Catalase, Superoxide Dismutase and Listeriolysin O Production by Listeria monocytogenes in Broth Containing Acetic and Hydrochloric Acids

1994 ◽  
Vol 57 (7) ◽  
pp. 626-628 ◽  
Author(s):  
LISA K. DIMMIG ◽  
ERIC R. MYERS ◽  
SCOTT E. MARTIN
Keyword(s):  
Superoxide Dismutase ◽  
Listeria Monocytogenes ◽  
Hydrochloric Acid ◽  
Enzyme Production ◽  
Growth Media ◽  
Listeriolysin O ◽  
Weak Acids ◽  
Sod Activity ◽  
Strong Acids

Cells of Listeria monocytogenes 10403S were propagated at 37°C in media acidified with either acetic or hydrochloric acid to determine the effect on the production of catalase (CA), superoxide dismutase (SOD) and listeriolysin O (LLO). The CA and LLO activities decreased while SOD activity increased as the pH of the growth media was decreased. Comparison of the acids indicated that neither acid caused significant differences in enzyme production except for SOD activity at pH 5.7. These results suggest that growth of L. monocytogenes in acid environments may influence the production of these enzymes, while growth in strong acids versus weak acids may not be significantly different.

Virulence of Listeria monocytogenes Propagated in NaCl Containing Media at 4, 25 and 37°C

1994 ◽  
Vol 57 (6) ◽  
pp. 475-478 ◽  
Author(s):  
ERIC R. MYERS ◽  
SCOTT E. MARTIN
Keyword(s):  
Superoxide Dismutase ◽  
Listeria Monocytogenes ◽  
Sodium Chloride ◽  
Mouse Model ◽  
Virulence Factor ◽  
Growth Temperature ◽  
Lethal Dose ◽  
Listeriolysin O ◽  
Sod Activity ◽  
Approximate Lethal Dose

Virulence, as determined in a mouse model, and virulence factor activities of catalase (CA), superoxide dismutase (SOD) and listeriolysin O (LLO), was examined in Listeria monocytogenes 10403S. Cells were propagated in media containing various concentrations of sodium chloride (NaCl) at 4, 25 and 37°C. Strain 10403S exhibited significant increases in CA activity and LLO when grown in media containing 428 mM of NaCl at 37°C. The CA activities at 4 and 25°C were significantly less, and the cells exhibited similar increases and decreases as cells grown at 37°C. When comparing the growth temperatures, the CA activity decreased as the growth temperature decreased. The SOD activity was significantly increased only when cells were propagated in media containing either 428 or 1,112 mM of NaCl. The SOD activity increased as the growth temperature decreased. No LLO activity was detected when cells were grown at 4 and 25°C. The production of these enzymes appeared to be thermoregulated. In addition, approximate lethal dose (ALD50) values were determined after intragastric (i.g.) and intraperitoneal (i.p.) infection. Each method of infection indicated that LLO was required for virulence, while growth in salt containing media, growth at 4°C, or the production of higher levels of CA, SOD and LLO did not appear to influence the virulence of L. monocytogenes.

Effects of Iron and Selenium on the Production of Catalase, Superoxide Dismutase, and Listeriolysin O in Listeria monocytogenes

1999 ◽  
Vol 62 (10) ◽  
pp. 1206-1209 ◽  
Author(s):  
CHRISTOPHER W. FISHER ◽  
SCOTT E. MARTIN
Keyword(s):  
Superoxide Dismutase ◽  
Listeria Monocytogenes ◽  
Listeriolysin O

Listeria monocytogenes 19112, Scott A, and 10403S were grown in tryptic soy broth (TSB) and TSB supplemented with 25 to 100 μg/ml of iron (Fe) and 0.5 to 2.5 μg/ml selenium (Se) to examine the effects on catalase (CA), superoxide dismutase (SOD), and listeriolysin O (LLO) activities. Growth in TSB supplemented with Fe resulted in significant increases in CA, SOD, and LLO activities in all three strains when compared to growth in TSB. The addition of 0.5 μg/ml Se to TSB resulted in significantly higher CA and LLO activities in L. monocytogenes 19112 but showed no effect on Scott A or 10403S. These results suggest that Fe plays a role in increasing the activities of CA, SOD, and LLO.

Influence of Plasmids on Catalase and Superoxide Dismutase Activities in Listeria monocytogenes

1995 ◽  
Vol 58 (9) ◽  
pp. 955-959 ◽  
Author(s):  
LOWELL L. ISOM ◽  
ALI H. AHMED ◽  
SCOTT E. MARTIN
Keyword(s):  
Superoxide Dismutase ◽  
Listeria Monocytogenes ◽  
Gradient Centrifugation ◽  
Plasmid Copy Number ◽  
Activity Levels ◽  
Wild Type ◽  
Cadmium Resistance ◽  
Sod Activity ◽  
Plasmid Copy ◽  
Cscl Density Gradient

Two of nine strains of Listeria monocytogenes examined were found to contain plasmid DNA. Strain 19112 contained a 31.1 kb plasmid and strain 7644 contained a 49.4 kb plasmid. Each of the strains was cured of its plasmid by heat treatment at 46°C. Both the wild-type and plasmid-negative forms of each strain were screened for cadmium resistance. The 31.1 kb plasmid of L. monocytogenes 19112 was shown to confer resistance to cadmium. Listeria monocytogenes 7644 did not show resistance to cadmium. The plasmids for both strains were isolated and purified by CsCl density-gradient centrifugation. Each plasmid was electroporated back into the respective plasmid-negative strain. The catalase (CA) and superoxide dismutase (SOD) activities were determined for the wild type, plasmid-negative and electroporated strains. There was a significant decrease in CA and SOD activities upon loss of the plasmid from each strain of L. monocytogenes. Strain 19112 showed a 36% decrease in CA activity and an 81% decrease in SOD activity as a result of plasmid removal. Strain 7644 showed a 22% decrease in both CA and SOD activities following plasmid loss. Catalase and SOD activity levels increased for both strains following reinsertion of the plasmid through electroporation. Catalase and SOD activity levels of L. monocytogenes 7644 were higher for the transformed strain than those of the wild type. Catalase and SOD activity levels of transformed L. monocytogenes 19112 were less than in the corresponding wild type. It appears that plasmids in L. monocytogenes strains 19112 and 7644 may be involved in influencing the regulation of the production of CA and SOD. Plasmid copy number may influence the level of activity of these enzymes.

