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PubMed2003

Actinomyces infection in a dog with pulmonary carcinoma.

Thoracic actinomycosis was diagnosed by bacterial isolation in a dog with a history of chronic productive cough, weight loss, pyrexia and a pulmonary mass lesion on radiography. Therapy with amoxycillin and clindamycin did not significantly improve the patient's condition and euthanasia was performed during exploratory thoracotomy. Histological examination of the affected lung lobes revealed the presence of peribronchiolar adenocarcinoma. Actinomycosis has been reported to co-exist with pulmonary neoplasia in humans and may mask the presence of malignancy.

Actinomyces↗
PubMed1975

Interrelation between guanosine tetraphosphate accumulation, ribonucleic acid synthesis, and streptomycin lethality in Escherichia coli CP78.

The effects of streptomycin on the synthesis of ribonucleic acid (RNA) and guanosine-3'-diphosphate-5'-diphosphate have been examined in the isogenic strains CP78 (rel(+)) and CP79 (rel-). In the absence of the required amino acids arginine, leucine, or threonine, streptomycin stimulates RNA synthesis in CP78 and this stimulation coincides with cell death. However, in the absence of histidine, also a required amino acid, streptomycin kills the cells without stimulation of RNA synthesis above that which occurs in the absence of streptomycin. In all of these instances, guanosine-3'-diphosphate-5'-diphosphate levels vary inversely with RNA synthesis, decreasing when a stimulation of RNA synthesis occurs. Streptomycin has little effect on guanosine-3'-diphosphate-5'-diphosphate levels in CP78 in the absence of histidine. Another histidine auxotroph, 15 T(-)H(-)U(-) (rel(+)), does show streptomycin-stimulated synthesis of RNA which is coincident with cell death. CP79 (rel(-)) is 10 times more susceptible to streptomycin than CP78 and streptomycin causes an inhibition of the relaxed synthesis of RNA. The greater susceptibility of CP79 may be due to a greater initial uptake of streptomycin by CP79.

Escherichia coli↗
PubMed1980

Carbon dioxide metabolism by Actinomyces viscosus: pathways for succinate and aspartate production.

14C-labeled bicarbonate was incorporated into trichloroacetic acid-insoluble material by cell suspensions of A. viscosus strain M100 and also into the four-carbon fermentation product, succinate, but not into the three-carbon fermentation product, lactate. The initial step in the conversion of 14C-labeled bicarbonate into both trichloroacetic acid-insoluble material and succinate was catalyzed by the enzyme phosphoenolypyruvate carboxylase, which served to convert the glycolytic intermediate, phosphoenolpyruvate, and bicarbonate to the four-carbon compound, oxalacetate. The metabolic fate of oxalacetate was its conversion to either trichloroacetic acid-insoluble material or succinate. One pathway by which oxalacetate may be metabolized into acid-insoluble material is via its conversion to the biosynthetic precursor aspartate by the action of glutamate aspartate aminotransferase. One source of the alpha-amino group of aspartate was the ammonium ion, which could be incorporated into glutamate, the substrate of the glutamate aspartate aminotransferase reaction, by the action of a reduced nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenase whose reducing equivalents could be derived from the nicotinamide adenine dinucleotide phosphate-dependent oxidative reactions of the hexose monophosphate pathway catalyzed by glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. Alternatively, oxalacetate was converted to the fermentation product, succinate, through the sequential action of malate dehydrogenase, fumarase, and succinic dehydrogenase. The resolution and partial purification of phosphoenolpyruvate carboxylase, glutamate aspartate aminotransferase, glutamate dehydrogenase, malate dehydrogenase, fumarase, and succinic dehydrogenase are also reported.

Actinomyces↗
PubMed1984

Specific inhibition of adsorption of Actinomyces viscosus T14V to saliva-treated hydroxyapatite by antibody against type 1 fimbriae.

Specific antibodies and their Fab fragments were used to study adsorption of Antinomyces viscosus T14V to saliva-treated hydroxyapatite. Antibody against A. viscosus T14V blocked adsorption of the strain to saliva-treated hydroxyapatite, and this activity was removed after preincubation of the immune immunoglobulin G (IgG) with purified type 1 fimbriae in amounts near equivalence but not after preincubation with type 2 fimbriae in antigen excess. Specific IgG or Fab fragments against type 1 fimbriae inhibited adsorption of strain T14V to saliva-treated hydroxyapatite and promoted desorption of cells already attached to the apatite surface. Anti-type 2 IgG or Fab fragments did not possess these activities. These data demonstrate that type 1 but not type 2 fimbriae mediate adsorption of strain T14V to the saliva-treated hydroxyapatite surface.

Actinomyces↗