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Infection and Immunity, September 1998, p. 4484-4490, Vol. 66, No. 9
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Alteration of HLA-B27 Peptide Presentation after Infection of Transfected Murine L Cells by Shigella flexneri

Florence Boisgérault,1 Joëlle Mounier,2 Vannary Tieng,1 Marie-Claude Stolzenberg,1 Iman Khalil-Daher,1 Michel Schmid,3 Philippe Sansonetti,2 Dominique Charron,1 and Antoine Toubert1,*

Unité d'Immunogénétique Humaine, INSERM U396, Institut Biomédical des Cordeliers, 75006 Paris, and Hôpital Saint-Louis, Centre G. Hayem, 75475 Paris Cedex 10,1 Unité de Pathogénie Microbienne Moléculaire, INSERM U389, Institut Pasteur, 75724 Paris Cedex 15,2 and Plateau Technique, Centre G. Hayem, Hôpital Saint-Louis, 75475 Paris Cedex 10,3 France

Received 27 December 1997/Returned for modification 6 March 1998/Accepted 29 May 1998

Shigella flexneri is a triggering agent for reactive arthritis in HLA-B27-susceptible individuals. Considering the intracellular multiplication of bacteria, it seems likely that bacterial peptides may be presented by the major histocompatibility complex (MHC) class I pathway. To examine this hypothesis, we infected HLA-B*2705- and/or human beta 2-microglobulin-transfected murine L-cell lines with M90T, an invasive strain of S. flexneri. Bacterial infection induced no detectable modifications in the biosynthesis and expression level of HLA-B27, as assessed by immunoprecipitation, Northern blot analysis, and flow cytometry. Using confocal microscopy, we observed that bacterial infection induced a clustering of HLA-B27 molecules during macropinocytosis and before bacterial dissemination from cell to cell. Peptides naturally bound to HLA-B27 molecules were acid eluted from infected cells and separated by high-performance liquid chromatography. Major differences were observed in high-performance liquid chromatography profiles and in the nature of peptides presented following bacterial infection. Although most of the antigens presented were not accessed by Edman degradation, we obtained two sequences partially homologous to bacterial proteins. These peptides lacked the major HLA-B27 peptide anchor (Arg) at position 2, and one had an unusual length of 14 amino acids. These data suggest that alterations in the peptide presentation by HLA-B27 occur during infection, which could be relevant to the pathogenesis of HLA-B27-related arthritis.

* Corresponding author. INSERM U.396, Hôpital Saint-Louis, Centre G. Hayem, 1, Av. C. Vellefaux, 75475 Paris Cedex 10, France. Phone: 33.1.42.49.95.42. Fax: 33.1.42.49.44.49. E-mail: toubert{at}histo.chu-stlouis.fr.

Infection and Immunity, September 1998, p. 4484-4490, Vol. 66, No. 9
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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