This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sheehan, B. J.
Right arrow Articles by Kroll, J. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sheehan, B. J.
Right arrow Articles by Kroll, J. S.

 Previous Article  |  Next Article 

Infection and Immunity, August 2000, p. 4778-4781, Vol. 68, No. 8
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

[Cu,Zn]-Superoxide Dismutase Mutants of the Swine Pathogen Actinobacillus pleuropneumoniae Are Unattenuated in Infections of the Natural Host

Brian J. Sheehan,1 Paul R. Langford,1 Andrew N. Rycroft,2 and J. Simon Kroll1,*

Molecular Infectious Diseases Group, Department of Paediatrics, Imperial College School of Medicine, St. Mary's Campus, London W2 1PG,1 and Department of Pathology and Infectious Diseases, The Royal Veterinary College, University of London, North Mymms, Hatfield, Hertfordshire AL9 7TA,2 United Kingdom

Received 31 January 2000/Returned for modification 17 April 2000/Accepted 1 May 2000

Actinobacillus pleuropneumoniae, the causative agent of porcine pleuropneumonia, contains a periplasmic Cu- and Zn-cofactored superoxide dismutase ([Cu,Zn]-SOD, or SodC) which has the potential, realized in other pathogens, to promote bacterial survival during infection by dismutating host-defense-derived superoxide. Here we describe the construction of a site-specific, [Cu,Zn]-SOD-deficient A. pleuropneumoniae serotype 1 mutant and show that although the mutant is highly sensitive to the microbicidal action of superoxide in vitro, it remains fully virulent in experimental pulmonary infection in pigs.


* Corresponding author. Mailing address: Molecular Infectious Diseases Group, Department of Paediatrics, Imperial College School of Medicine, St. Mary's Campus, London W2 1PG, United Kingdom. Phone: 020 7886 6220. Fax: 020 7886 6284. E-mail: s.kroll{at}ic.ac.uk.


Infection and Immunity, August 2000, p. 4778-4781, Vol. 68, No. 8
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Auger, E., Deslandes, V., Ramjeet, M., Contreras, I., Nash, J. H. E., Harel, J., Gottschalk, M., Olivier, M., Jacques, M. (2009). Host-Pathogen Interactions of Actinobacillus pleuropneumoniae with Porcine Lung and Tracheal Epithelial Cells. Infect. Immun. 77: 1426-1441 [Abstract] [Full Text]  
  • Balashova, N. V., Park, D. H., Patel, J. K., Figurski, D. H., Kachlany, S. C. (2007). Interaction between Leukotoxin and Cu,Zn Superoxide Dismutase in Aggregatibacter actinomycetemcomitans. Infect. Immun. 75: 4490-4497 [Abstract] [Full Text]  
  • Keith, K. E., Valvano, M. A. (2007). Characterization of SodC, a Periplasmic Superoxide Dismutase from Burkholderia cenocepacia. Infect. Immun. 75: 2451-2460 [Abstract] [Full Text]  
  • Fung, W. W. M., O'Dwyer, C. A., Sinha, S., Brauer, A. L., Murphy, T. F., Kroll, J. S., Langford, P. R. (2006). 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. 44: 4222-4226 [Abstract] [Full Text]  
  • Beddek, A. J., Sheehan, B. J., Bosse, J. T., Rycroft, A. N., Kroll, J. S., Langford, P. R. (2004). Two TonB Systems in Actinobacillus pleuropneumoniae: Their Roles in Iron Acquisition and Virulence. Infect. Immun. 72: 701-708 [Abstract] [Full Text]  
  • Bong, C. T. H., Fortney, K. R., Katz, B. P., Hood, A. F., Mateo, L. R. S., Kawula, T. H., Spinola, S. M. (2002). A Superoxide Dismutase C Mutant of Haemophilus ducreyi Is Virulent in Human Volunteers. Infect. Immun. 70: 1367-1371 [Abstract] [Full Text]  
  • Sansone, A., Watson, P. R., Wallis, T. S., Langford, P. R., Kroll, J. S. (2002). The role of two periplasmic copper- and zinc-cofactored superoxide dismutases in the virulence of Salmonella choleraesuis. Microbiology 148: 719-726 [Abstract] [Full Text]  
  • Piddington, D. L., Fang, F. C., Laessig, T., Cooper, A. M., Orme, I. M., Buchmeier, N. A. (2001). Cu,Zn Superoxide Dismutase of Mycobacterium tuberculosis Contributes to Survival in Activated Macrophages That Are Generating an Oxidative Burst. Infect. Immun. 69: 4980-4987 [Abstract] [Full Text]  
  • Baltes, N., Tonpitak, W., Gerlach, G.-F., Hennig-Pauka, I., Hoffmann-Moujahid, A., Ganter, M., Rothkotter, H.-J. (2001). Actinobacillus pleuropneumoniae Iron Transport and Urease Activity: Effects on Bacterial Virulence and Host Immune Response. Infect. Immun. 69: 472-478 [Abstract] [Full Text]  
  • Battistoni, A., Pacello, F., Mazzetti, A. P., Capo, C., Kroll, J. S., Langford, P. R., Sansone, A., Donnarumma, G., Valenti, P., Rotilio, G. (2001). 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. 276: 30315-30325 [Abstract] [Full Text]