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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2006-4-6
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/CD66 antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/DC-specific ICAM-3 grabbing...,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins, C-Type,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Mannans,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/lipid-linked oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/opacity proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0741-5400
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pubmed:author |
pubmed-author:ChenTieT,
pubmed-author:HeJohnnyJ,
pubmed-author:HongSoon-CheolSC,
pubmed-author:KlenaJohnJ,
pubmed-author:KnazzeQuitaQ,
pubmed-author:LiGelingG,
pubmed-author:NobileCinziaC,
pubmed-author:PantelicMilicaM,
pubmed-author:RadovichMilanM,
pubmed-author:SchwartzOlivierO,
pubmed-author:ZhangPeiP
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pubmed:issnType |
Print
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pubmed:volume |
79
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
731-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16461738-Antibodies,
pubmed-meshheading:16461738-Antigenic Variation,
pubmed-meshheading:16461738-Antigens, Bacterial,
pubmed-meshheading:16461738-Antigens, CD,
pubmed-meshheading:16461738-Bacterial Adhesion,
pubmed-meshheading:16461738-Binding Sites,
pubmed-meshheading:16461738-Cell Adhesion Molecules,
pubmed-meshheading:16461738-Cells, Cultured,
pubmed-meshheading:16461738-Dendritic Cells,
pubmed-meshheading:16461738-Escherichia coli,
pubmed-meshheading:16461738-HeLa Cells,
pubmed-meshheading:16461738-Humans,
pubmed-meshheading:16461738-Lectins, C-Type,
pubmed-meshheading:16461738-Lipopolysaccharides,
pubmed-meshheading:16461738-Mannans,
pubmed-meshheading:16461738-Neisseria gonorrhoeae,
pubmed-meshheading:16461738-Phagocytosis,
pubmed-meshheading:16461738-Receptors, Cell Surface
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pubmed:year |
2006
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pubmed:articleTitle |
DC-SIGN (CD209) recognition of Neisseria gonorrhoeae is circumvented by lipooligosaccharide variation.
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pubmed:affiliation |
Department of Biomedical Sciences, College of Medicine, University of Illinois at Chicago, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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