Action of penicillin on Borrelia hermsii

Barbour, Alan G.; Todd, William J.; Stoenner, Herbert G.

doi:10.1128/aac.21.5.823

Cited by 40 publications

(27 citation statements)

References 30 publications

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“…B. hermsii outer membrane vesicles (OMV) were generated by the method previously described for the isolation of the B. burgdorferi OMV (15,50,53). Briefly, 10 11 B. hermsii cells were washed twice in PBS supplemented with 0.1% bovine serum albumin (BSA) and centrifuged at 6,000 ϫ g for 20 min. The pelleted cells were resuspended in 90 ml of ice-cold 25 mM citrate buffer (pH 3.2) containing 0.1% BSA.…”

Section: Methodsmentioning

confidence: 99%

“…Chromosomal DNA was isolated from approximately 10 11 B. hermsii serotype 7 passage 10 organisms (14), and linear plasmid and supercoiled plasmid DNAs were isolated from CsCl preparations as previously described (19). B. hermsii genomic, linear, and circular plasmid DNA libraries were constructed by using the lambda EXlox vector (Novagen) as follows.…”

Section: Methodsmentioning

confidence: 99%

“…Although visualized by freeze fracture electron microscopy, these transmembrane outer membrane proteins have not been identified in B. hermsii. Indeed, relatively few subsurface and surface proteins have been identified in B. hermsii (2,10,32,39,48). Since outer membrane proteins have been shown to serve as protective immunogens, we have attempted to identify and characterize these proteins from B. hermsii in order to relate ultrastructure to mechanisms of virulence, physiology, and immunity.…”

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confidence: 99%

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Sequence analysis and characterization of a 40-kilodalton Borrelia hermsii glycerophosphodiester phosphodiesterase homolog

Shang¹,

Skare²,

Erdjument‐Bromage³

et al. 1997

J Bacteriol

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We report the purification, molecular cloning, and characterization of a 40-kDa glycerophosphodiester phosphodiesterase homolog from Borrelia hermsii. The 40-kDa protein was solubilized from whole organisms with 0.1% Triton X-100, phase partitioned into the Triton X-114 detergent phase, and purified by fastperformance liquid chromatography (FPLC). The gene encoding the 40-kDa protein was cloned from a B. hermsii chromosomal DNA lambda EXlox expression library and identified by using affinity antibodies generated against the purified native protein. The deduced amino acid sequence included a 20-amino-acid signal peptide encoding a putative leader peptidase II cleavage site, indicating that the 40-kDa protein was a lipoprotein. Based on significant homology (31 to 52% identity) of the 40-kDa protein to glycerophosphodiester phosphodiesterases of Escherichia coli (GlpQ), Bacillus subtilis (GlpQ), and Haemophilus influenzae (Hpd; protein D), we have designated this B. hermsii 40-kDa lipoprotein a glycerophosphodiester phosphodiesterase (Gpd) homolog, the first B. hermsii lipoprotein to have a putative functional assignment. A nonlipidated form of the Gpd homolog was overproduced as a fusion protein in E. coli BL21(DE3)(pLysE) and was used to immunize rabbits to generate specific antiserum. Immunoblot analysis with anti-Gpd serum recognized recombinant H. influenzae protein D, and conversely, antiserum to H. influenzae protein D recognized recombinant B. hermsii Gpd (rGpd), indicating antigenic conservation between these proteins. Antiserum to rGpd also identified native Gpd as a constituent of purified outer membrane vesicles prepared from B. hermsii. Screening of other pathogenic spirochetes with anti-rGpd serum revealed the presence of antigenically related proteins in Borrelia burgdorferi, Treponema pallidum, and Leptospira kirschneri. Further sequence analysis both upstream and downstream of the Gpd homolog showed additional homologs of glycerol metabolism, including a glycerol-3-phosphate transporter (GlpT), a glycerol-3-phosphate dehydrogenase (GlpD), and a thioredoxin reductase (TrxB).The pathogenic spirochete Borrelia hermsii is one of the etiologic agents of tick-borne relapsing fever. Infection in humans and other vertebrates is commonly characterized by recurring episodes of high fever and bacteremia with intermittent afebrile periods (55). In humans, other clinical manifestations may include pronounced muscle and joint pains, splenomegaly, hepatomegaly, jaundice, and rash, as well as respiratory, cardiovascular, and central nervous system involvement (7). The well-documented relapse phenomenon is associated with the ability of these organisms to undergo multiphasic antigenic variation during the course of disease (56). A major surfaceexposed lipoprotein designated the variable membrane protein (Vmp) has been correlated with this antigenic variation (4, 9, 11). This switching from an initial Vmp type to another prior to the establishment of a protective antibody response is thought to enable the escape of...

