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Translatome and transcriptome profiling of SH-SY5Y cells treated with sublytic doses of staphylococcal alpha-hemolysin

ABSTRACT: Genome-wide analysis of translation has the potential to provide major contributions in understanding the pathophysiology of infection processes, given the complex interplay between pathogens and host cells. Informations about the translational state of mRNAs or the activity of RNA binding proteins and ncRNAs after treatment with sublytic doses of pore forming toxins are completely missing. This study uncovers the reshaping undergoing in the translational control system of the host in response to sublytic doses of staphylococcal α-hemolysin (AHL). Keywords: translatome profiling, polysomal profiling, polysomal RNA, translational control, translational profiling, polysome profiling, post-transcriptional regulation, staphylococcal α-hemolysin, pore forming toxins, PTF.

ORGANISM(S): Homo sapiens

PROVIDER: GSE50652 | GEO | 2015/04/01

SECONDARY ACCESSION(S): PRJNA218202

REPOSITORIES: GEO

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Translatome and transcriptome profiling of SH-SY5Y cells treated with sublytic doses of staphylococcal alpha-hemolysin

Project description:Genome-wide analysis of translation has the potential to provide major contributions in understanding the pathophysiology of infection processes, given the complex interplay between pathogens and host cells. Informations about the translational state of mRNAs or the activity of RNA binding proteins and ncRNAs after treatment with sublytic doses of pore forming toxins are completely missing. This study uncovers the reshaping undergoing in the translational control system of the host in response to sublytic doses of staphylococcal α-hemolysin (AHL). Keywords: translatome profiling, polysomal profiling, polysomal RNA, translational control, translational profiling, polysome profiling, post-transcriptional regulation, staphylococcal α-hemolysin, pore forming toxins, PTF. The comparison between translatome and transcriptome profiling was used to discover mRNA-specific changes of the SH-SY5Y cells transcriptome and translatome in response to sublytic doses of staphylococcal α-hemolysin (AHL). To identify translationally regulated mRNAs, gene expression signals derived from the polysomal mRNA populations were compared by microarrays analysis to those obtained from total RNAs. Polysomal mRNA and total mRNA were isolated from SH-SY5Y cells treated with sublytic doses (3nM) of AHL for 2 hours. Cells lysates were collected from untreated cells (control) and from treated cells. All experiments were run in biological triplicates.

2015-04-01 | E-GEOD-50652 | biostudies-arrayexpress

Translatome and transcriptome profiling of SH-SY5Y cells treated with staphylococcal alpha-hemolysin oligomers

Project description:Genome-wide analysis of translation has the potential to provide major contributions in understanding the pathophysiology of infection processes, given the complex interplay between pathogens and host cells. This study uncovers the reshaping undergoing in the translational control system of the host in response to staphylococcal α-hemolysin oligomers (rAHL). Keywords: translatome profiling, polysomal profiling, polysomal RNA, translational control, translational profiling, polysome profiling, post-transcriptional regulation, staphylococcal α-hemolysin, pore forming toxins, PTF.

2015-04-01 | GSE60543 | GEO

Translatome and transcriptome profiling of SH-SY5Y cells treated with staphylococcal alpha-hemolysin oligomers

Project description:Genome-wide analysis of translation has the potential to provide major contributions in understanding the pathophysiology of infection processes, given the complex interplay between pathogens and host cells. This study uncovers the reshaping undergoing in the translational control system of the host in response to staphylococcal α-hemolysin oligomers (rAHL). Keywords: translatome profiling, polysomal profiling, polysomal RNA, translational control, translational profiling, polysome profiling, post-transcriptional regulation, staphylococcal α-hemolysin, pore forming toxins, PTF. The comparison between translatome and transcriptome profiling was used to discover mRNA-specific changes of the SH-SY5Y cells transcriptome and translatome in response to staphylococcal α-hemolysin oligomers (rAHL). To identify translationally regulated mRNAs, gene expression signals derived from the polysomal mRNA populations were compared by microarrays analysis to those obtained from total RNAs. Polysomal mRNA and total mRNA were isolated from SH-SY5Y cells treated with 3nM of extracted oligomers (rAHL) for 2 hours. Cells lysates were collected from untreated cells (control) and from treated cells. All experiments were run in biological triplicates.

