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Published online before print February 3, 2006
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*Department of Biomedical Sciences, College of Medicine, University of Illinois at Chicago;
Virus and Immunity Group in the Department of Virology, Institut Pasteur, France;
Department of Microbiology and Immunology, Division of Infectious Diseases, Walther Oncology Center, Indiana University School of Medicine, Indianapolis; and
Molecular Epidemiology, Enteric Diseases Research Program, U.S. Naval Medical Research Unit-3, Cairo, Egypt
@ To whom correspondence should be addressed. E-mail: KlenaJ{at}namru3.med.navy.mil.
| Abstract |
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Neisseria gonorrhoeae (GC) or Escherichia coli HB101 (hereafter referred to as E. coli) expressing opacity (Opa) proteins adhere to human host cells and stimulate phagocytosis as a result of the interaction of certain Opa proteins to carcinoembryonic antigen-related cellular adhesion molecule 1 (CEACAM1; CD66a) receptors. Our experiments show that the Opa-CEACAM1 interaction does not play a significant role in adherence between these bacteria and dendritic cells (DCs). Instead, phagocytosis of GC and E. coli by DCs is mediated by the DC-specific intercellular adhesion molecule-grabbing nonintegrin, (SIGN; CD209) receptor. DC-SIGN recognition and subsequent phagocytosis of GC are limited, however, to a lipooligosaccharide (LOS) mutant (lgtB) of GC. This conclusion is supported by experiments demonstrating that HeLa cells expressing human DC-SIGN (HeLa-DC-SIGN) bind exclusively to and engulf an lgtB mutant of GC, and this interaction is blocked specifically by an anti-DC-SIGN antibody. The experiments suggest that LOS variation may have evolved as a mechanism for GC to avoid phagocytosis by DCs.
Key Words: Escherichia coli dendritic cells CEACAM1 (CD66a)
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