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From the * Laboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York,
10021-6399; and the 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 (HeLaCEA) 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.
Institute of Immunobiology, University of Freiburg, Freiburg D-79104, Germany
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