JBC Avanti Polar Lipids

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hassett, D. J.
Right arrow Articles by Cohen, M. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hassett, D. J.
Right arrow Articles by Cohen, M. S.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 262, Issue 28, 13404-13408, Oct, 1987

Bacteria form intracellular free radicals in response to paraquat and streptonigrin. Demonstration of the potency of hydroxyl radical

DJ Hassett, BE Britigan, T Svendsen, GM Rosen and MS Cohen
Department of Pharmacology, Duke University Medical Center, Durham, North Carolina 27710.

The generation of oxygen reduction products by Neisseria gonorrhoeae FA1090 upon exposure to streptonigrin (SNG) and paraquat (PQ2+) and their toxicity was examined. N. gonorrhoeae exhibited maximal cyanide- insensitive respiration, which was employed as an indicator of superoxide (O2-) formation, in the presence of 0.064 mM streptonigrin and 90 mM PQ2+, respectively. Using the concentrations of SNG and PQ2+ described above, complete lethality (greater than 10(8) cells/ml) was observed among cells exposed to SNG, whereas PQ2+ reduced viability by only 3 logs. In an attempt to determine the oxygen radical species generated by gonococci when exposed to SNG, dimethyl sulfoxide, Fe3+, KCN, and the spin trap 5,5-dimethyl-1-pyrroline-N-oxide (DMPO), we were able to detect .OH manifested as the methyl adduct (DMPO-CH3). The production of the latter species was not inhibited by catalase, suggesting intracellular .OH generation. When PQ2+ was substituted for SNG, only low levels of DMPO-CH3 were observed, the production of which ceased within 8 min. SNG and PQ2+, added to a O2(-)- generating system in the presence of Fe3+, promoted increased .OH generation. The iron chelator diethyl-enetriaminepentaacetic acid enhanced the generation of spin-trapped .OH and O2- in the presence of PQ2+. The addition of catalase to this system, however, eliminated the DMPO-CH3 signal, showing that the .OH in this system was extracellular. PQ2+-mediated generation of extracellular .OH in the presence of Fe3+- diethylenetriaminepentaacetic acid EDTA did not enhance the killing of gonococci by PQ2+. These data show that the lethality of SNG relative to PQ2+ is due to the inherent ability of SNG to catalyze the formation of critical levels of intracellular .OH, detectable through the use of spin trapping techniques.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Appl. Environ. Microbiol.Home page
W. Kitphati, P. Ngok-ngam, S. Suwanmaneerat, R. Sukchawalit, and S. Mongkolsuk
Agrobacterium tumefaciens fur Has Important Physiological Roles in Iron and Manganese Homeostasis, the Oxidative Stress Response, and Full Virulence
Appl. Envir. Microbiol., August 1, 2007; 73(15): 4760 - 4768.
[Abstract] [Full Text] [PDF]


Home page
Microbiol. Mol. Biol. Rev.Home page
K. L. Seib, H.-J. Wu, S. P. Kidd, M. A. Apicella, M. P. Jennings, and A. G. McEwan
Defenses against Oxidative Stress in Neisseria gonorrhoeae: a System Tailored for a Challenging Environment
Microbiol. Mol. Biol. Rev., June 1, 2006; 70(2): 344 - 361.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
C. Y. Loo, K. Mitrakul, S. Jaafar, C. Gyurko, C. V. Hughes, and N. Ganeshkumar
Role of a nosX Homolog in Streptococcus gordonii in Aerobic Growth and Biofilm Formation
J. Bacteriol., December 15, 2004; 186(24): 8193 - 8206.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
Y. M. Ibrahim, A. R. Kerr, J. McCluskey, and T. J. Mitchell
Role of HtrA in the Virulence and Competence of Streptococcus pneumoniae
Infect. Immun., June 1, 2004; 72(6): 3584 - 3591.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
H.-J. Tseng, A. G. McEwan, M. A. Apicella, and M. P. Jennings
OxyR Acts as a Repressor of Catalase Expression in Neisseria gonorrhoeae
Infect. Immun., January 1, 2003; 71(1): 550 - 556.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
M. Elgrably-Weiss, S. Park, E. Schlosser-Silverman, I. Rosenshine, J. Imlay, and S. Altuvia
A Salmonella enterica Serovar Typhimurium hemA Mutant Is Highly Susceptible to Oxidative DNA Damage
J. Bacteriol., July 15, 2002; 184(14): 3774 - 3784.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
H.-J. Tseng, A. G. McEwan, J. C. Paton, and M. P. Jennings
Virulence of Streptococcus pneumoniae: PsaA Mutants Are Hypersensitive to Oxidative Stress
Infect. Immun., March 1, 2002; 70(3): 1635 - 1639.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
K. E. Wilks, K. L. R. Dunn, J. L. Farrant, K. M. Reddin, A. R. Gorringe, P. R. Langford, and J. S. Kroll
Periplasmic Superoxide Dismutase in Meningococcal Pathogenicity
Infect. Immun., January 1, 1998; 66(1): 213 - 217.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1987 by the American Society for Biochemistry and Molecular Biology.