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Originally published In Press as doi:10.1074/jbc.M108135200 on December 19, 2001

J. Biol. Chem., Vol. 277, Issue 9, 7438-7446, March 1, 2002
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Nuclear Factor-kappa B Directs Carcinoembryonic Antigen-related Cellular Adhesion Molecule 1 Receptor Expression in Neisseria gonorrhoeae-infected Epithelial Cells*

Petra Muenzner, Oliver Billker, Thomas F. MeyerDagger , and Michael Naumann

From the Max-Planck-Institute of Infection Biology, Department of Molecular Biology, Schumannstrasse 21/22, Berlin 10117, Germany

The human-specific pathogen Neisseria gonorrhoeae expresses opacity-associated (Opa) protein adhesins that bind to various members of the carcinoembryonic antigen-related cellular adhesion molecule (CEACAM) family. In this study, we have analyzed the mechanism underlying N. gonorrhoeae-induced CEACAM up-regulation in epithelial cells. Epithelial cells represent the first barrier for the microbial pathogen. We therefore characterized CEACAM expression in primary human ovarian surface epithelial (HOSE) cells and found that CEACAM1-3 (L, S) and CEACAM1-4 (L, S) splice variants mediate an increased Opa52-dependent gonoccocal binding to HOSE cells. Up-regulation of these CEACAM molecules in HOSE cells is a direct process that takes place within 2 h postinfection and depends on close contact between microbial pathogen and HOSE cells. N. gonorrhoeae-triggered CEACAM1 up-regulation involves activation of the transcription factor nuclear factor kappa B (NF-kappa B), which translocates as a p50/p65 heterodimer into the nucleus, and an NF-kappa B-specific inhibitory peptide inhibited CEACAM1-receptor up-regulation in N. gonorrhoeae-infected HOSE cells. Bacterial lipopolysaccharides did not induce NF-kappa B and CEACAM up-regulation, which corresponds to our findings that HOSE cells do not express toll-like receptor 4. The ability of N. gonorrhoeae to up-regulate its epithelial receptor CEACAM1 through NF-kappa B suggests an important mechanism allowing efficient bacterial colonization during the initial infection process.

* This work was supported in part by Deutsche Forschungsgemeinschaft Grant Me705/5-1 and the Fonds der Chemischen Industrie and by a European Molecular Biology Organization long term fellowship (to O. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 49-30-284-60- 402; Fax: 49-30-28460-401; E-mail: meyer@mpiib-berlin.mpg.de.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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