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Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria
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| Zeitschriftentitel: | Journal of Innate Immunity |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Journal of Innate Immunity, 11, 2019, 4, S. 303-315 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
S. Karger AG
|
| Schlagwörter: |
| author_facet |
Binsker, Ulrike Kohler, Thomas P. Hammerschmidt, Sven Binsker, Ulrike Kohler, Thomas P. Hammerschmidt, Sven |
|---|---|
| author |
Binsker, Ulrike Kohler, Thomas P. Hammerschmidt, Sven |
| spellingShingle |
Binsker, Ulrike Kohler, Thomas P. Hammerschmidt, Sven Journal of Innate Immunity Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria Immunology and Allergy |
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binsker, ulrike |
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Binsker, Ulrike Kohler, Thomas P. Hammerschmidt, Sven 1662-811X 1662-8128 S. Karger AG Immunology and Allergy http://dx.doi.org/10.1159/000496033 <jats:p>A successful colonization of different compartments of the human host requires multifactorial contacts between bacterial surface proteins and host factors. Extracellular matrix proteins and matricellular proteins such as thrombospondin-1 play a pivotal role as adhesive substrates to ensure a strong interaction with pathobionts like the Gram-positive <i>Streptococcus pneumoniae</i> and <i>Staphylococcus aureus.</i> The human glycoprotein thrombospondin-1 is a component of the extracellular matrix and is highly abundant in the bloodstream during bacteremia. Human platelets secrete thrombospondin-1, which is then acquired by invading pathogens to facilitate colonization and immune evasion. Gram-positive bacteria express a broad spectrum of surface-exposed proteins, some of which also recognize thrombospondin-1. This review highlights the importance of thrombospondin-1 as an adhesion substrate to facilitate colonization, and we summarize the variety of thrombospondin-1-binding proteins of <i>S. pneumoniae</i> and <i>S. aureus</i>.</jats:p> Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria Journal of Innate Immunity |
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| title |
Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria |
| title_unstemmed |
Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria |
| title_full |
Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria |
| title_fullStr |
Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria |
| title_full_unstemmed |
Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria |
| title_short |
Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria |
| title_sort |
contribution of human thrombospondin-1 to the pathogenesis of gram-positive bacteria |
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Immunology and Allergy |
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http://dx.doi.org/10.1159/000496033 |
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2019 |
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303-315 |
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<jats:p>A successful colonization of different compartments of the human host requires multifactorial contacts between bacterial surface proteins and host factors. Extracellular matrix proteins and matricellular proteins such as thrombospondin-1 play a pivotal role as adhesive substrates to ensure a strong interaction with pathobionts like the Gram-positive <i>Streptococcus pneumoniae</i> and <i>Staphylococcus aureus.</i> The human glycoprotein thrombospondin-1 is a component of the extracellular matrix and is highly abundant in the bloodstream during bacteremia. Human platelets secrete thrombospondin-1, which is then acquired by invading pathogens to facilitate colonization and immune evasion. Gram-positive bacteria express a broad spectrum of surface-exposed proteins, some of which also recognize thrombospondin-1. This review highlights the importance of thrombospondin-1 as an adhesion substrate to facilitate colonization, and we summarize the variety of thrombospondin-1-binding proteins of <i>S. pneumoniae</i> and <i>S. aureus</i>.</jats:p> |
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| description | <jats:p>A successful colonization of different compartments of the human host requires multifactorial contacts between bacterial surface proteins and host factors. Extracellular matrix proteins and matricellular proteins such as thrombospondin-1 play a pivotal role as adhesive substrates to ensure a strong interaction with pathobionts like the Gram-positive <i>Streptococcus pneumoniae</i> and <i>Staphylococcus aureus.</i> The human glycoprotein thrombospondin-1 is a component of the extracellular matrix and is highly abundant in the bloodstream during bacteremia. Human platelets secrete thrombospondin-1, which is then acquired by invading pathogens to facilitate colonization and immune evasion. Gram-positive bacteria express a broad spectrum of surface-exposed proteins, some of which also recognize thrombospondin-1. This review highlights the importance of thrombospondin-1 as an adhesion substrate to facilitate colonization, and we summarize the variety of thrombospondin-1-binding proteins of <i>S. pneumoniae</i> and <i>S. aureus</i>.</jats:p> |
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| spelling | Binsker, Ulrike Kohler, Thomas P. Hammerschmidt, Sven 1662-811X 1662-8128 S. Karger AG Immunology and Allergy http://dx.doi.org/10.1159/000496033 <jats:p>A successful colonization of different compartments of the human host requires multifactorial contacts between bacterial surface proteins and host factors. Extracellular matrix proteins and matricellular proteins such as thrombospondin-1 play a pivotal role as adhesive substrates to ensure a strong interaction with pathobionts like the Gram-positive <i>Streptococcus pneumoniae</i> and <i>Staphylococcus aureus.</i> The human glycoprotein thrombospondin-1 is a component of the extracellular matrix and is highly abundant in the bloodstream during bacteremia. Human platelets secrete thrombospondin-1, which is then acquired by invading pathogens to facilitate colonization and immune evasion. Gram-positive bacteria express a broad spectrum of surface-exposed proteins, some of which also recognize thrombospondin-1. This review highlights the importance of thrombospondin-1 as an adhesion substrate to facilitate colonization, and we summarize the variety of thrombospondin-1-binding proteins of <i>S. pneumoniae</i> and <i>S. aureus</i>.</jats:p> Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria Journal of Innate Immunity |
| spellingShingle | Binsker, Ulrike, Kohler, Thomas P., Hammerschmidt, Sven, Journal of Innate Immunity, Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria, Immunology and Allergy |
| title | Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria |
| title_full | Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria |
| title_fullStr | Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria |
| title_full_unstemmed | Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria |
| title_short | Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria |
| title_sort | contribution of human thrombospondin-1 to the pathogenesis of gram-positive bacteria |
| title_unstemmed | Contribution of Human Thrombospondin-1 to the Pathogenesis of Gram-Positive Bacteria |
| topic | Immunology and Allergy |
| url | http://dx.doi.org/10.1159/000496033 |