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

doi:10.1189/jlb.0405184

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

Microbiology, Immunology & Genetics

Research output: Contribution to journal › Article › peer-review

43 Scopus citations

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 language	English
Pages (from-to)	731-738
Number of pages	8
Journal	Journal of Leukocyte Biology
Volume	79
Issue number	4
DOIs	https://doi.org/10.1189/jlb.0405184
State	Published - Apr 2006

Keywords

CEACAM1 (CD66a)
Dendritic cells
Escherichia coli

Access to Document

10.1189/jlb.0405184

Cite this

@article{f1cda16a63e24dc992e1c9655fb47425,

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 = apr,

doi = "10.1189/jlb.0405184",

language = "English",

volume = "79",

pages = "731--738",

journal = "Journal of Leukocyte Biology",

issn = "0741-5400",

publisher = "Wiley-Blackwell",

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

U2 - 10.1189/jlb.0405184

DO - 10.1189/jlb.0405184

M3 - Article

C2 - 16461738

AN - SCOPUS:33746436758

SN - 0741-5400

VL - 79

SP - 731

EP - 738

JO - Journal of Leukocyte Biology

JF - Journal of Leukocyte Biology

IS - 4

ER -

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

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this