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Sequence analysis and characterization of a 40-kilodalton Borrelia hermsii glycerophosphodiester phosphodiesterase homolog

Shang¹,

Skare²,

Erdjument‐Bromage³

et al. 1997

J Bacteriol

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“…Release of pro-inflammatory bacterial products occurs from spirochetes both spontaneously 6 and upon immune or antibiotic mediated lysis. [7][8][9] Furthermore, release of outer membrane lipoproteins from spirochetes into the extracellular environment can occur independently of blebs. 6 However, little is known about whether bacterial products can be released in vivo and disseminate into tissues like the brain to cause inflammation.…”

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confidence: 99%

Bacterial Lipoproteins Can Disseminate from the Periphery to Inflame the Brain

Londoño

Cadavid

2010

The American Journal of Pathology

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The current view is that bacteria need to enter the brain to cause inflammation. However, in mice infected with the spirochete Borrelia turicatae, we observed widespread cerebral inflammation despite a paucity of spirochetes in the brain parenchyma at times of high bacteremia. Here we studied the possibility that bacterial lipoproteins may be capable of disseminating from the periphery across the bloodbrain barrier to inflame the brain. For this we injected normal and infected mice intraperitoneally with lanthanide-labeled variable outer membrane lipoproteins of B. turicatae and measured their localization in blood, various peripheral organs, and whole and capillary-depleted brain protein extracts at various times. Lanthanide-labeled nonlipidated lipoproteins of B. turicatae and mouse albumin were used as controls. Brain inflammation was measured by TaqMan RT-PCR amplification of genes known to be upregulated in response to borrelial infection. The results showed that the two lipoproteins we studied , LVsp1 and LVsp2 , were capable of inflaming the brain after intraperitoneal injection to different degrees: LVsp1 was better than LVsp2 and Bt1 spirochetes at moving from blood to brain. The dissemination of LVsp1 from the periphery to the brain occurred under normal conditions and significantly increased with infection. In contrast, LVsp2 disseminated better to peripheral organs. We conclude that some bacterial lipoproteins can disseminate from the periphery to inflame the brain. The traditional belief is that bacteria need to cross the blood brain barrier (BBB) to cause brain inflammation. However, during studies in mice persistently infected with the relapsing fever spirochete Borrelia turicatae, we noticed widespread cerebral microgliosis that could not be explained by the presence of spirochetes in the brain parenchyma.

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“…Similar forms can be produced by placing spirochetes in hypotonic solutions (Umemoto and Manikawa 1980) and by exposure to antibiotics (Furudawa 1975;Barbour et al 1982).…”

Section: Discussionmentioning

confidence: 99%

Determinants of Infectivity of Pathogens in Vector Ticks

Spielman¹

1990

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Action of penicillin on Borrelia hermsii

Cited by 40 publications

References 30 publications

Sequence analysis and characterization of a 40-kilodalton Borrelia hermsii glycerophosphodiester phosphodiesterase homolog

Sequence analysis and characterization of a 40-kilodalton Borrelia hermsii glycerophosphodiester phosphodiesterase homolog

Bacterial Lipoproteins Can Disseminate from the Periphery to Inflame the Brain

Determinants of Infectivity of Pathogens in Vector Ticks

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