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Infection and Immunity, September 2004, p. 5097-5105, Vol. 72, No. 9
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.9.5097-5105.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Major Histocompatibility Complex Class I Peptide Presentation after Salmonella enterica Serovar Typhimurium Infection Assessed via Stable Isotope Tagging of the B27-Presented Peptide Repertoire

Jeffrey H. Ringrose,1* Hugo D. Meiring,2 Dave Speijer,3 Theodorus E. W. Feltkamp,4 Cecile A. C. M. van Els,5 Ad P. J. M. de Jong,2 and Jacob Dankert1

Department of Medical Microbiology,1 Department of Biochemistry, Academic Medical Centre, University of Amsterdam,3 Arthron, Amsterdam,4 Laboratory for Organic Analytical Chemistry, National Institute of Public Health and the Environment,2 Laboratory of Vaccine Research, Netherlands Vaccine Institute, Bilthoven, The Netherlands5

Received 28 January 2004/ Returned for modification 20 May 2004/ Accepted 28 May 2004

Reactive arthritis (ReA) induced by infection with several gram-negative bacteria is strongly associated with expression of the major histocompatibility complex class I molecule HLA-B27. It is thought that due to the intracellular lifestyle of ReA-inducing bacteria, bacterial fragments can be presented by HLA-B27. Cytotoxic T cells recognizing such bacterial peptides or other induced host peptides could cross-react with self peptides presented in the joints, giving rise to disease. Studies to analyze the B27 peptide repertoire in relation to infection were severely hampered, as complex peptide profiles obtained from separate infected and noninfected cell preparations had to be compared. For this study, we applied a new approach to examine the effect of Salmonella enterica serovar Typhimurium infection on the B27 peptide repertoire presented by the HLA-B*2704 subtype associated with disease. Firstly, we showed that both host cell and S. enterica serovar Typhimurium proteins can be tagged metabolically with stable-isotope-labeled arginine. We then designed experiments so that either the tagged endogenous or tagged bacterial B*2704-presented peptide repertoires from infected cells could be analyzed by mass spectrometry from single peptide preparations that included uninfected controls. Using this new approach, we found no evidence for significant changes in endogenous B*2704 peptide presentation after infection or for any S. enterica serovar Typhimurium-derived B27-bound peptide. In conclusion, the hypothesis that S. enterica serovar Typhimurium induces changes in B27 peptide presentation could not be supported.

* Corresponding author. Mailing address: Department of Human Virology, AMC K1-110, Meibergdreef 15, 1105AZ Amsterdam, The Netherlands. Phone: 31-20-5663297. Fax: 31-20-6915519. E-mail: j.ringrose{at}amc.uva.nl.

Editor: F. C. Fang

Infection and Immunity, September 2004, p. 5097-5105, Vol. 72, No. 9
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.9.5097-5105.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Cragnolini, J. J., de Castro, J. A. L. (2008). Identification of Endogenously Presented Peptides from Chlamydia trachomatis with High Homology to Human Proteins and to a Natural Self-ligand of HLA-B27. Mol. Cell. Proteomics 7: 170-180 [Abstract] [Full Text]  
  • Marcilla, M., Cragnolini, J. J., Lopez de Castro, J. A. (2007). Proteasome-independent HLA-B27 Ligands Arise Mainly from Small Basic Proteins. Mol. Cell. Proteomics 6: 923-938 [Abstract] [Full Text]  


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