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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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Multiple Opa proteins promote adherence to  HeLa-CEA. pGEM, pEXA,  pEXB, pEXC, pEXH, and pEXI  were incubated with HeLaCEA (A) for 4 h. All of Opa+ E.  coli adhered to the cell lines. (B)  Addition of COL-1 antibody  (CD66) inhibited adherence of  OpaI and OpaC E. coli to HeLaCEA. Control antibody IB4  (CD18) had no effect when  added at the same final concentration (25 μg/ml). The interaction of pEXI and pEXC with  HeLa-CEA was for 2 h and only  accounted for the lower bacterial  counts.
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Figure 4: Multiple Opa proteins promote adherence to HeLa-CEA. pGEM, pEXA, pEXB, pEXC, pEXH, and pEXI were incubated with HeLaCEA (A) for 4 h. All of Opa+ E. coli adhered to the cell lines. (B) Addition of COL-1 antibody (CD66) inhibited adherence of OpaI and OpaC E. coli to HeLaCEA. Control antibody IB4 (CD18) had no effect when added at the same final concentration (25 μg/ml). The interaction of pEXI and pEXC with HeLa-CEA was for 2 h and only accounted for the lower bacterial counts.

Mentions: Since strain MS11 can express several Opa proteins, we examined whether other Opa proteins possess the same function, as illustrated in Fig. 4 A. HeLa-CEA cells also bound OpaA, OpaB, OpaC, and OpaH E. coli with similar efficiency, but only OpaA-mediated adherence was strongly inhibited by soluble heparin. The adherence mediated by OpaI and OpaC was inhibited by anti-CEA antibody (COL-1), but not by IB4 directed to CD18 antigen (Fig. 4 B). These results demonstrate that CEA antigen serves as receptor for several Opa proteins.


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

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

Multiple Opa proteins promote adherence to  HeLa-CEA. pGEM, pEXA,  pEXB, pEXC, pEXH, and pEXI  were incubated with HeLaCEA (A) for 4 h. All of Opa+ E.  coli adhered to the cell lines. (B)  Addition of COL-1 antibody  (CD66) inhibited adherence of  OpaI and OpaC E. coli to HeLaCEA. Control antibody IB4  (CD18) had no effect when  added at the same final concentration (25 μg/ml). The interaction of pEXI and pEXC with  HeLa-CEA was for 2 h and only  accounted for the lower bacterial  counts.
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Related In: Results  -  Collection

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

Figure 4: Multiple Opa proteins promote adherence to HeLa-CEA. pGEM, pEXA, pEXB, pEXC, pEXH, and pEXI were incubated with HeLaCEA (A) for 4 h. All of Opa+ E. coli adhered to the cell lines. (B) Addition of COL-1 antibody (CD66) inhibited adherence of OpaI and OpaC E. coli to HeLaCEA. Control antibody IB4 (CD18) had no effect when added at the same final concentration (25 μg/ml). The interaction of pEXI and pEXC with HeLa-CEA was for 2 h and only accounted for the lower bacterial counts.
Mentions: Since strain MS11 can express several Opa proteins, we examined whether other Opa proteins possess the same function, as illustrated in Fig. 4 A. HeLa-CEA cells also bound OpaA, OpaB, OpaC, and OpaH E. coli with similar efficiency, but only OpaA-mediated adherence was strongly inhibited by soluble heparin. The adherence mediated by OpaI and OpaC was inhibited by anti-CEA antibody (COL-1), but not by IB4 directed to CD18 antigen (Fig. 4 B). These results demonstrate that CEA antigen serves as receptor for several Opa proteins.

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