Book

Lyme Disease Book 2012

Publisher: Intech, Editor: Ali Karami and others

ABSTRACT Lyme disease, or Lyme borreliosis, is an emerging infectious disease caused by bacteria belonging to the genus borrelia. Borrelia burgdorferi, in the strict sense. This book deals mostly with the molecular biology of the Lyme disease agent orrelia burgdorferi. It has been written by experts in the relevant field and is tailored to the need of researchers, advanced students of biology, molecular biology, molecular genetics of microorganism. It will also be of use to infectious disease experts and people in other disciplines needing to know more about Lyme borreliosis. The book contains chapters on the molecular biology of the Lyme disease agent, zoonotic peculiarities of Bb, advancement in Bb antibody testing, the serology diagnostic schemes in Bb, discovering Lyme disease in ticks and dogs, adaptation to glucosamine starvation in Bb, and porins in the genus borrelia.

0 Bookmarks
 · 
207 Views
  • Source
    Microbiological reviews 01/1987; 50(4):381-400.
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: We were unable to demonstrate the presence of the classic enterobacterium-type lipopolysaccharide in the cells of the Lyme disease spirochete, Borrelia burgdorferi B31. This finding was primarily based on chemical analysis and the absence of free lipid A upon mild acid hydrolysis of the appropriate cell extracts. These results do not preclude the possible existence of an unusual lipopolysaccharide-like compound(s) in B. burgdorferi.
    Infection and Immunity 10/1987; 55(9):2311-3. · 4.07 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: A fundamental ultrastructural feature shared by the spirochetal pathogens Treponema pallidum subsp. pallidum (T. pallidum) and Borrelia burgdorferi, the etiological agents of venereal syphilis and Lyme disease, respectively, is that their most abundant membrane proteins contain covalently attached fatty acids. In this study, we identified the fatty acids covalently bound to lipoproteins of B. burgdorferi and T. pallidum and examined potential acyl donors to these molecules. Palmitate was the predominant fatty acid of both B. burgdorferi and T. pallidum lipoproteins. T. pallidum lipoproteins also contained substantial amounts of stearate, a fatty acid not typically prevalent in prokaryotic lipoproteins. In both spirochetes, the fatty acids of cellular lipids differed from those of their respective lipoproteins. To characterize phospholipids in these organisms, spirochetes were metabolically labeled with [3H]palmitate or [3H]oleate; B. burgdorferi contained only phosphatidylglycerol and phosphatidylcholine, while T. pallidum contained phosphatidylglycerol, phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, phosphatidylinositol, and cardiolipin. Although palmitate predominated in the lipoproteins, there were no apparent differences in the incorporation of these two fatty acids into phospholipids (putative acyl donors). Phospholipase A1 and A2 digestion of phosphatidylcholine from B. burgdorferi and T. pallidum labeled with either [3H]palmitate or [3H]oleate also revealed that neither fatty acid was incorporated preferentially into the 1 and 2 positions (potential acyl donor sites) of the glycerol backbone. The combined findings suggest that fatty acid utilization during lipoprotein synthesis is determined largely by the fatty acid specificities of the lipoprotein acyl transferases. These findings also provide the basis for ongoing efforts to elucidate the relationship between lipoprotein acylation and the physiological functions and inflammatory activities of these molecules.
    Journal of Bacteriology 05/1994; 176(8):2151-7. · 3.19 Impact Factor

Full-text

View
725 Downloads
Available from
May 21, 2014