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Papers In Press, published online ahead of print December 19, 2001
Molekulare Biologie, Max-Planck-Institut für Infektionsbiologie, Berlin 10117
Corresponding Author: naumann{at}mpiib-berlin.mpg.de
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 upregulation 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. Upregulation of these CEACAM molecules in HOSE cells is a direct process that takes place within 2 h post infection and depends on close contact between microbial pathogen and HOSE cells. N. gonorrhoeae-triggered CEACAM1 upregulation involves activation of the transcription factor nuclear factor kB (NF-kB), which translocates as a p50/p65 heterodimer into the nucleus, and an NF-kB-specific inhibitory peptide inhibited CEACAM1-receptor upregulation in N. gonorrhoeae-infected HOSE cells. Bacterial lipopolysaccharides (LPS) did not induce NF-kB and CEACAM upregulation, which corresponds to our results that HOSE cells do not express toll-like receptor 4 (TLR4). The ability of N. gonorrhoeae to upregulate its epithelial receptor CEACAM1 through NF-kB suggests an important mechanism allowing efficient bacterial colonization during the initial infection process.
J. Biol. Chem, 10.1074/jbc.M108135200
Submitted on August 23, 2001
Revised on December 19, 2001
Accepted on December 19, 2001
Nuclear factor-kB directs CEACAM1 receptor expression in Neisseria gonorrhoeae-infected epithelial cells
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