2015-04-01 | E-GEOD-60543 | biostudies-arrayexpress

Host Response Signature to Staphylococcus aureus alpha-Hemolysin

Project description:Staphylococcus aureus pneumonia causes significant morbidity and mortality. Alpha-hemolysin (Hla), a pore-forming cytotoxin of S. aureus, has been identified through animal models of pneumonia as a critical virulence factor that induces lung injury. In spite of considerable molecular knowledge of how this cytotoxin injures the host, the precise host response to Hla in the context of infection remains poorly understood. We employed whole-genome expression profiling of infected lung to define the host response to wild-type S. aureus compared with an Hla-deficient isogenic mutant in experimental pneumonia. These data provide a complete expression profile at four and at twenty-four hours post-infection, revealing a unique response to the toxin-expressing strain. Gene ontogeny analysis revealed significant differences in the extracellular matrix and cardiomyopathy pathways, both of which govern cellular interactions in the tissue microenvironment. Evaluation of individual transcript responses to Hla-secreting bacteria was notable for upregulation of host cytokine and chemokine genes, including the p19 subunit of interleukin-23. Consistent with this observation, the cellular immune response to infection was characterized by a prominent TH17 response to wild-type staphylococci. These findings define specific host mRNA responses to Hla-producing S. aureus, coupling the pulmonary TH17 response to the presence of this cytotoxin. Expression profiling to define the host response to a single virulence factor proved to be a valuable tool in identifying pathways for further investigation in S. aureus pneumonia. This approach may be broadly applicable to the study of bacterial toxins, defining host pathways that can be targeted to mitigate toxin-induced disease. Animals were treated with PBS, S. aureus wild-type, or S. aureus Hla-deficient isogenic mutant.

2012-05-20 | E-GEOD-38053 | biostudies-arrayexpress

Host Response Signature to Staphylococcus aureus alpha-Hemolysin

2012-05-21 | GSE38053 | GEO

Residues 1 to 563 of α-hemolysin alone form a fully functional pore and their proper membrane insertion depends on the acylation status of the molecule

Project description:The acylated pore-forming Repeats in ToXin (RTX) cytolysins α-hemolysin (HlyA) and adenylate cyclase toxin (CyaA) bind primarily to β2 integrins of leukocytes. HlyA binds the common CD18 subunit of the β2 integrins and CyaA selectively binds the CD11b subunit of complement receptor 3 (CR3). However, both toxins can also bind and permeabilize membranes of a variety of nonmyeloid cells. We constructed HlyA1-563/CyaA860-1706 hybrid molecules activated by the CyaA-activating acyltransferase CyaC, or by the HlyA-activating acyltransferase HlyC. We show that the C-terminal portion of the HlyA molecule, comprising the acylated segment and the RTX domain (residues 564 to 1024), can be functionally swapped with the CyaC-activated acylated segment bearing palmitoylated Lys983 and the much larger RTX domain of CyaA. Compared to the CD18-interacting HlyA, the CR3-interacting HlyA1-563/CyaA860-1706 hybrid exhibited a selectively reduced cytotoxicity on human THP-1 monocytes and Chinese hamster ovary (CHO) cells expressing CR3 (CHO-CR3) or lymphocyte function-associated antigen 1 (CHO-LFA1). However, the mono-palmitoylated HlyA1-563/CyaA860-1706 hybrid remained fully hemolytic and cytolytic toward erythrocytes and mock-transfected CHO cells and exhibited a comparable membrane activity on artificial planar lipid membranes as the bi-myristoylated HlyA. Thus, regardless of the length or number of the attached fatty acyl chains, the CyaC-activated HlyA1-563/CyaA860-1706 hybrid and the intact HlyA were comparably active on cells or artificial membranes lacking β2 integrins. These data suggest that once the hydrophobic pore-forming domain comprising N-terminal half of HlyA is brought into close contact with the cell membrane by the mono-palmitoylated acylated segment of CyaA, it can efficiently form fully cytolytic HlyA-like membrane pores.

2024-03-25 | PXD046160 | Pride

Homo sapiens

Project description:Translatome and transcriptome profiling of SH-SY5Y cells treated with sublytic doses of staphylococcal alpha-hemolysin

| PRJNA218202 | ENA

Pore-forming toxin alpha-hemolysin efficiently improve the immunogenicity and protective efficacy of protein antigens by increasing antigen uptake and targeting ADAM10

Project description:Pore-forming toxin alpha-hemolysin efficiently improve the immunogenicity and protective efficacy of protein antigens by increasing antigen uptake and targeting ADAM10

| PRJNA702922 | ENA

Effect of V. cholerae biofilm formation and hemolysin production on human macrophages

Project description:In this study we determined the gene expression of THP-1 derived macrophages during the interaction with V. cholerae wildtype cells, biofilm-deficient or hemolysin-deficient mutants.

2023-05-11 | GSE184077 | GEO

Comparison of S. aureus PVL-positive and PVL-negative isogenic strains in exponential and stationary phase of growth

Project description:The Staphylococcus aureus Panton Valentine leukocidin (PVL) is a pore-forming toxin secreted by strains epidemiologically associated with the current outbreak of community-associated methicillin-resistant Staphylococcus aureus (CA-MRSA) and with the often lethal necrotizing pneumonia. To investigate the role of PVL in pulmonary disease, we tested the pathogenicity of clinical isolates, isogenic PVL-negative and PVL-positive S. aureus strains, as well as purified PVL, in a mouse acute pneumonia model. Here we show that PVL is sufficient to cause pneumonia and that the expression of this leukotoxin induces global changes in transcriptional levels of genes encoding secreted and cell-wall-anchored staphylococcal proteins, including the lung inflammatory factor staphylococcal protein A (Spa). Keywords: comparative transcription profile in the presence or absence of PVL toxin

2007-02-13 | GSE6985 | GEO

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