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Gram-positive three-component antimicrobial peptide-sensing system
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
|---|---|
| Personen und Körperschaften: | , , , , , |
| In: | Proceedings of the National Academy of Sciences, 104, 2007, 22, S. 9469-9474 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
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| Schlagwörter: |
| author_facet |
Li, Min Lai, Yuping Villaruz, Amer E. Cha, David J. Sturdevant, Daniel E. Otto, Michael Li, Min Lai, Yuping Villaruz, Amer E. Cha, David J. Sturdevant, Daniel E. Otto, Michael |
|---|---|
| author |
Li, Min Lai, Yuping Villaruz, Amer E. Cha, David J. Sturdevant, Daniel E. Otto, Michael |
| spellingShingle |
Li, Min Lai, Yuping Villaruz, Amer E. Cha, David J. Sturdevant, Daniel E. Otto, Michael Proceedings of the National Academy of Sciences Gram-positive three-component antimicrobial peptide-sensing system Multidisciplinary |
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li, min |
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Li, Min Lai, Yuping Villaruz, Amer E. Cha, David J. Sturdevant, Daniel E. Otto, Michael 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.0702159104 <jats:p> To survive during colonization or infection of the human body, microorganisms must circumvent mechanisms of innate host defense. Antimicrobial peptides represent a key component of innate host defense, especially in phagocytes and on epithelial surfaces. However, it is not known how the clinically important group of Gram-positive bacteria sense antimicrobial peptides to coordinate a directed defensive response. By determining the genome-wide gene regulatory response to human β-defensin 3 in the nosocomial pathogen <jats:italic>Staphylococcus epidermidis</jats:italic> , we discovered an antimicrobial peptide sensor system that controls major specific resistance mechanisms of Gram-positive bacteria and is unrelated to the Gram-negative PhoP/PhoQ system. It contains a classical two-component signal transducer and an unusual third protein, all of which are indispensable for signal transduction and antimicrobial peptide resistance. Furthermore, our data indicate that a very short, extracellular loop with a high density of negative charges in the sensor protein is responsible for antimicrobial peptide binding and the observed specificity for cationic antimicrobial peptides. Our study shows that Gram-positive bacteria have developed an efficient and unique way of controlling resistance mechanisms to antimicrobial peptides, which may provide a promising target for antimicrobial drug development. </jats:p> Gram-positive three-component antimicrobial peptide-sensing system Proceedings of the National Academy of Sciences |
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| title |
Gram-positive three-component antimicrobial peptide-sensing system |
| title_unstemmed |
Gram-positive three-component antimicrobial peptide-sensing system |
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Gram-positive three-component antimicrobial peptide-sensing system |
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Gram-positive three-component antimicrobial peptide-sensing system |
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Gram-positive three-component antimicrobial peptide-sensing system |
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Gram-positive three-component antimicrobial peptide-sensing system |
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gram-positive three-component antimicrobial peptide-sensing system |
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Multidisciplinary |
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http://dx.doi.org/10.1073/pnas.0702159104 |
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2007 |
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9469-9474 |
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<jats:p>
To survive during colonization or infection of the human body, microorganisms must circumvent mechanisms of innate host defense. Antimicrobial peptides represent a key component of innate host defense, especially in phagocytes and on epithelial surfaces. However, it is not known how the clinically important group of Gram-positive bacteria sense antimicrobial peptides to coordinate a directed defensive response. By determining the genome-wide gene regulatory response to human β-defensin 3 in the nosocomial pathogen
<jats:italic>Staphylococcus epidermidis</jats:italic>
, we discovered an antimicrobial peptide sensor system that controls major specific resistance mechanisms of Gram-positive bacteria and is unrelated to the Gram-negative PhoP/PhoQ system. It contains a classical two-component signal transducer and an unusual third protein, all of which are indispensable for signal transduction and antimicrobial peptide resistance. Furthermore, our data indicate that a very short, extracellular loop with a high density of negative charges in the sensor protein is responsible for antimicrobial peptide binding and the observed specificity for cationic antimicrobial peptides. Our study shows that Gram-positive bacteria have developed an efficient and unique way of controlling resistance mechanisms to antimicrobial peptides, which may provide a promising target for antimicrobial drug development.
