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Several carcinoembryonic antigens (CD66) serve as receptors for gonococcal opacity proteins.

Chen T, Grunert F, Medina-Marino A, Gotschlich EC - J. Exp. Med. (1997)

Bottom Line: This conclusion was based on the following observations.We also compared the adherence and invasion by Opa+ bacteria of CD66 transfected HeLa cells: HeLa-BGPa, HeLa-CGM6, HeLa-NCA, HeLa-CGM1a, HeLa-CEA, and HeLa-Neo serving as negative control.Among the Opa proteins tested, OpaC proved to be bifunctional, able to mediate adherence to both syndecan receptors and to CD66 antigens.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, NY 10021-6399, USA.

ABSTRACT
Neisseria gonorrhoeae (GC) is a human pathogen that adheres to and invades genital surfaces. Although pili are required for the initial adherence, the interaction of GC with epithelial cells is also promoted by a family of outer membrane proteins, the opacity (Opa) proteins such as OpaA protein from strain MS11. Studies have demonstrated that the interaction of the OpaA GC with epithelial cells involves binding to heparan sulfate attached to syndecan receptors. However, other Opa proteins interact with CEA gene family member 1 (CGM1) or biliary glycoprotein (BGP), members of the CD66 antigen family. In this study, we demonstrate that, in addition, the 180-kD carcinoembryonic antigen (CEA) is a receptor for Opa proteins. This conclusion was based on the following observations. First, transfected HeLa cells expressing CEA (HeLa-CEA) and the CEA-expressing colon cancer cell line (LS 174T) bound and subsequently engulfed the Opa+ bacteria. These interactions were inhibited by anti-CEA antibody, but could not be inhibited by addition of heparin. Furthermore, OpaI E. coli directly bound purified CEA. We also compared the adherence and invasion by Opa+ bacteria of CD66 transfected HeLa cells: HeLa-BGPa, HeLa-CGM6, HeLa-NCA, HeLa-CGM1a, HeLa-CEA, and HeLa-Neo serving as negative control. Using OpaI as the prototype, the relative ability of the transfected HeLa cell lines to support adherence was (CEA = BGPa >CGM1a >NCA >CGM6 = Neo). The ability to mediate invasion of the transfectant cells was (CGM1a >CEA >BGPa >NCA >CGM6 = Neo). Among the Opa proteins tested, OpaC proved to be bifunctional, able to mediate adherence to both syndecan receptors and to CD66 antigens.

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Electron micrographs of internalization of OpaI E. coli and  GC by HeLa-CEA and LS 174T. The micrographs demonstrate the ability of HeLa-CEA to internalize OpaI E. coli (A) and OpaI GC (B). CEAexpressing colon cancer cells (LS 174T) were also able to engulf OpaI E.  coli (C) and OpaI GC (D). The engulfment of OpaI CG by HeLaCGM1a (E) served as a positive control. Bar, 1 μm.
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Figure 2: Electron micrographs of internalization of OpaI E. coli and GC by HeLa-CEA and LS 174T. The micrographs demonstrate the ability of HeLa-CEA to internalize OpaI E. coli (A) and OpaI GC (B). CEAexpressing colon cancer cells (LS 174T) were also able to engulf OpaI E. coli (C) and OpaI GC (D). The engulfment of OpaI CG by HeLaCGM1a (E) served as a positive control. Bar, 1 μm.

Mentions: The ability of these cell lines to promote invasion showed a different pattern. Although the adherence of pEXI to HeLa-BGPa was high, invasion was limited (Fig. 1 B). Electron microscopy demonstrated that HeLa-CEA cells were also able to engulf pEXI (Fig. 1 B) and OpaI GC (Fig. 2). However, compared to HeLa-CGM1a (Fig. 1 B, 2E), HeLaCEA cells demonstrated lower ability to internalize pEXI or OpaI GC (Figs. 1 B and 2 B). Virtually all HeLaCGM1a cells contained large numbers of GC, but a lower degree of cellular invasion by OpaI bacteria was observed with HeLa-CEA cells. HeLa-NCA and HeLa-CGM6 were hardly invaded at all.


