Acid sphingomyelinase is involved in CEACAM receptor-mediated phagocytosis of Neisseria gonorrhoeae Export

@article{citeulike:3177461, abstract = {The interaction with human phagocytes is a hallmark of symptomatic Neisseria gonorrhoeae infections. Gonococcal outer membrane proteins of the Opa family induce the opsonin-independent uptake of the bacteria that relies on CEACAM receptors and an active signaling machinery of the phagocyte. Here, we show that CEACAM receptor-mediated phagocytosis of Opa52-expressing N. gonorrhoeae into human cells results in a rapid activation of the acid sphingomyelinase. Inhibition of this enzyme by imipramine or SR33557 abolishes opsonin-independent internalization without affecting bacterial adherence. Reconstitution of ceramide, the product of acid sphingomyelinase activity, in imipramine- or SR33557-treated cells restores internalization of the bacteria. Furthermore, we demonstrate that CEACAM receptor-initiated stimulation of other signalling molecules, in particular Src-like tyrosine kinases and Jun N-terminal kinases, requires acid sphingomyelinase. These studies provide evidence for a crucial role of the acid sphingomyelinase for CEACAM receptor-initiated signalling events and internalization of Opa52-expressing N. gonorrhoeae into human neutrophils.}, author = {Hauck, C. R. and Grassm\'{e}, H. and Bock, J. and Jendrossek, V. and Ferlinz, K. and Meyer, T. F. and Gulbins, E.}, citeulike-article-id = {3177461}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/S0014-5793(00)01851-2}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6T36-40VSJTF-C/2/934fa088163e0147b28b61e4634eb3c5}, day = {4}, doi = {10.1016/S0014-5793(00)01851-2}, journal = {FEBS Letters}, keywords = {acid, ceacam, gonorrhoeae, sphingomyelin, sphingomyelinase}, month = {August}, number = {3}, pages = {260--266}, posted-at = {2008-09-01 05:41:46}, priority = {2}, title = {Acid sphingomyelinase is involved in CEACAM receptor-mediated phagocytosis of Neisseria gonorrhoeae}, url = {http://dx.doi.org/10.1016/S0014-5793(00)01851-2}, volume = {478}, year = {2000} }

TY - JOUR ID - citeulike:3177461 L3 - citeulike-article-id:3177461 N2 - The interaction with human phagocytes is a hallmark of symptomatic Neisseria gonorrhoeae infections. Gonococcal outer membrane proteins of the Opa family induce the opsonin-independent uptake of the bacteria that relies on CEACAM receptors and an active signaling machinery of the phagocyte. Here, we show that CEACAM receptor-mediated phagocytosis of Opa52-expressing N. gonorrhoeae into human cells results in a rapid activation of the acid sphingomyelinase. Inhibition of this enzyme by imipramine or SR33557 abolishes opsonin-independent internalization without affecting bacterial adherence. Reconstitution of ceramide, the product of acid sphingomyelinase activity, in imipramine- or SR33557-treated cells restores internalization of the bacteria. Furthermore, we demonstrate that CEACAM receptor-initiated stimulation of other signalling molecules, in particular Src-like tyrosine kinases and Jun N-terminal kinases, requires acid sphingomyelinase. These studies provide evidence for a crucial role of the acid sphingomyelinase for CEACAM receptor-initiated signalling events and internalization of Opa52-expressing N. gonorrhoeae into human neutrophils. IS - 3 JF - FEBS Letters EP - 266 TI - Acid sphingomyelinase is involved in CEACAM receptor-mediated phagocytosis of Neisseria gonorrhoeae VL - 478 SP - 260 KW - acid KW - ceacam KW - gonorrhoeae KW - sphingomyelin KW - sphingomyelinase AU - Hauck, CR AU - Grassmé, H AU - Bock, J AU - Jendrossek, V AU - Ferlinz, K AU - Meyer, TF AU - Gulbins, E PY - 2000/08/04/ UR - http://dx.doi.org/10.1016/S0014-5793(00)01851-2 ER -