Transcriptomics,Multiomics

Dataset Information

3

The antimicrobial peptide-sensing system aps of Staphylococcus aureus


ABSTRACT: Staphylococcus aureus is a leading cause of hospital-associated infections. In addition, highly virulent strains of methicillin-resistant S. aureus (MRSA) are currently spreading outside health care settings. Survival in the human host is largely defined by the ability of S. aureus to resist mechanisms of innate host defense, of which antimicrobial peptides form a key part especially on epithelia and in neutrophil phagosomes. Here we demonstrate that the antimicrobial-peptide sensing system aps of the standard community-associated MRSA strain MW2 controls resistance to cationic antimicrobial peptides. The core of aps-controlled resistance mechanisms comprised the D-alanylation of teichoic acids (dlt operon), the incorporation of cationic lysyl-phosphatidylglycerol (L-PG) in the bacterial membrane (mprF), and the vraF/vraG putative antimicrobial peptide transporter. Further, the observed increased production of L-PG under the influence of cationic antimicrobial peptides was accompanied by the up-regulation of lysine biosynthesis. In noticeable difference to the aps system of S. epidermidis, only selected antimicrobial peptides strongly induced the aps response. Heterologous complementation with the S. epidermidis apsS gene indicated that this is likely caused by differences in the short extracellular loop of ApsS that interacts with the inducing antimicrobial peptide. Our study shows that the antimicrobial peptide sensor system aps is functional in the important human pathogen S. aureus, significant interspecies differences exist in the induction of the aps gene regulatory response, and aps inducibility is clearly distinguishable from effectiveness towards a given antimicrobial peptide. Keywords: Wild type control vs treated vs mutant Wild type untreated in triplicate is compared to wild type treated in triplicate along with three mutants in triplicate with and without treatment of indolicidin, totalling 30 samples

OTHER RELATED OMICS DATASETS IN: PRJNA101451

ORGANISM(S): Staphylococcus Aureus

SUBMITTER: Michael Otto   Yuping Lai  Min Li  Dan Sturdevant  Amer E Villaruz  Daniel E Sturdevant 

PROVIDER: E-GEOD-8400 | ArrayExpress | 2008-04-06

SECONDARY ACCESSION(S): GSE8400PRJNA101451

REPOSITORIES: GEO, ArrayExpress

Dataset's files

Source:
Action DRS
E-GEOD-8400.README.txt Txt
E-GEOD-8400.eSet.r Other
E-GEOD-8400.idf.txt Idf
E-GEOD-8400.processed.1.zip Processed
E-GEOD-8400.raw.1.zip Raw
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Publications

The antimicrobial peptide-sensing system aps of Staphylococcus aureus.

Li Min M   Cha David J DJ   Lai Yuping Y   Villaruz Amer E AE   Sturdevant Daniel E DE   Otto Michael M  

Molecular microbiology 20071024 5


Staphylococcus aureus is a leading cause of hospital-associated and, more recently, community-associated infections caused by highly virulent methicillin-resistant strains (CA-MRSA). S. aureus survival in the human host is largely defined by the ability to evade attacks by antimicrobial peptides (AMPs) and other mechanisms of innate host defence. Here we show that AMPs induce resistance mechanisms in CA-MRSA via the aps AMP sensor/regulator system, including (i) the d-alanylation of teichoic aci  ...[more]

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