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Journal of Bacteriology, March 2005, p. 1710-1715, Vol. 187, No. 5
0021-9193/05/$08.00+0     doi:10.1128/JB.187.5.1710-1715.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

The Core Lipopolysaccharide of Escherichia coli Is a Ligand for the Dendritic-Cell-Specific Intercellular Adhesion Molecule Nonintegrin CD209 Receptor

School of Molecular Biosciences, Washington State University, Pullman, Washington,¹ Department of Microbiology and Immunology, Division of Infectious Diseases, Walther Oncology Center, Indiana University School of Medicine, Indianapolis, Indiana,² Virus and Immunity Group, Department of Virology, Institut Pasteur, Paris, France,³ Department of Microbiology and Immunology, Baylor College of Medicine, Houston, Texas⁴

Received 1 November 2004/ Accepted 16 November 2004

The dendritic-cell-specific intercellular adhesion molecule nonintegrin (DC-SIGN) CD209 is a receptor for Escherichia coli K-12 that promotes bacterial adherence and phagocytosis. However, the ligand of E. coli for DC-SIGN has not yet been identified. In this study, we found that DC-SIGN did not mediate the phagocytosis of several pathogenic strains of E. coli, including enteropathogenic E. coli, enterohemorrhagic E. coli, enterotoxigenic E. coli, and uropathogenic E. coli, in dendritic cells or HeLa cells expressing human DC-SIGN antigen. However, we showed that an outer core lipopolysaccharide (LPS) (rough) mutant, unlike an inner core LPS (deep rough) mutant or O-antigen-expressing recombinant of E. coli K-12 was phagocytosed. These results demonstrate that the host cells expressing DC-SIGN can phagocytose E. coli in part by interacting with the complete core region of the LPS molecule. These results provide a mechanism for how O antigen acts as an antiphagocytic factor.

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