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- W1497492892 abstract "Antimicrobial peptides (AMPs) form a crucial part of human innate host defense, especially in neutrophil phagosomes and on epithelial surfaces. Bacteria have a variety of efficient resistance mechanisms to human AMPs, such as efflux pumps, secreted proteases, and alterations of the bacterial cell surface that are aimed to minimize attraction of the typically cationic AMPs. In addition, bacteria have specific sensors that activate AMP resistance mechanisms when AMPs are present. The prototypical Gram-negative PhoP/PhoQ and the Gram-positive Aps AMP-sensing systems were first described and investigated in Salmonella typhimurium and Staphylococcus epidermidis, respectively. Both include a classical bacterial two-component sensor/regulator system, but show many structural, mechanistic, and functional differences. The PhoP/PhoQ regulon controls a variety of genes not necessarily limited to AMP resistance mechanisms, but apparently aimed to combat innate host defense on a broad scale. In contrast, the staphylococcal Aps system predominantly upregulates AMP resistance mechanisms, namely the D-alanylation of teichoic acids, inclusion of lysyl-phosphati-dylglycerol in the cytoplasmic membrane, and expression of the putative VraFG AMP efflux pump. Notably, both systems are crucial for virulence and represent possible targets for antimicrobial therapy." @default.
- W1497492892 created "2016-06-24" @default.
- W1497492892 creator A5056173398 @default.
- W1497492892 date "2009-01-01" @default.
- W1497492892 modified "2023-10-11" @default.
- W1497492892 title "Bacterial Sensing of Antimicrobial Peptides" @default.
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- W1497492892 doi "https://doi.org/10.1159/000219377" @default.
- W1497492892 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2777530" @default.
- W1497492892 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19494583" @default.
- W1497492892 hasPublicationYear "2009" @default.
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