Eintrag weiter verarbeiten
Gram-positive three-component antimicrobial peptide-sensing system
Gespeichert in:
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
|
Schlagwörter: |
Zusammenfassung: | <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> |
---|---|
Umfang: | 9469-9474 |
ISSN: |
0027-8424
1091-6490 |
DOI: | 10.1073/pnas.0702159104 |