title: DC-SIGN (CD209) recognition of Neisseria gonorrhoeae is circumvented by lipooligosaccharide variation.
abstract: 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.
authors.affiliation: Department of Biomedical Sciences, College of Medicine, University of Illinois at Chicago, USA.
authors.forename: Pei
authors.initials: P
authors.lastname: Zhang
authors.forename: Olivier
authors.initials: O
authors.lastname: Schwartz
authors.forename: Milica
authors.initials: M
authors.lastname: Pantelic
authors.forename: Geling
authors.initials: G
authors.lastname: Li
authors.forename: Quita
authors.initials: Q
authors.lastname: Knazze
authors.forename: Cinzia
authors.initials: C
authors.lastname: Nobile
authors.forename: Milan
authors.initials: M
authors.lastname: Radovich
authors.forename: Johnny
authors.initials: J
authors.lastname: He
authors.forename: Soon-Cheol
authors.initials: SC
authors.lastname: Hong
authors.forename: John
authors.initials: J
authors.lastname: Klena
authors.forename: Tie
authors.initials: T
authors.lastname: Chen
mesh_terms: D000906:Antibodies / Q000494:pharmacology; D000940:Antigenic Variation / Q000276:immunology*; D000942:Antigens, Bacterial / Q000276:immunology; D015703:Antigens, CD / Q000096:biosynthesis; D001422:Bacterial Adhesion / Q000276:immunology; D001665:Binding Sites; D015815:Cell Adhesion Molecules / Q000037:antagonists & inhibitors / Q000096:biosynthesis / Q000276:immunology*; D002478:Cells, Cultured; D003713:Dendritic Cells / Q000276:immunology / Q000382:microbiology; D004926:Escherichia coli / Q000276:immunology; D006367:HeLa Cells; D006801:Humans; D037181:Lectins, C-Type / Q000037:antagonists & inhibitors / Q000276:immunology*; D008070:Lipopolysaccharides / Q000276:immunology*; D008351:Mannans / Q000494:pharmacology; D009344:Neisseria gonorrhoeae / Q000276:immunology*; D010587:Phagocytosis / Q000276:immunology; D011956:Receptors, Cell Surface / Q000037:antagonists & inhibitors / Q000276:immunology*; D000099215:DC-Specific ICAM-3 Grabbing Nonintegrin
chemical_list: D000906:Antibodies; D000942:Antigens, Bacterial; D015703:Antigens, CD; D015815:Cell Adhesion Molecules; D037181:Lectins, C-Type; D008070:Lipopolysaccharides; D008351:Mannans; D011956:Receptors, Cell Surface; D000099215:DC-Specific ICAM-3 Grabbing Nonintegrin; C069847:CD66 antigens; C023023:lipid-linked oligosaccharides; C050308:opacity proteins