Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
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Target Concepts:
Gene/Protein
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Query: UMLS:C0348321 (
Haemophilus
)
15,372
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
We examined the killing of Actinobacillus actinomycetemcomitans and
Haemophilus
aphrophilus by oxygen metabolites generated by the xanthine-xanthine oxidase (X-XO) system. This system generates a mixture of oxidants, including
superoxide radical
, hydrogen peroxide, hydroxyl radical, and possibly singlet oxygen. Differential sensitivity to the X-XO system was observed among strains of A. actinomycetemcomitans; notably, 2 catalase-deficient strains and 2 strains representative of serotypes b and c were the most susceptible. H. aphrophilus was not sensitive. The amount of oxidants produced by the X-XO system more closely correlated with killing than the ratio of oxidant production. Cytochrome c, superoxide dismutase, catalase, dimethyl sulfoxide, and desferrioxamine were used to determine the role of
superoxide radical
, hydrogen peroxide and hydroxyl radical in the bactericidal process. Hydrogen peroxide was the major bactericidal agent against A. actinomycetemcomitans.
Superoxide anion
participated in killing of A. actinomycetemcomitans to varying but lesser degrees. The intracellular generation of hydroxyl radical was implicated in the killing of several strains. We conclude that (i) strains of A. actinomycetemcomitans are differentially sensitive to the bactericidal effects of the X-XO system and (ii) of the oxidants produced by the X-XO system, hydrogen peroxide is the most bactericidal against A. actinomycetemcomitans.
...
PMID:Sensitivity of Actinobacillus actinomycetemcomitans and Haemophilus aphrophilus to oxidative killing. 166 50
Copper- and zinc-containing superoxide dismutases ([Cu,Zn]-SODs) are generally considered almost exclusively eukaryotic enzymes, protecting the cytosol and extracellular compartments of higher organisms from damage by oxygen free-radicals. The recent description of a few examples of bacterial forms of the enzyme, located in the periplasm of different Gram-negative micro-organisms, prompted a re-evaluation of this general perception. A PCR-based approach has been developed and used successfully to identify bacterial genes encoding [Cu,Zn]-SOD in a wide range of important human and animal pathogens-members of the
Haemophilus
, Actinobacillus and Pasteurella (HAP) group, and Neisseria meningitidis. Comparison of [Cu,Zn]-SOD peptide sequences found in Haemophilus ducreyi, Actinobacillus pleuropneumoniae, Actinobacillus actinomycetemcomitans, Pasteurella multocida, and N. meningitidis with previously described bacterial proteins and examples of eukaryotic [Cu,Zn]-SOD has shown that the bacterial proteins constitute a distinct family apparently widely separated in evolutionary terms from the eukaryotic examples. The widespread occurrence of [Cu,Zn]-SOD in the periplasm of bacterial pathogens, appropriately located to dismute exogenously derived
superoxide radical
anions, suggests that this enzyme may play a role in the interactive biology of organisms with their hosts and so contribute to their capacity to cause disease.
...
PMID:Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinct from the eukaryotic enzyme, and not so rare after all! 749 39