</jats:p> |
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| author | Li, Min, Lai, Yuping, Villaruz, Amer E., Cha, David J., Sturdevant, Daniel E., Otto, Michael |
| author_facet | Li, Min, Lai, Yuping, Villaruz, Amer E., Cha, David J., Sturdevant, Daniel E., Otto, Michael, Li, Min, Lai, Yuping, Villaruz, Amer E., Cha, David J., Sturdevant, Daniel E., Otto, Michael |
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| description | <jats:p> To survive during colonization or infection of the human body, microorganisms must circumvent mechanisms of innate host defense. Antimicrobial peptides represent a key component of innate host defense, especially in phagocytes and on epithelial surfaces. However, it is not known how the clinically important group of Gram-positive bacteria sense antimicrobial peptides to coordinate a directed defensive response. By determining the genome-wide gene regulatory response to human β-defensin 3 in the nosocomial pathogen <jats:italic>Staphylococcus epidermidis</jats:italic> , we discovered an antimicrobial peptide sensor system that controls major specific resistance mechanisms of Gram-positive bacteria and is unrelated to the Gram-negative PhoP/PhoQ system. It contains a classical two-component signal transducer and an unusual third protein, all of which are indispensable for signal transduction and antimicrobial peptide resistance. Furthermore, our data indicate that a very short, extracellular loop with a high density of negative charges in the sensor protein is responsible for antimicrobial peptide binding and the observed specificity for cationic antimicrobial peptides. Our study shows that Gram-positive bacteria have developed an efficient and unique way of controlling resistance mechanisms to antimicrobial peptides, which may provide a promising target for antimicrobial drug development. </jats:p> |
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| spelling | Li, Min Lai, Yuping Villaruz, Amer E. Cha, David J. Sturdevant, Daniel E. Otto, Michael 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.0702159104 <jats:p> To survive during colonization or infection of the human body, microorganisms must circumvent mechanisms of innate host defense. Antimicrobial peptides represent a key component of innate host defense, especially in phagocytes and on epithelial surfaces. However, it is not known how the clinically important group of Gram-positive bacteria sense antimicrobial peptides to coordinate a directed defensive response. By determining the genome-wide gene regulatory response to human β-defensin 3 in the nosocomial pathogen <jats:italic>Staphylococcus epidermidis</jats:italic> , we discovered an antimicrobial peptide sensor system that controls major specific resistance mechanisms of Gram-positive bacteria and is unrelated to the Gram-negative PhoP/PhoQ system. It contains a classical two-component signal transducer and an unusual third protein, all of which are indispensable for signal transduction and antimicrobial peptide resistance. Furthermore, our data indicate that a very short, extracellular loop with a high density of negative charges in the sensor protein is responsible for antimicrobial peptide binding and the observed specificity for cationic antimicrobial peptides. Our study shows that Gram-positive bacteria have developed an efficient and unique way of controlling resistance mechanisms to antimicrobial peptides, which may provide a promising target for antimicrobial drug development. </jats:p> Gram-positive three-component antimicrobial peptide-sensing system Proceedings of the National Academy of Sciences |
| spellingShingle | Li, Min, Lai, Yuping, Villaruz, Amer E., Cha, David J., Sturdevant, Daniel E., Otto, Michael, Proceedings of the National Academy of Sciences, Gram-positive three-component antimicrobial peptide-sensing system, Multidisciplinary |
| title | Gram-positive three-component antimicrobial peptide-sensing system |
| title_full | Gram-positive three-component antimicrobial peptide-sensing system |
| title_fullStr | Gram-positive three-component antimicrobial peptide-sensing system |
| title_full_unstemmed | Gram-positive three-component antimicrobial peptide-sensing system |
| title_short | Gram-positive three-component antimicrobial peptide-sensing system |
| title_sort | gram-positive three-component antimicrobial peptide-sensing system |
| title_unstemmed | Gram-positive three-component antimicrobial peptide-sensing system |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.0702159104 |