Enzymatic degradation of H2O2 by Leptospira

Corin, Robert E.; Boggs, E; Cox, Charles D.

doi:10.1128/iai.22.3.672-675.1978

Cited by 17 publications

(6 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Catalase and peroxidase activities were distributed among the Leptospira serovars in a pattern which had been observed previously in semiquantitative assays performed in this laboratory (14). Peroxidase activities fluctuated approximately 30-fold within the genus, with the pathogenic L. interrogans serovars possessing lower amounts than the L. biflexa serovars.…”

Section: Resultssupporting

confidence: 77%

See 1 more Smart Citation

Distribution of superoxide dismutase, catalase, and peroxidase activities among Treponema pallidum and other spirochetes

Austin¹,

Barbieri²,

Corin³

et al. 1981

Infect Immun

Self Cite

View full text Add to dashboard Cite

Representative members of Spirochaetales were surveyed for their content of superoxide dismutase (SOD), catalase, and peroxidase activities. Only Leptospira exhibited peroxidase activity. Obligately anaerobic cultivable Treponema and Spirochaeta possessed no SOD or peroxidative capabilities. Upon polyacrylamide gel electrophoresis, Spirochaeta aurantia, Borrelia hermsi, and five Leptospira biflexa serovars showed SOD activity associated with one electrophoretic band which was inhibited by H202, suggesting that they were iron-containing dismutases. These spirochetes could be distinguished by differences in relative mobilities of their SODs. SOD activity, but not catalase activity, was induced aerobically in S. aurantia. All Leptospira interrogans serovars and two L. biflexa serovars lacked significant SOD activity. These SOD-deficient strains of Leptospira, with one exception, possessed high levels of catalase activity. The Nichols strain of virulent Treponema pallidum possessed SOD and catalase activities, but lacked peroxidase activity. The SOD in T. pallidum exhibited two electrophoretic bands containing copper and zinc, and its relative mobility was identical to that of purified rabbit SOD. Immunization of sheep with purified rabbit SOD resulted in antiserum which inhibited both rabbit SOD and T. pallidum SOD assayed by spectrophotometric analysis or activity staining following polyacrylamide gel electrophoresis. In agarose gel diffusion, precipitin lines of identity were observed between purified rabbit SOD and cell extracts of T. pallidum. These data indicated that the SOD activity detected in T. pallidum was host derived.

show abstract

Section: Resultssupporting

confidence: 77%

“…L. biflexa B-7 and other serovars of L. biflexa possess peroxidase activity. These findings generally support a previous semiquantitative survey of peroxidative activities in Leptospira (14). The presence of catalase or peroxidase activities (or both) may alleviate the need for SOD in these spirochetes.…”

Section: Figsupporting

confidence: 89%

Distribution of superoxide dismutase, catalase, and peroxidase activities among Treponema pallidum and other spirochetes

Austin¹,

Barbieri²,

Corin³

et al. 1981

Infect Immun

Self Cite

View full text Add to dashboard Cite

show abstract

“…Catalase and peroxidase activity and H 2 O 2 detoxification have previously been established in Leptospira. 69,70 In our studies, we have detected 1.151-fold upregulation of a catalase (KatE) in response to growth of L. interrogans in -Fe/FBS media (Table 3). In L. interrogans, the gene encoding this protein resides in a putative two-component operon with a gene encoding the ankyrin-like protein AnkB, a genetic organization that is mirrored in the pathogen Pseudomonas aeruginosa.…”

