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Papers In Press, published online ahead of print April 16, 2001
Molekulare Biologie, Max-Planck-Institut für Infektionsbiologie, Berlin 10117
Corresponding Author: naumann{at}mpiib-berlin.mpg.de
Neisseria gonorrhoeae express Opa protein adhesins that mediate binding to various members of the CEACAM (previously CD66) receptor family. Although human umbilical vein endothelial cells (HUVECs) express little CEACAM receptor in vitro, we found neisserial infection to induce expression of CEACAM1-3L and CEACAM-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 was more rapid with adherent bacteria. Since the time course of induction was similar to that seen for induced pro-inflammatory cytokines, we tested whether CEACAM1 expression could be controlled by a similar mechanism. Gonococcal infection activated a NF-kB heterodimer consisting of p50 and p65, and inhibitors that prevent the nuclear translocation of activated NF-kB complex inhibited CEACAM1 transcript expression. Each of these effects could be mimicked by using culture filtrates or purified LPS instead of intact bacteria. Together, our results support a model whereby the outer membrane "blebs" that are actively released by gonococci trigger a TLR-4-dependent activation of NF-kB, which up-regulates the expression of CEACAM1 to allow Opa52-mediated neisserial binding. The regulation of CEACAM1 expression by NF-kB also implies a broader role for this receptor in the general inflammatory response to infection.
J. Biol. Chem, 10.1074/jbc.M006883200
Submitted on August 1, 2000
Revised on April 16, 2001
Accepted on April 16, 2001
Pathogenic Neisseria trigger expression of their CEACAM1 (CD66a) receptor on primary endothelial cells by activating the immediate early response transcription factor NF-kappaB
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