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


     

Microbiology 141 (1995), 2271-2279
This Article
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 CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kroll, J. S.
Right arrow Articles by Keil, A. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kroll, J. S.
Right arrow Articles by Keil, A. D.
Agricola
Right arrow Articles by Kroll, J. S.
Right arrow Articles by Keil, A. D.

microbiology, Vol 141, 2271-2279, Copyright © 1995 by Society for General Microbiology

ARTICLES

Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinct from the eukaryotic enzyme, and not so rare after all!

JS Kroll, PR Langford, KE Wilks and AD Keil
Department of Paediatrics, Imperial College of Science, Technology and Medicine, St Mary's Hospital, London, UK.

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.


This article has been cited by other articles:


Home page
 J. Bacteriol.Home page
R. Krishnakumar, B. Kim, E. A. Mollo, J. A. Imlay, and J. M. Slauch
Structural Properties of Periplasmic SodCI That Correlate with Virulence in Salmonella enterica Serovar Typhimurium
J. Bacteriol., June 15, 2007; 189(12): 4343 - 4352.
[Abstract] [Full Text] [PDF]

Home page
 J. Clin. Microbiol.Home page
J. Zhou, D. K. S. Law, M. L. Sill, and R. S. W. Tsang
Nucleotide Sequence Diversity of the bexA Gene in Serotypeable Haemophilus influenzae Strains Recovered from Invasive Disease Patients in Canada
J. Clin. Microbiol., June 1, 2007; 45(6): 1996 - 1999.
[Abstract] [Full Text] [PDF]

Home page
 J. Clin. Microbiol.Home page
W. W. M. Fung, C. A. O'Dwyer, S. Sinha, A. L. Brauer, T. F. Murphy, J. S. Kroll, and P. R. Langford
Presence of Copper- and Zinc-Containing Superoxide Dismutase in Commensal Haemophilus haemolyticus Isolates Can Be Used as a Marker To Discriminate Them from Nontypeable H. influenzae Isolates
J. Clin. Microbiol., November 1, 2006; 44(11): 4222 - 4226.
[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
K. D. Passalacqua, N. H. Bergman, A. Herring-Palmer, and P. Hanna
The Superoxide Dismutases of Bacillus anthracis Do Not Cooperatively Protect against Endogenous Superoxide Stress
J. Bacteriol., June 1, 2006; 188(11): 3837 - 3848.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
J. M. Gee, M. W. Valderas, M. E. Kovach, V. K. Grippe, G. T. Robertson, W.-L. Ng, J. M. Richardson, M. E. Winkler, and R. M. Roop II
The Brucella abortus Cu,Zn Superoxide Dismutase Is Required for Optimal Resistance to Oxidative Killing by Murine Macrophages and Wild-Type Virulence in Experimentally Infected Mice
Infect. Immun., May 1, 2005; 73(5): 2873 - 2880.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
R. Krishnakumar, M. Craig, J. A. Imlay, and J. M. Slauch
Differences in Enzymatic Properties Allow SodCI but Not SodCII To Contribute to Virulence in Salmonella enterica Serovar Typhimurium Strain 14028
J. Bacteriol., August 15, 2004; 186(16): 5230 - 5238.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
K. L. R. Dunn, J. L. Farrant, P. R. Langford, and J. S. Kroll
Bacterial [Cu,Zn]-Cofactored Superoxide Dismutase Protects Opsonized, Encapsulated Neisseria meningitidis from Phagocytosis by Human Monocytes/Macrophages
Infect. Immun., March 1, 2003; 71(3): 1604 - 1607.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
A. Sansone, P. R. Watson, T. S. Wallis, P. R. Langford, and J. S. Kroll
The role of two periplasmic copper- and zinc-cofactored superoxide dismutases in the virulence of Salmonella choleraesuis
Microbiology, March 1, 2002; 148(3): 719 - 726.
[Abstract] [Full Text] [PDF]

