DC-SIGN (CD209) recognition of Neisseria gonorrhoeae is circumvented by lipooligosaccharide variation

Pei Zhang, Olivier Schwartz, Milica Pantelic, Geling Li, Quita Knazze, Cinzia Nobile, Milan Radovich, Johnny He, Soon Cheol Hong, John Klena, Tie Chen

Research output: Contribution to journalArticle

31 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)731-738
Number of pages8
JournalJournal of Leukocyte Biology
Volume79
Issue number4
DOIs
StatePublished - Apr 2006

Fingerprint

Neisseria gonorrhoeae
Dendritic Cells
Phagocytosis
Escherichia coli
Cytophagocytosis
Carcinoembryonic Antigen
Cell Adhesion Molecules
lipid-linked oligosaccharides
HeLa Cells
Bacteria
Antibodies

Keywords

  • CEACAM1 (CD66a)
  • Dendritic cells
  • Escherichia coli

ASJC Scopus subject areas

  • Cell Biology

Cite this

Zhang, P., Schwartz, O., Pantelic, M., Li, G., Knazze, Q., Nobile, C., ... Chen, T. (2006). DC-SIGN (CD209) recognition of Neisseria gonorrhoeae is circumvented by lipooligosaccharide variation. Journal of Leukocyte Biology, 79(4), 731-738. https://doi.org/10.1189/jlb.0405184

DC-SIGN (CD209) recognition of Neisseria gonorrhoeae is circumvented by lipooligosaccharide variation. / Zhang, Pei; Schwartz, Olivier; Pantelic, Milica; Li, Geling; Knazze, Quita; Nobile, Cinzia; Radovich, Milan; He, Johnny; Hong, Soon Cheol; Klena, John; Chen, Tie.

In: Journal of Leukocyte Biology, Vol. 79, No. 4, 04.2006, p. 731-738.

Research output: Contribution to journalArticle

Zhang, P, Schwartz, O, Pantelic, M, Li, G, Knazze, Q, Nobile, C, Radovich, M, He, J, Hong, SC, Klena, J & Chen, T 2006, 'DC-SIGN (CD209) recognition of Neisseria gonorrhoeae is circumvented by lipooligosaccharide variation', Journal of Leukocyte Biology, vol. 79, no. 4, pp. 731-738. https://doi.org/10.1189/jlb.0405184
Zhang, Pei ; Schwartz, Olivier ; Pantelic, Milica ; Li, Geling ; Knazze, Quita ; Nobile, Cinzia ; Radovich, Milan ; He, Johnny ; Hong, Soon Cheol ; Klena, John ; Chen, Tie. / DC-SIGN (CD209) recognition of Neisseria gonorrhoeae is circumvented by lipooligosaccharide variation. In: Journal of Leukocyte Biology. 2006 ; Vol. 79, No. 4. pp. 731-738.
@article{b20eef842ea7485aafe4e563b26f1ec6,
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.",
keywords = "CEACAM1 (CD66a), Dendritic cells, Escherichia coli",
author = "Pei Zhang and Olivier Schwartz and Milica Pantelic and Geling Li and Quita Knazze and Cinzia Nobile and Milan Radovich and Johnny He and Hong, {Soon Cheol} and John Klena and Tie Chen",
year = "2006",
month = "4",
doi = "10.1189/jlb.0405184",
language = "English",
volume = "79",
pages = "731--738",
journal = "Journal of Leukocyte Biology",
issn = "0741-5400",
publisher = "FASEB",
number = "4",

}

TY - JOUR

T1 - DC-SIGN (CD209) recognition of Neisseria gonorrhoeae is circumvented by lipooligosaccharide variation

AU - Zhang, Pei

AU - Schwartz, Olivier

AU - Pantelic, Milica

AU - Li, Geling

AU - Knazze, Quita

AU - Nobile, Cinzia

AU - Radovich, Milan

AU - He, Johnny

AU - Hong, Soon Cheol

AU - Klena, John

AU - Chen, Tie

PY - 2006/4

Y1 - 2006/4

N2 - 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.

AB - 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.

KW - CEACAM1 (CD66a)

KW - Dendritic cells

KW - Escherichia coli

UR - http://www.scopus.com/inward/record.url?scp=33746436758&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33746436758&partnerID=8YFLogxK

U2 - 10.1189/jlb.0405184

DO - 10.1189/jlb.0405184

M3 - Article

C2 - 16461738

AN - SCOPUS:33746436758

VL - 79

SP - 731

EP - 738

JO - Journal of Leukocyte Biology

JF - Journal of Leukocyte Biology

SN - 0741-5400

IS - 4

ER -