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J. Biol. Chem., Vol. 276, Issue 26, 24331-24340, June 29, 2001
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From the Neisseria gonorrhoeae express
opacity-associated (Opa) protein adhesins that mediate binding to
various members of the carcinoembryonic antigen-related cellular
adhesion molecule (CEACAM; previously CD66) receptor family.
Although human umbilical vein endothelial cells express little CEACAM
receptor in vitro, we found neisserial infection to induce
expression of CEACAM1, CEACAM1-3L, and CECAM1-4L splice
variants. This mediates an increased
Opa52-dependent binding of gonococci by these
cells. The induced receptor expression did not require bacterial Opa
expression, but it was more rapid with adherent bacteria. Because the
time course of induction was similar to that seen for induced
proinflammatory cytokines, we tested whether CEACAM1 expression could
be controlled by a similar mechanism. Gonococcal infection activated a
nuclear factor-
Pathogenic Neisseria Trigger Expression of Their
Carcinoembryonic Antigen-related Cellular Adhesion Molecule 1 (CEACAM1;
Previously CD66a) Receptor on Primary Endothelial Cells by Activating
the Immediate Early Response Transcription Factor, Nuclear
Factor-
B*
§,
§¶, and
**
Max-Planck-Institut für Biologie,
Abteilung Infektionsbiologie, Spemannstrasse 34, 72076 Tübingen,
the § Max-Planck-Institut für Infektionsbiologie,
Abteilung Molekulare Biologie, Schumannstrasse 21/22, Berlin (Mitte)
D-10117, Germany, and the
Department of Medical Genetics and
Microbiology, University of Toronto, Toronto M5S 1A8, Canada.
B (NF-
B) heterodimer consisting of p50 and p65,
and inhibitors that prevent the nuclear translocation of activated
NF-
B complex inhibited CEACAM1 transcript expression. Each of these
effects could be mimicked by using culture filtrates or purified
lipopolysaccharide instead of intact bacteria. Together, our results
support a model whereby the outer membrane "blebs" that are
actively released by gonococci trigger a Toll-like receptor-4-dependent activation of NF-
B, which
up-regulates the expression of CEACAM1 to allow
Opa52-mediated neisserial binding. The regulation of
CEACAM1 expression by NF-
B also implies a broader role for this
receptor in the general inflammatory response to infection.
*
This study was supported in part by Deutsche
Forschungsgemeinschaft Grants Me705/5-1 and Na292/5-2 and by the Fonds
der Chemischen Industrie.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.
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