Combined Effects of pH and Temperature on Listeriolysin O Production by Listeria monocytogenes SLCC 5764

1996 ◽  
Vol 59 (10) ◽  
pp. 1076-1078 ◽  
Author(s):  
LISA S. SCHILLING ◽  
SCOTT E. MARTIN
Keyword(s):  
Acetic Acid ◽  
Listeria Monocytogenes ◽  
Hydrochloric Acid ◽  
Sodium Hydroxide ◽  
Combined Effects ◽  
Listeriolysin O ◽  
Effects Of Ph ◽  
Acidic Conditions ◽  
Effects Of Temperature

Listeria monocytogenes SLCC 5764 was propagated at 4, 25, or 37°C in tryptic soy broth (TSB) acidified with either acetic acid at pH 5.2, 5.7, or 7.0, or hydrochloric acid at pH 5.0, 5.7, or 7.0; or made alkaline with sodium hydroxide at pH 7.5, 8.5, or 9.5. These studies were undertaken to determine the combined effects of temperature and pH on the production of listeriolysin O (LLO). The LLO activity was greatest after the cells were propagated in TSB acidified by either acid to pH 7.0 at 37°C. Very little LLO activity was detected for cells propagated at 4° under acidic conditions. There were no significant differences found between the LLO produced in media acidified with either acid. The LLO activity was highest after the cells were propagated in media at pH 7.5 at 37°C.

An inducible iron-containing superoxide dismutase in Rhizobium japonicum

1981 ◽  
Vol 27 (11) ◽  
pp. 1202-1208 ◽  
Author(s):  
Mark D. Stowers ◽  
Gerald H. Elkan
Keyword(s):  
Superoxide Dismutase ◽  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Metal Content ◽  
Methyl Viologen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Rhizobium Japonicum ◽  
Growth Media ◽  
Sod Activity ◽  
Rhizobium Spp

Crude extracts of Rhizobium japonicum contained a single superoxide dismutase (SOD) as revealed by polyacrylamide gel electrophoresis. Rhizobium japonicum SOD was determined to be iron-containing by criteria of sensitivity to 5 mM H2O2 and 1 mM NaN3. Growth media strongly influenced SOD activity. The addition of methyl viologen to cultures of R. japonicum 61A76NS, growing in complex medium, caused induction of the enzyme. Yeast extract was essential for induction of SOD. Puromycin blocked the induction of the enzyme. Rhizobium spp. were surveyed for SOD activity, electrophoretic mobility on polyacrylamide gels, and metal content.

Su.78. Analysis of T-Cell Responses to Listeria Monocytogenes Listeriolysin O in Healthy Adults

2006 ◽  
Vol 119 ◽  
pp. S186
Author(s):  
Johannes Hampl ◽  
Shruti Mathur ◽  
Weiqun Liu ◽  
Peter Lauer ◽  
Thomas Dubensky ◽  
...  
Keyword(s):  
Listeria Monocytogenes ◽  
T Cell ◽  
T Cell Responses ◽  
Healthy Adults ◽  
Listeriolysin O ◽  
Cell Responses

10-gingerol induces oxidative stress through HTR1A in cumulus cells: in-vitro and in-silico studies

2020 ◽  
Vol 0 (0) ◽  
Author(s):  
Kiptiyah Kiptiyah ◽  
Widodo Widodo ◽  
Gatot Ciptadi ◽  
Aulanni’am Aulanni’Am ◽  
Mohammad A. Widodo ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Cell Culture ◽  
Superoxide Dismutase ◽  
In Silico ◽  
Cumulus Cell ◽  
Cumulus Cells ◽  
Sod Activity ◽  
In Silico Studies ◽  
Incubation Periods

AbstractBackgroundWe investigated whether 10-gingerol is able to induce oxidative stress in cumulus cells.MethodsFor the in-vitro research, we used a cumulus cell culture in M199, containing 10-gingerol in various concentrations (0, 12, 16, and 20 µM), and detected oxidative stress through superoxide dismutase (SOD) activity and malondialdehyde (MDA) concentrations, with incubation periods of 24, 48, 72, and 96 h. The obtained results were confirmed by in-silico studies.ResultsThe in-vitro data revealed that SOD activity and MDA concentration increased with increasing incubation periods: SOD activity at 0 µM (1.39 ± 0.24i), 12 µM (16.42 ± 0.35ab), 16 µM (17.28 ± 0.55ab), 20 µM (17.81 ± 0.12a), with a contribution of 71.1%. MDA concentration at 0 µM (17.82 ± 1.39 l), 12 µM (72.99 ± 0.31c), 16 µM (79.77 ± 4.19b), 20 µM (85.07 ± 2.57a), with a contribution of 73.1%. Based on this, the in-silico data uncovered that 10˗gingerol induces oxidative stress in cumulus cells by inhibiting HTR1A functions and inactivating GSK3B and AKT˗1.Conclusions10-gingerol induces oxidative stress in cumulus cells through enhancing SOD activity and MDA concentration by inhibiting HTR1A functions and inactivating GSK3B and AKT˗1.

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