Section: Flagellar and Chemotaxismentioning

confidence: 61%

Global Proteome Analysis of Leptospira interrogans

et al. 2009

View full text Add to dashboard Cite

Comparative global proteome analyses were performed on Leptospira interrogans serovar Copenhageni grown under conventional in vitro conditions and those mimicking in vivo conditions (iron limitation and serum presence). Proteomic analyses were conducted using iTRAQ and LC-ESI-tandem mass spectrometry complemented with two-dimensional gel electrophoresis and MALDI-TOF mass spectrometry. A total of 563 proteins were identified in this study. Altered expression of 65 proteins, including upregulation of the L. interrogans virulence factor Loa22 and 5 novel proteins with homology to virulence factors found in other pathogens, was observed between the comparative conditions. Immunoblot analyses confirmed upregulation of 5 of the known or putative virulence factors in L. interrogans exposed to the in vivo-like environmental conditions. Further, ELISA analyses using serum from patients with leptospirosis and immunofluorescence studies performed on liver sections derived from L. interrogans-infected hamsters verified expression of all but one of the identified proteins during infection. These studies, which represent the first documented comparative global proteome analysis of Leptospira, demonstrated proteome alterations under conditions that mimic in vivo infection and allowed for the identification of novel putative L. interrogans virulence factors.

show abstract

“…The presence of a single hydroperoxidase in L. pneumophila was supported by the fact that when cells were Baltimore (1), Burlington (1), Detroit 1 (1). 16 0.00-0.10 (0.019 ± 0.035) Flint 1 (1), Gastonia (1), Knoxville 1 (1), Memphis (1), New York 1 (1), Rochester (1), Philadelphia 2 (1), LA 1 (4), Dallas 4 (5), Cambridge 2 (5), Chicago 8 (7), IN23 (9) Buffalo (1), Berkeley (1), Miami Beach (1), Philadelphia 1 (1), 11 0.14-0.27 (0.224 ± 0.049) Bellingham (1), Togus (2), Bloomington (3), Dallas 17 (5), Chicago 2 (6), Houston 2 (6), Concord a Catalase and peroxidase activities are expressed in international units (35); for SOD, 1 unit is that amount of enzyme (milligrams) giving 50% inhibition of the spontaneous oxidation of pyrogallol under test conditions (24). grown on BCYE, harvested at different times, and analyzed for their catalase and peroxidase, quantitative changes in enzyme activities were identical.…”

Section: Resultsmentioning

confidence: 99%

Determination of catalase, peroxidase, and superoxide dismutase within the genus Legionella

Pine¹,

Hoffman²,

Malcolm³

et al. 1984

J Clin Microbiol

View full text Add to dashboard Cite

We examined 40 strains of Legionella for reduced-oxygen scavenging enzymes. Using a simple reaction chamber with a Swinney filter for the Beers and Sizer assay, we determined the catalase activity of live cells grown on buffered charcoal-yeast extract agar. For 29 strains of Legionella pneumophila, the apparent firstorder rate constants for catalase ranged from 0.000 to 0.005. Similarly, low values ranging from 0.001 to 0.005 were observed for Legionella wadsworthii, Legionella oakridgensis, and Legionella gormanii. High catalase activities were found for Legionella jordanis, Legionella longbeachae, Legionella micdadei, and Legionella bozemanii, with first-order rate constant values of 0.010 to 0.035. Cell-free extracts were analyzed for catalase, peroxidase, and superoxide dismutase. Cell-free extracts of all strains had superoxide dismutase levels ranging from 8.2 to 30.5 U per mg of protein. The species could be characterized by their catalase and peroxidase since L. pneumophila and L. gormanii had only peroxidase (relative molecular weight [Mn, 150,000); L. dumoffii had a peroxidase (Mr, 150,000) plus a catalase (Mr, 174,000); and all remaining species had catalase only (Mn,

show abstract

Enzymatic degradation of H2O2 by Leptospira

Cited by 17 publications

References 17 publications

Distribution of superoxide dismutase, catalase, and peroxidase activities among Treponema pallidum and other spirochetes

Distribution of superoxide dismutase, catalase, and peroxidase activities among Treponema pallidum and other spirochetes

Global Proteome Analysis of Leptospira interrogans

Determination of catalase, peroxidase, and superoxide dismutase within the genus Legionella

Contact Info

Product

Resources

About