopy revealed that the mutants were completely deficient in periplasmic flagella [2].

References