| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
* Department of Biomedical Sciences, College of Medicine, University of Illinois at Chicago, Rockford, IL 61107;
Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602;
Division of Microbiological Studies, U.S. Food and Drug Administration, College Park, MD 20740;
Faculty of Life Sciences, Department of Marine Biology, University of Vienna, Vienna, Austria;
¶ Salmonella Genetic Stock Centre, Department of Biological Sciences, Alberta, Canada;
|| Department of Microbiology and Immunology, Indiana University School of Medicine, Indianapolis, IN 46202; and
# School of Biological Sciences, University of Canterbury, Christchurch, New Zealand
Our recent studies have shown that the dendritic cell-specific ICAM nonintegrin CD209 (DC-SIGN) specifically binds to the core LPS of Escherichia coli K12 (E. coli), promoting bacterial adherence and phagocytosis. In this current study, we attempted to map the sites within the core LPS that are directly involved in LPS-DC-SIGN interaction. We took advantage of four sets of well-defined core LPS mutants, which are derived from E. coli, Salmonella enterica serovar Typhimurium, Neisseria gonorrhoeae, and Haemophilus ducreyi and determined interaction of each of these four sets with DC-SIGN. Our results demonstrated that N-acetylglucosamine (GlcNAc) sugar residues within the core LPS in these bacteria play an essential role in targeting the DC-SIGN receptor. Our results also imply that DC-SIGN is an innate immune receptor and the interaction of bacterial core LPS and DC-SIGN may represent a primeval interaction between Gram-negative bacteria and host phagocytic cells.
The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
1 This work was supported by Public Health Service Grant R01AI 47736 (to T.C.).
2 Address correspondence and reprint requests to Dr. Tie Chen, Department of Biomedical Sciences, College of Medicine, University of Illinois at Chicago, 1601 Parkview Avenue, Rockford, IL 61107; E-mail address: tiechen{at}uic.edu or Dr. John Klena, School of Biological Sciences, University of Canterbury, Christchurch, New Zealand; E-mail address: paua4T{at}yahoo.com
3 Abbreviations used in this paper: DC, dendritic cell; DC-SIGN, DC-specific ICAM nonintegrin; LOS, lipo-oligosaccharide; Opa, opacity.
This article has been cited by other articles:
|
|
 |
|
  P. Zhang, M. Skurnik, S.-S. Zhang, O. Schwartz, R. Kalyanasundaram, S. Bulgheresi, J. J. He, J. D. Klena, B. J. Hinnebusch, and T. Chen Human Dendritic Cell-Specific Intercellular Adhesion Molecule-Grabbing Nonintegrin (CD209) Is a Receptor for Yersinia pestis That Promotes Phagocytosis by Dendritic Cells Infect. Immun., May 1, 2008; 76(5): 2070 - 2079. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. Sahly, Y. Keisari, E. Crouch, N. Sharon, and I. Ofek Recognition of Bacterial Surface Polysaccharides by Lectins of the Innate Immune System and Its Contribution to Defense against Infection: the Case of Pulmonary Pathogens Infect. Immun., April 1, 2008; 76(4): 1322 - 1332. [Full Text] [PDF]
|
|
|
|
|
|
K. E. Banks, T. L. Humphreys, W. Li, B. P. Katz, D. S. Wilkes, and S. M. Spinola Haemophilus ducreyi Partially Activates Human Myeloid Dendritic Cells Infect. Immun., December 1, 2007; 75(12): 5678 - 5685. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