Home page
 J. Clin. Microbiol.Home page
P. R. Langford, B. J. Sheehan, T. Shaikh, and J. S. Kroll
Active Copper- and Zinc-Containing Superoxide Dismutase in the Cryptic Genospecies of Haemophilus Causing Urogenital and Neonatal Infections Discriminates Them from Haemophilus influenzae Sensu Stricto
J. Clin. Microbiol., January 1, 2002; 40(1): 268 - 270.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
V. Leclere, A. Chotteau-Lelievre, F. Gancel, M. Imbert, and R. Blondeau
Occurrence of two superoxide dismutases in Aeromonas hydrophila: molecular cloning and differential expression of the sodA and sodB genes
Microbiology, November 1, 2001; 147(11): 3105 - 3111.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
B. J. Sheehan, P. R. Langford, A. N. Rycroft, and J. S. Kroll
[Cu,Zn]-Superoxide Dismutase Mutants of the Swine Pathogen Actinobacillus pleuropneumoniae Are Unattenuated in Infections of the Natural Host
Infect. Immun., August 1, 2000; 68(8): 4778 - 4781.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
A. Battistoni, F. Pacello, S. Folcarelli, M. Ajello, G. Donnarumma, R. Greco, M. Grazia Ammendolia, D. Touati, G. Rotilio, and P. Valenti
Increased Expression of Periplasmic Cu,Zn Superoxide Dismutase Enhances Survival of Escherichia coli Invasive Strains within Nonphagocytic Cells
Infect. Immun., January 1, 2000; 68(1): 30 - 37.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Yamahara, T. Shiono, T. Suzuki, K. Tanaka, S. Takio, K. Sato, S. Yamazaki, and T. Satoh
Isolation of a Germin-like Protein with Manganese Superoxide Dismutase Activity from Cells of a Moss, Barbula unguiculata
J. Biol. Chem., November 19, 1999; 274(47): 33274 - 33278.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
M. C. Lynch and H. K. Kuramitsu
Role of Superoxide Dismutase Activity in the Physiology of Porphyromonas gingivalis
Infect. Immun., July 1, 1999; 67(7): 3367 - 3375.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
F. C. Fang, M. A. DeGroote, J. W. Foster, A. J. Baumler, U. Ochsner, T. Testerman, S. Bearson, J.-C. Giard, Y. Xu, G. Campbell, et al.
Virulent Salmonella typhimurium has two periplasmic Cu, Zn-superoxide dismutases
PNAS, June 22, 1999; 96(13): 7502 - 7507.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
J. S. Kroll, K. E. Wilks, J. L. Farrant, and P. R. Langford
Natural genetic exchange between Haemophilus and Neisseria: Intergeneric transfer of chromosomal genes between major human pathogens
PNAS, October 13, 1998; 95(21): 12381 - 12385.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Battistoni, S. Folcarelli, L. Cervoni, F. Polizio, A. Desideri, A. Giartosio, and G. Rotilio
Role of the Dimeric Structure in Cu,Zn Superoxide Dismutase. pH-DEPENDENT, REVERSIBLE DENATURATION OF THE MONOMERIC ENZYME FROM ESCHERICHIA COLI
J. Biol. Chem., March 6, 1998; 273(10): 5655 - 5661.
[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 page
 Proc. Natl. Acad. Sci. USAHome page
M. A. De Groote, U. A. Ochsner, M. U. Shiloh, C. Nathan, J. M. McCord, M. C. Dinauer, S. J. Libby, A. Vazquez-Torres, Y. Xu, and F. C. Fang
Periplasmic superoxide dismutase protects Salmonella from products of phagocyte NADPH-oxidase and nitric oxide synthase
PNAS, December 9, 1997; 94(25): 13997 - 14001.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
Y. Bourne, S. M. Redford, H. M. Steinman, J. R. Lepock, J. A. Tainer, and E. D. Getzoff
Novel dimeric interface and electrostatic recognition in bacterial Cu,Zn superoxide dismutase
PNAS, November 12, 1996; 93(23): 12774 - 12779.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
F. Pacello, P. R. Langford, J. S. Kroll, C. Indiani, G. Smulevich, A. Desideri, G. Rotilio, and A. Battistoni
A Novel Heme Protein, the Cu,Zn-Superoxide Dismutase from Haemophilus ducreyi
J. Biol. Chem., August 3, 2001; 276(32): 30326 - 30334.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Battistoni, F. Pacello, A. P. Mazzetti, C. Capo, J. S. Kroll, P. R. Langford, A. Sansone, G. Donnarumma, P. Valenti, and G. Rotilio
A Histidine-rich Metal Binding Domain at the N Terminus of Cu,Zn-Superoxide Dismutases from Pathogenic Bacteria. A NOVEL STRATEGY FOR METAL CHAPERONING
J. Biol. Chem., August 3, 2001; 276(32): 30315 - 30325.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 1995 Society for General Microbiology.