Several carcinoembryonic antigens (CD66) serve as receptors for gonococcal opacity proteins.

Chen T, Grunert F, Medina-Marino A, Gotschlich EC - J. Exp. Med. (1997)

Electron micrographs of internalization of OpaI E. coli and  GC by HeLa-CEA and LS 174T. The micrographs demonstrate the ability of HeLa-CEA to internalize OpaI E. coli (A) and OpaI GC (B). CEAexpressing colon cancer cells (LS 174T) were also able to engulf OpaI E.  coli (C) and OpaI GC (D). The engulfment of OpaI CG by HeLaCGM1a (E) served as a positive control. Bar, 1 μm.
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Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2196295&req=5

Figure 2: Electron micrographs of internalization of OpaI E. coli and GC by HeLa-CEA and LS 174T. The micrographs demonstrate the ability of HeLa-CEA to internalize OpaI E. coli (A) and OpaI GC (B). CEAexpressing colon cancer cells (LS 174T) were also able to engulf OpaI E. coli (C) and OpaI GC (D). The engulfment of OpaI CG by HeLaCGM1a (E) served as a positive control. Bar, 1 μm.
Mentions: The ability of these cell lines to promote invasion showed a different pattern. Although the adherence of pEXI to HeLa-BGPa was high, invasion was limited (Fig. 1 B). Electron microscopy demonstrated that HeLa-CEA cells were also able to engulf pEXI (Fig. 1 B) and OpaI GC (Fig. 2). However, compared to HeLa-CGM1a (Fig. 1 B, 2E), HeLaCEA cells demonstrated lower ability to internalize pEXI or OpaI GC (Figs. 1 B and 2 B). Virtually all HeLaCGM1a cells contained large numbers of GC, but a lower degree of cellular invasion by OpaI bacteria was observed with HeLa-CEA cells. HeLa-NCA and HeLa-CGM6 were hardly invaded at all.

Bottom Line: This conclusion was based on the following observations.We also compared the adherence and invasion by Opa+ bacteria of CD66 transfected HeLa cells: HeLa-BGPa, HeLa-CGM6, HeLa-NCA, HeLa-CGM1a, HeLa-CEA, and HeLa-Neo serving as negative control.Among the Opa proteins tested, OpaC proved to be bifunctional, able to mediate adherence to both syndecan receptors and to CD66 antigens.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, NY 10021-6399, USA.

ABSTRACT
Neisseria gonorrhoeae (GC) is a human pathogen that adheres to and invades genital surfaces. Although pili are required for the initial adherence, the interaction of GC with epithelial cells is also promoted by a family of outer membrane proteins, the opacity (Opa) proteins such as OpaA protein from strain MS11. Studies have demonstrated that the interaction of the OpaA GC with epithelial cells involves binding to heparan sulfate attached to syndecan receptors. However, other Opa proteins interact with CEA gene family member 1 (CGM1) or biliary glycoprotein (BGP), members of the CD66 antigen family. In this study, we demonstrate that, in addition, the 180-kD carcinoembryonic antigen (CEA) is a receptor for Opa proteins. This conclusion was based on the following observations. First, transfected HeLa cells expressing CEA (HeLa-CEA) and the CEA-expressing colon cancer cell line (LS 174T) bound and subsequently engulfed the Opa+ bacteria. These interactions were inhibited by anti-CEA antibody, but could not be inhibited by addition of heparin. Furthermore, OpaI E. coli directly bound purified CEA. We also compared the adherence and invasion by Opa+ bacteria of CD66 transfected HeLa cells: HeLa-BGPa, HeLa-CGM6, HeLa-NCA, HeLa-CGM1a, HeLa-CEA, and HeLa-Neo serving as negative control. Using OpaI as the prototype, the relative ability of the transfected HeLa cell lines to support adherence was (CEA = BGPa >CGM1a >NCA >CGM6 = Neo). The ability to mediate invasion of the transfectant cells was (CGM1a >CEA >BGPa >NCA >CGM6 = Neo). Among the Opa proteins tested, OpaC proved to be bifunctional, able to mediate adherence to both syndecan receptors and to CD66 antigens.

Show MeSH
Related in: MedlinePlus