Platelets, Bacterial Adhesins and the Pneumococcus
Systemic infections with pathogenic or facultative pathogenic bacteria are associated with activation and aggregation of platelets leading to thrombocytopenia and activation of the clotting system. Bacterial proteins leading to platelet activation and aggregation have been identified, and while plat...
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MDPI AG
2022-03-01
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Online Access: | https://www.mdpi.com/2073-4409/11/7/1121 |
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author | Kristin Jahn Thomas P. Kohler Lena-Sophie Swiatek Sergej Wiebe Sven Hammerschmidt |
author_facet | Kristin Jahn Thomas P. Kohler Lena-Sophie Swiatek Sergej Wiebe Sven Hammerschmidt |
author_sort | Kristin Jahn |
collection | DOAJ |
description | Systemic infections with pathogenic or facultative pathogenic bacteria are associated with activation and aggregation of platelets leading to thrombocytopenia and activation of the clotting system. Bacterial proteins leading to platelet activation and aggregation have been identified, and while platelet receptors are recognized, induced signal transduction cascades are still often unknown. In addition to proteinaceous adhesins, pathogenic bacteria such as <i>Staphylococcus aureus</i> and <i>Streptococcus pneumoniae</i> also produce toxins such as pneumolysin and alpha-hemolysin. They bind to cellular receptors or form pores, which can result in disturbance of physiological functions of platelets. Here, we discuss the bacteria-platelet interplay in the context of adhesin–receptor interactions and platelet-activating bacterial proteins, with a main emphasis on <i>S. aureus</i> and <i>S. pneumoniae</i>. More importantly, we summarize recent findings of how <i>S. aureus</i> toxins and the pore-forming toxin pneumolysin of <i>S. pneumoniae</i> interfere with platelet function. Finally, the relevance of platelet dysfunction due to killing by toxins and potential treatment interventions protecting platelets against cell death are summarized. |
first_indexed | 2024-03-09T12:01:06Z |
format | Article |
id | doaj.art-d707fbbaa4104095878e9b856f7b6aac |
institution | Directory Open Access Journal |
issn | 2073-4409 |
language | English |
last_indexed | 2024-03-09T12:01:06Z |
publishDate | 2022-03-01 |
publisher | MDPI AG |
record_format | Article |
series | Cells |
spelling | doaj.art-d707fbbaa4104095878e9b856f7b6aac2023-11-30T23:03:46ZengMDPI AGCells2073-44092022-03-01117112110.3390/cells11071121Platelets, Bacterial Adhesins and the PneumococcusKristin Jahn0Thomas P. Kohler1Lena-Sophie Swiatek2Sergej Wiebe3Sven Hammerschmidt4Center for Functional Genomics of Microbes, Department of Molecular Genetics and Infection Biology, Interfaculty Institute for Genetics and Functional Genomics, University of Greifswald, 17489 Greifswald, GermanyCenter for Functional Genomics of Microbes, Department of Molecular Genetics and Infection Biology, Interfaculty Institute for Genetics and Functional Genomics, University of Greifswald, 17489 Greifswald, GermanyCenter for Functional Genomics of Microbes, Department of Molecular Genetics and Infection Biology, Interfaculty Institute for Genetics and Functional Genomics, University of Greifswald, 17489 Greifswald, GermanyCenter for Functional Genomics of Microbes, Department of Molecular Genetics and Infection Biology, Interfaculty Institute for Genetics and Functional Genomics, University of Greifswald, 17489 Greifswald, GermanyCenter for Functional Genomics of Microbes, Department of Molecular Genetics and Infection Biology, Interfaculty Institute for Genetics and Functional Genomics, University of Greifswald, 17489 Greifswald, GermanySystemic infections with pathogenic or facultative pathogenic bacteria are associated with activation and aggregation of platelets leading to thrombocytopenia and activation of the clotting system. Bacterial proteins leading to platelet activation and aggregation have been identified, and while platelet receptors are recognized, induced signal transduction cascades are still often unknown. In addition to proteinaceous adhesins, pathogenic bacteria such as <i>Staphylococcus aureus</i> and <i>Streptococcus pneumoniae</i> also produce toxins such as pneumolysin and alpha-hemolysin. They bind to cellular receptors or form pores, which can result in disturbance of physiological functions of platelets. Here, we discuss the bacteria-platelet interplay in the context of adhesin–receptor interactions and platelet-activating bacterial proteins, with a main emphasis on <i>S. aureus</i> and <i>S. pneumoniae</i>. More importantly, we summarize recent findings of how <i>S. aureus</i> toxins and the pore-forming toxin pneumolysin of <i>S. pneumoniae</i> interfere with platelet function. Finally, the relevance of platelet dysfunction due to killing by toxins and potential treatment interventions protecting platelets against cell death are summarized.https://www.mdpi.com/2073-4409/11/7/1121<i>Streptococcus pneumoniae</i>platelet killingplatelet activationpore formationsurface proteinstoxin |
spellingShingle | Kristin Jahn Thomas P. Kohler Lena-Sophie Swiatek Sergej Wiebe Sven Hammerschmidt Platelets, Bacterial Adhesins and the Pneumococcus Cells <i>Streptococcus pneumoniae</i> platelet killing platelet activation pore formation surface proteins toxin |
title | Platelets, Bacterial Adhesins and the Pneumococcus |
title_full | Platelets, Bacterial Adhesins and the Pneumococcus |
title_fullStr | Platelets, Bacterial Adhesins and the Pneumococcus |
title_full_unstemmed | Platelets, Bacterial Adhesins and the Pneumococcus |
title_short | Platelets, Bacterial Adhesins and the Pneumococcus |
title_sort | platelets bacterial adhesins and the pneumococcus |
topic | <i>Streptococcus pneumoniae</i> platelet killing platelet activation pore formation surface proteins toxin |
url | https://www.mdpi.com/2073-4409/11/7/1121 |
work_keys_str_mv | AT kristinjahn plateletsbacterialadhesinsandthepneumococcus AT thomaspkohler plateletsbacterialadhesinsandthepneumococcus AT lenasophieswiatek plateletsbacterialadhesinsandthepneumococcus AT sergejwiebe plateletsbacterialadhesinsandthepneumococcus AT svenhammerschmidt plateletsbacterialadhesinsandthepneumococcus |