Identification of Sphingomyelinase on the Surface of Chlamydia pneumoniae: Possible Role in the Entry into Its Host Cells
We have recently suggested a novel mechanism, autoendocytosis, for the entry of certain microbes into their hosts, with a key role played by the sphingomyelinase-catalyzed topical conversion of sphingomyelin to ceramide, the differences in the biophysical properties of these two lipids providing the...
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| Format: | Article |
| Language: | English |
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Wiley
2014-01-01
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| Series: | Interdisciplinary Perspectives on Infectious Diseases |
| Online Access: | http://dx.doi.org/10.1155/2014/412827 |
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| author | Tuula A. Peñate Medina Juha T. Korhonen Riitta Lahesmaa Mirja Puolakkainen Oula Peñate Medina Paavo K. J. Kinnunen |
| author_facet | Tuula A. Peñate Medina Juha T. Korhonen Riitta Lahesmaa Mirja Puolakkainen Oula Peñate Medina Paavo K. J. Kinnunen |
| author_sort | Tuula A. Peñate Medina |
| collection | DOAJ |
| description | We have recently suggested a novel mechanism, autoendocytosis, for the entry of certain microbes into their hosts, with a key role played by the sphingomyelinase-catalyzed topical conversion of sphingomyelin to ceramide, the differences in the biophysical properties of these two lipids providing the driving force. The only requirement for such microbes to utilize this mechanism is that they should have a catalytically active SMase on their outer surface while the target cells should expose sphingomyelin in the external leaflet of their plasma membrane. In pursuit of possible microbial candidates, which could utilize this putative mechanism, we conducted a sequence similarity search for SMase. Because of the intriguing cellular and biochemical characteristics of the poorly understood entry of Chlamydia into its host cells these microbes were of particular interest. SMase activity was measured in vitro from isolated C. pneumoniae elementary bodies (EB) and in the lysate from E. coli cells transfected with a plasmid expressing CPn0300 protein having sequence similarity to SMase. Finally, pretreatment of host cells with exogenous SMase resulting in loss plasma membrane sphingomyelin attenuated attachment of EB. |
| format | Article |
| id | doaj-art-175cc59f0b91497580ffced9c2cb4a19 |
| institution | Kabale University |
| issn | 1687-708X 1687-7098 |
| language | English |
| publishDate | 2014-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Interdisciplinary Perspectives on Infectious Diseases |
| spelling | doaj-art-175cc59f0b91497580ffced9c2cb4a192025-02-03T05:47:58ZengWileyInterdisciplinary Perspectives on Infectious Diseases1687-708X1687-70982014-01-01201410.1155/2014/412827412827Identification of Sphingomyelinase on the Surface of Chlamydia pneumoniae: Possible Role in the Entry into Its Host CellsTuula A. Peñate Medina0Juha T. Korhonen1Riitta Lahesmaa2Mirja Puolakkainen3Oula Peñate Medina4Paavo K. J. Kinnunen5Helsinki Biophysics & Biomembrane Group, Medical Biochemistry, Institute of Biomedicine, University of Helsinki, 00014 Helsinki, FinlandTurku Centre for Biotechnology, 20520 Turku, FinlandTurku Centre for Biotechnology, 20520 Turku, FinlandHUSLAB, Department of Virology, Haartman Institute, University of Helsinki, 00014 Helsinki, FinlandHelsinki Biophysics & Biomembrane Group, Medical Biochemistry, Institute of Biomedicine, University of Helsinki, 00014 Helsinki, FinlandHelsinki Biophysics & Biomembrane Group, Medical Biochemistry, Institute of Biomedicine, University of Helsinki, 00014 Helsinki, FinlandWe have recently suggested a novel mechanism, autoendocytosis, for the entry of certain microbes into their hosts, with a key role played by the sphingomyelinase-catalyzed topical conversion of sphingomyelin to ceramide, the differences in the biophysical properties of these two lipids providing the driving force. The only requirement for such microbes to utilize this mechanism is that they should have a catalytically active SMase on their outer surface while the target cells should expose sphingomyelin in the external leaflet of their plasma membrane. In pursuit of possible microbial candidates, which could utilize this putative mechanism, we conducted a sequence similarity search for SMase. Because of the intriguing cellular and biochemical characteristics of the poorly understood entry of Chlamydia into its host cells these microbes were of particular interest. SMase activity was measured in vitro from isolated C. pneumoniae elementary bodies (EB) and in the lysate from E. coli cells transfected with a plasmid expressing CPn0300 protein having sequence similarity to SMase. Finally, pretreatment of host cells with exogenous SMase resulting in loss plasma membrane sphingomyelin attenuated attachment of EB.http://dx.doi.org/10.1155/2014/412827 |
| spellingShingle | Tuula A. Peñate Medina Juha T. Korhonen Riitta Lahesmaa Mirja Puolakkainen Oula Peñate Medina Paavo K. J. Kinnunen Identification of Sphingomyelinase on the Surface of Chlamydia pneumoniae: Possible Role in the Entry into Its Host Cells Interdisciplinary Perspectives on Infectious Diseases |
| title | Identification of Sphingomyelinase on the Surface of Chlamydia pneumoniae: Possible Role in the Entry into Its Host Cells |
| title_full | Identification of Sphingomyelinase on the Surface of Chlamydia pneumoniae: Possible Role in the Entry into Its Host Cells |
| title_fullStr | Identification of Sphingomyelinase on the Surface of Chlamydia pneumoniae: Possible Role in the Entry into Its Host Cells |
| title_full_unstemmed | Identification of Sphingomyelinase on the Surface of Chlamydia pneumoniae: Possible Role in the Entry into Its Host Cells |
| title_short | Identification of Sphingomyelinase on the Surface of Chlamydia pneumoniae: Possible Role in the Entry into Its Host Cells |
| title_sort | identification of sphingomyelinase on the surface of chlamydia pneumoniae possible role in the entry into its host cells |
| url | http://dx.doi.org/10.1155/2014/412827 |
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