SEARCH:   Advanced

Blood, 1 April 2007, Vol. 109, No. 7, pp. 2936-2943. Prepublished online as a Blood First Edition Paper on November 28, 2006; DOI 10.1182/blood-2006-06-015461. This Article Full Text Full Text (PDF) All Versions of this Article: blood-2006-06-015461v1 109/7/2936    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Bestebroer, J. Articles by de Haas, C. J. C. Search for Related Content PubMed PubMed Citation Articles by Bestebroer, J. Articles by de Haas, C. J. C. Related Collections Immunobiology Phagocytes Cytoskeleton Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  IMMUNOBIOLOGY Staphylococcal superantigen-like 5 binds PSGL-1 and inhibits P-selectin–mediated neutrophil rolling Jovanka Bestebroer1, Miriam J. J. G. Poppelier1, Laurien H. Ulfman2, Peter J. Lenting3, Cecile V. Denis4,5, Kok P. M. van Kessel1, Jos A. G. van Strijp1, and Carla J. C. de Haas1 1 Experimental Microbiology, University Medical Center Utrecht, The Netherlands; 2 Department of Pulmonary Diseases, University Medical Center Utrecht, The Netherlands; 3 Department of Haematology, University Medical Center Utrecht, The Netherlands; 4 Institut National de la Santé et de la Recherche Médicale (INSERM) Unité 770, Le Kremlin-Bicêtre, France; 5 Université Paris-Sud, Le Kremlin-Bicêtre, France Staphylococcus aureus secretes several virulence factors interfering with host-cell functions. Staphylococcal superantigen-like (SSL) proteins are a family of 11 exotoxins with structural homology to superantigens but with generally unknown functions. Recently, we described that chemotaxis inhibitory protein of Staphylococcus aureus (CHIPS31-121), a potent inhibitor of C5a-induced responses, is structurally homologous to the C-terminal domain of SSL5. Here, we identify P-selectin glycoprotein ligand-1 (PSGL-1), involved in the initial rolling of neutrophils along the endothelium, as a target for SSL5. SSL5 specifically bound to Chinese hamster ovary cells stably expressing PSGL-1 (CHO–PSGL-1), which was dependent of sulfation and sialylation. Furthermore, SSL5 bound to PSGL-1/Ig fusion protein immobilized on a biosensor chip. SSL5 affected binding of soluble P-selectin/Fc chimera, the principle ligand of PSGL-1, to CHO–PSGL-1 cells and inhibited adhesion of neutrophils to immobilized P-selectin under static conditions. Under flow conditions SSL5 strongly decreased neutrophil rolling on immobilized P-selectin/Fc and activated human endothelial cells. In conclusion, SSL5 interferes with the interaction between PSGL-1 and P-selectin, suggesting that S aureus uses SSL5 to prevent neutrophil extravasation toward the site of infection. This makes SSL5 a potential lead for the development of new anti-inflammatory compounds for disorders characterized by excessive recruitment of leukocytes. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: I. Jongerius, J. Kohl, M. K. Pandey, M. Ruyken, K. P.M. van Kessel, J. A.G. van Strijp, and S. H.M. Rooijakkers Staphylococcal complement evasion by various convertase-blocking molecules J. Exp. Med., October 1, 2007; 204(10): 2461 - 2471. [Abstract] [Full Text] [PDF] P. A. Ramsland, N. Willoughby, H. M. Trist, W. Farrugia, P. M. Hogarth, J. D. Fraser, and B. D. Wines Structural basis for evasion of IgA immunity by Staphylococcus aureus revealed in the complex of SSL7 with Fc of human IgA1 PNAS, September 18, 2007; 104(38): 15051 - 15056. [Abstract] [Full Text] [PDF]

	Copyright © 2007 by American Society of Hematology         Online ISSN: 1528-0020