ArticleMicrobiology (Reading, England)2012
The role of catalase in gonococcal resistance to peroxynitrite.
Article in Microbiology (Reading, England), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed, 6 citations in OpenAlex.
- Bacterium of one thousand and one variants: genetic diversity ofMicrobial genomics · 2023Review
- How the Knowledge of Interactions between Meningococcus and the Human Immune System Has Been Used to Prepare Effective Neisseria meningitidis Vaccines.Journal of immunology research · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We have reported that Neisseria gonorrhoeae is extremely resistant to reactive nitrogen species (RNS) including peroxynitrite (PN). Recent literature suggests that catalase can provide protection against commercial preparations of PN. Though wild-type gonococci were shown to be highly resistant to 2 mM PN, Neisseria meningitidis and a gonococcal katA mutant were both shown to be extremely sensitive to 2 mM PN. Analysis of translational fusions to lacZ of the catalase promoters from N. gonorrhoeae and N. meningitidis demonstrated that basal katA expression from gonococci is 80-fold higher than in meningococci, though meningococcal katA retains a greater capacity to be activated by OxyR. This activation capacity was shown to be due to a single base pair difference in the -10 transcription element between the two kat promoters. PN resistance was initially shown to be associated with increasing catalase expression; however, commercial preparations of PN were later revealed to contain higher levels of contaminating hydrogen peroxide (H2O2) than expected. Removal of H2O2 from PN preparations with manganese dioxide markedly reduced PN toxicity in a gonococcal katA mutant. Simultaneous treatment with non-lethal concentrations of PN and H2O2 was highly lethal, indicating that these agents act synergistically. When treatment was separated by 5 min, high levels of bacterial killing occurred only when PN was added first. Our results suggest that killing of N. gonorrhoeae ΔkatA by commercial PN preparations is likely due to H2O2, that H2O2 is more toxic in the presence of PN, and that PN, on its own, may not be as toxic as previously believed.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.