Lyme Disease—a Tick-Borne Spirochetosis?

Burgdorfer, Willy; Barbour, Alan G.; Hayes, Stanley F.; Benach, Jorge L.; Grunwaldt, Edgar; Davis, Jeffrey P.

doi:10.1126/science.7043737

Cited by 2,594 publications

(1,387 citation statements)

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“…The spirochete Borrelia burgdorferi is the causative agent of Lyme disease (Burgdorfer et al, 1982). Lyme disease is a multi-systemic disorder which, if not treated early, can develop into chronic infection (Steere, 1989).…”

Section: Introductionmentioning

confidence: 99%

Cloning and analysis of a Borrelia burgdorferi membrane‐interactive protein exhibiting haemolytic activity

Guina

Oliver

1997

Molecular Microbiology

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SummaryWe cloned the gene encoding a membrane-interactive protein of Borrelia burgdorferi by means of its haemolytic activity in Escherichia coli. The haemolytic activity was erythrocyte-species specific, with progressively decreasing activity for erythrocytes from horse, sheep, and rabbit, respectively. Genetic analysis of the haemolytic determinant revealed two borrelia haemolysin genes, blyA and blyB, that are part of a predicted four-gene operon which is present in multiple copies on the 30 kb circular plasmid(s) of B. burgdorferi B31. blyA encodes a predicted ␣-helical 7.4 kDa protein with a hydrophobic central region and a positively charged C-terminus, which is structurally homologous to a large group of pore-forming toxins with cytolytic activity. blyB encodes a soluble protein which stabilized BlyA and enhanced haemolytic activity. While the majority of BlyA in E. coli was membrane-associated, only soluble protein was haemolytically active. The haemolytic activity was shown to be highly protease sensitive, heat labile, independent of divalent cations, and extremely dependent on protein concentration, consistent with a requirement for oligomerization as the mechanism of action. BlyA was highly purified from E. coli in a single step utilizing Triton X-114 phase partitioning. Genetic analysis of blyA and blyB mutants indicated that the stability, membrane association, and activity of BlyA was dependent on subtle changes in its sequence and on the BlyB protein. The bly genes were found to be expressed at a very low level in cultured B. burgdorferi.

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Section: Introductionmentioning

confidence: 99%

Cloning and analysis of a Borrelia burgdorferi membrane‐interactive protein exhibiting haemolytic activity

Guina

Oliver

1997

Molecular Microbiology

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“…The exogenous lipoprotein most studied in the brain is the bacterial outer surface protein A (ospA), which is produced by B. burgdorferi [12,13]. B. burgdorferi causes Lyme disease, which is the most common tick-borne infection in Europe and in North America [14].…”

Section: Introductionmentioning

confidence: 99%

Lipoproteins and Diseases of the Brain

Kim¹,

Palmore²

2017

Advances in Lipoprotein Research

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Apolipoprotein E4 (apoE4) and outer surface protein A (ospA) are pathogenic lipoproteins involved in the progression of Alzheimer's disease and Lyme neuroborreliosis, respectively. Results from previous studies indicate that apoE4 exhibits neurotoxicity by activating amyloid beta pathways, and ospA causes damage to the brain by stimulating immune activity of microglia and astrocytes. These results, however, lack information about the specific interactions that develop between neurons and these two lipoproteins. It is essential to investigate the effect of these lipoproteins on neuronal morphology and function to better understand the mechanism of damage and disease of the brain. This chapter summarizes previous studies on the role of apoE4 and ospA in diseases of the brain and discusses experimental results from our own work that suggests new roles for apoE4 and ospA in neuronal outgrowth and synaptic loss.

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“…suggested that the epidemiology of Lyme disease indicated transmission by an arthropod vector due to the geographic clustering of patients in rural areas and the seasonal occurrence of the symptoms [7]. Subsequently, Dr. Willy Burgdorfer and coworkers observed spirochetes in the midgut tissues from ticks collected in a Lyme disease endemic area [1]. These spirochetes produced a skin rash resembling erythema migrans when injected into rabbits, and sera from Lyme disease patients reacted with the bacteria in indirect immunofluorescence assays.…”

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Biology of Infection with Borrelia burgdorferi

Tilly

Rosa

Stewart

2008

Infectious Disease Clinics of North America

183

177

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The spirochete Borrelia burgdorferi is a tick-borne obligate parasite whose normal reservoir is a variety of small mammals [1]. Whereas infection of these natural hosts does not lead to disease, infection of humans can result in Lyme disease, as a consequence of the human immunopathological response to B. burgdorferi [2,3]. Consistent with the pathogenesis of Lyme disease, bacterial products that allow B. burgdorferi to replicate and survive, rather than true "virulence factors," appear to be primarily what is required for the bacterium to cause disease in a susceptible host. In support of this idea, the genome sequence of B31, the type strain of B. burgdorferi sensu stricto [4,5], revealed that the bacterium lacks factors common to many bacterial pathogens, such as lipopolysaccharide, toxins, and specialized secretion systems. In this chapter, we will describe the basic biology of B. burgdorferi, and some of the bacterial components required to infect and survive in the mammalian and tick hosts.

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Lyme Disease—a Tick-Borne Spirochetosis?

Cited by 2,594 publications

References 13 publications

Cloning and analysis of a Borrelia burgdorferi membrane‐interactive protein exhibiting haemolytic activity

Cloning and analysis of a Borrelia burgdorferi membrane‐interactive protein exhibiting haemolytic activity

Lipoproteins and Diseases of the Brain

Biology of Infection with Borrelia burgdorferi

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