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Infection and Immunity, January 2001, p. 154-158, Vol. 69, No. 1
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.1.154-158.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Cloning and Expression of the Actinobacillus actinomycetemcomitans Thioredoxin (trx) Gene and Assessment of Cytokine Inhibitory Activity

Brian Henderson,1,* Peter Tabona,1 Stephen Poole,2 and Sean P. Nair1

Cellular Microbiology Research Group, Eastman Dental Institute, University College London, London WC1X 8LD,1 and Division of Endocrinology, National Institute for Biological Standards and Control, Potters Bar, Herts,2 United Kingdom

Received 14 September 2000/Accepted 11 October 2000

Thioredoxin is a ubiquitous redox control and cell stress protein. Unexpectedly, in recent years, thioredoxins have been found to exhibit both cytokine and chemokine activities, and there is increasing evidence that this class of protein plays a role in the pathogenesis of inflammatory diseases. In spite of this evidence, it has been reported that the oral bacterium and periodontopathogen Actinobacillus actinomycetemcomitans secretes an immunosuppressive factor (termed suppressive factor 1 [SF1] [T. Kurita-Ochiai and K. Ochiai, Infect. Immun. 64:50-54, 1996]) whose N-terminal sequence, we have determined, identifies it as thioredoxin. We have cloned and expressed the gene encoding the thioredoxin of A. actinomycetemcomitans and have purified the protein to homogeneity. The A. actinomycetemcomitans trx gene has 52 and 76% identities, respectively, to the trx genes of Escherichia coli and Haemophilus influenzae. Enzymatic analysis revealed that the recombinant protein had the expected redox activity. When the recombinant thioredoxin was tested for its capacity to inhibit the production of cytokines by human peripheral blood mononuclear cells, it showed no significant inhibitory capacity. We therefore conclude that the thioredoxin of A. actinomycetemcomitans does not act as an immunosuppressive factor, at least with human leukocytes in cultures, and that the identity of SF1 remains to be elucidated.

* Corresponding author. Mailing address: Cellular Microbiology Research Group, Eastman Dental Institute, University College London, 256 Gray's Inn Rd., London WC1X 8LD, United Kingdom. Phone: 0171 915 1190. Fax: 0171 915 1190. E-mail: b.henderson{at}eastman.ucl.ac.uk.

Infection and Immunity, January 2001, p. 154-158, Vol. 69, No. 1
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.1.154-158.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Henderson, B., Allan, E., Coates, A. R. M. (2006). Stress Wars: the Direct Role of Host and Bacterial Molecular Chaperones in Bacterial Infection. Infect. Immun. 74: 3693-3706 [Full Text]  
  • Akifusa, S., Heywood, W., Nair, S. P., Stenbeck, G., Henderson, B. (2005). Mechanism of internalization of the cytolethal distending toxin of Actinobacillus actinomycetemcomitans. Microbiology 151: 1395-1402 [Abstract] [Full Text]  
  • HENDERSON, B., WILSON, M., SHARP, L., WARD, J. M. (2002). Actinobacillus actinomycetemcomitans. J Med Microbiol 51: 1013-1020 [Full Text]  
  • Akifusa, S., Poole, S., Lewthwaite, J., Henderson, B., Nair, S. P. (2001). Recombinant Actinobacillus actinomycetemcomitans Cytolethal Distending Toxin Proteins Are Required To Interact To Inhibit Human Cell Cycle Progression and To Stimulate Human Leukocyte Cytokine Synthesis. Infect. Immun. 69: 5925-5930 [Abstract] [Full Text]  


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