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

Abstract

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,

Characteristics and Pathogenicity of Non‐Melibiose‐Fermenting Strains of Yersinia pseudotuberculosis O3

“…In this investigation, SOD activity in the MF and NMF strains was much lower than that in other intracellular parasites (1,2,14,17,25,39,46,54). However, catalase activity in the MF strains was approximately the same as that in other intracellular parasites (1,2,14,17,25,39,46,54) though the activity in NMF was clearly low. Since low SOD and catalase activity should reduce the resistance of microorganisms (3,18), we think that the low activity of catalase production in NMF strains attributes to their low pathogenicity.…”

“…We also suggest that resistance to phagocytosis and catalase production activity are important for determining the pathogenicity of Y. pseudotuberculosis for the following reason. Resistance to phagocytosis is an important factor in the pathogenicity of Yersinia organisms; the existence of this factor stimulates infectivity and this brings about an infectious disease called yersiniosis (38)(39)(40)(41)53). It has been shown that the resistance of Yersinia organisms to phagocytosis depends on outer-membrane proteins encoded by virulence plasmids (6,7,10,36,47).…”

“…In Y pseudotuberculosis, resistance against phagocytosis is closely related to the existence of virulence plasmid (6,7,10,35,47,53). Furthermore, it is reported that intracellular parasites including Y pseudotuberculosis are highly active in the production of catalase and superoxide dismutase (SOD) (1,2,14,17,25,39,46,54). However, there are no reports on the role of catalase and SOD activities of Yersinia organisms in the resistance against phagocytosis.…”

Salicylic acid and ascorbic acid retrieve activity of antioxidative enzymes and structure of Caralluma tuberculata calli on PEG stress

“…To determine catalase (CAT; EC 1.11.1.6) activity, 25.0 mM buffer of potassium phosphate containing 0.1 mM EDTA (pH 7.0) is mixed with 10.0 mM H 2 O 2 and enzyme extract (Pine et al 1984). Within one min of enzyme extract mixing, the reduction in the absorbance of H 2 O 2 (E = 39.4 mM −1 cm −1 ) is recorded at 240 nm on spectrophotometer.…”

Identification of a novel periplasmic catalase-peroxidase KatA of Legionella pneumophila

“…In contrast, catalase-peroxidases are identi¢ed from only bacteria except for a few species of fungi. L. pneumophila exhibits catalase-peroxidase activities but not true catalase activities [3,4]. Recently, Bandyopadhyay and Steinman showed that L. pneumophila possessed two catalase-peroxidase genes, katA and katB, and they cloned only the katB [5].…”