U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

SRX21202517: GSM7670365: LAC_ΔcamS_rep3; Staphylococcus aureus; RNA-Seq
1 ILLUMINA (Illumina NovaSeq 6000) run: 59.5M spots, 18G bases, 5.5Gb downloads

External Id: GSM7670365_r1
Submitted by: Genetics and Genome Biology, University of Leicester
Study: The Staphylococcus aureus CamS lipoprotein is a repressor of toxin production that shapes host-pathogen interaction
show Abstracthide Abstract
Lipoproteins of the opportunistic pathogen Staphylococcus aureus play a crucial role in various cellular processes and host interactions. Consisting of a protein and a lipid moiety, they support nutrient acquisition and anchor the protein to the bacterial membrane. Recently, we identified several processed and secreted small linear peptides that derive from the secretion signal sequence of S. aureus lipoproteins. Here, we show for the first time, that the protein moiety of the S. aureus lipoprotein CamS has a biological role that is distinct from its associated linear peptide staph-cAM373. The small peptide was shown to be involved in interspecies horizontal gene transfer, the primary mechanism for the dissemination of antibiotic resistance among bacteria. We provide evidence that the CamS protein moiety is a potent repressor of cytotoxins, such as a-toxin and leukocidins. The CamS-mediated suppression of toxin transcription was reflected by altered disease severity in in vivo infection models involving skin and soft tissue, as well as bloodstream infections. Collectively, we have uncovered the role of the protein moiety of the staphylococcal lipoprotein CamS as a previously uncharacterized repressor of S. aureus toxin production, which consequently regulates virulence and disease outcomes. Notably, the camS gene is conserved in S. aureus, and we also demonstrated the muted transcriptional response of cytotoxins in another S. aureus lineage. Our findings provide the first evidence of distinct biological functions of the protein moiety and its associated linear peptide for a specific lipoprotein. Therefore, lipoproteins in S. aureus consist of three functional components: a lipid moiety, a protein moiety, and a small linear peptide, with putative different biological roles that might not only determine the outcome of host-pathogen interactions but also drive the acquisition of antibiotic resistance determinants. Overall design: RNA sequencing of S. aureus LAC wild type, mutant and complemented strains to determine differences in their gene expression profiles.
Sample: LAC_ΔcamS_rep3
SAMN36776090 • SRS18460368 • All experiments • All runs
Library:
Name: GSM7670365
Instrument: Illumina NovaSeq 6000
Strategy: RNA-Seq
Source: TRANSCRIPTOMIC
Selection: cDNA
Layout: PAIRED
Construction protocol: RNA was extracted using a RNeasy Mini Kit with the following modifications. Cells were lysed by incubation with 100 mM TRIS-HCL with 800 ng/µl lysostaphin for 25 min at 37 °C. Subsequently, 700 µl RLT buffer containing β-mercaptoethanol were added and samples were transferred to lysing matrix B tubes and the samples were subjected to three bead beating steps (30 sec x 3; 1 min on ice in between). RNA was treated with turbo DNAse kit according to manufacturers instructions. Depletion of ribosomal RNA and library preparations were performed at the Genomics Core at the University of Colorado Anschutz Medical Campus using the Illumina Ribo-ZeroTm Plus rRNA depletion kit and the Zymo-Seq RiboFree total RNA library kit.
Runs: 1 run, 59.5M spots, 18G bases, 5.5Gb
Run# of Spots# of BasesSizePublished
SRR2546987359,496,19918G5.5Gb2023-11-20

ID:
28638839

Supplemental Content

Search details

See more...

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...