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Proteomic study of Staphylococcus haemolyticus after the host-microbe co-colonisation

ABSTRACT: In this study, the adhesive and biofilm forming properties of ten clinical and ten commensal S. haemolyticus isolates were examined using standard adhesion and biofilm assays, in addition we selected one clinical S. haemolyticus isolate for bacterial surface shaving. The surface shaving approach was used to identify upregulated S. haemolyticus proteins subsequent to human keratinocyte colonization. Relative quantification of up and downregulated proteins was performed by labelling proteins with tandem mass tags (TMT), prior to Mass Spectrometry analysis.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Staphylococcus Haemolyticus

SUBMITTER: Sahlgrenska Academy Proteomics Core

LAB HEAD: Roger Karlsson

PROVIDER: PXD014450 | Pride | 2020-05-26

REPOSITORIES: Pride

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			Action	DRS
	2838_PD1.4.msf	Msf
	QEHF_180226_15.raw	Raw
	QEHF_180226_16.raw	Raw
	QEHF_180226_17.raw	Raw
	QEHF_180226_18.raw	Raw

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Publications

Identification of surface proteins in a clinical Staphylococcus haemolyticus isolate by bacterial surface shaving.

Wolden Runa R Pain Maria M Karlsson Roger R Karlsson Anders A Aarag Fredheim Elizabeth G EG Cavanagh Jorunn Pauline JP

BMC microbiology 20200407 1

<h4>Background</h4>The skin commensal Staphylococcus haemolyticus is an emerging nosocomial pathogen. Despite its clinical relevance, published information about S. haemolyticus virulence factors is scarce. In this study, the adhesive and biofilm forming properties of ten clinical and ten commensal S. haemolyticus strains were examined using standard adhesion and biofilm assays. One of the clinical strains was used to identify expressed surface proteins using bacterial surface shaving. Protein a ...[more]

PMID: 32264835

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Proteomic analysis of anti-MRSA activity of caerin 1.1/1.9 in a murine skin infection model

Project description:Caerin 1 is a family of host-defense peptides with antimicrobial property originally isolated from Australia tree frog. Caerin 1.1+1.9 has been shown to inhibit multiple antibiotic resistant bacteria infection both in vitro and in vivo. In current study, we compare the MICs of caerin 1.1/1.9 with commonly used antibiotics against S. aureus, Copper-Green Pseudomonas aeruginosa, Acinetobacter baumannii, and Streptococcus haemolyticus. We demonstrate that caerin 1.1/1.9 not only prevent the formation of biofilm by A. Baumann, but also have therapeutic effect on established biofilm. In addition, we find that caerin1.1/1.9 significantly inhibit the growth of methicillin-resistant Staphylococcus aureus (MRSA) strain in a murine skin infection model. The quantitative proteomic analysis suggested that caerin1.1/1.9 largely activate oxidative phosphorylation, as well as several pathways associated with tissue repair and growth, with respect to the untreated tissues infected with MRSA in mice. In summary, our results suggest that caerin 1.1/1.9 have the potential to be used as a drug candidate treating complicated antibiotic resistant bacterial infection in human.

2023-10-11 | PXD044425 | Pride

Within-host adaptive phenotypic responses of bovine Staphylococcus aureus

Project description:The Gram-positive bacterium S. aureus is one of the most common causes of contagious bovine mastitis. A predominant S. aureus clone persists within its host over a long period. In the present study, we compared the surface proteome of two isolates, collected from a naturally infected dairy cow with chronic, subclinical mastitis: an initial isolate (IN) and a host-adapted strain (HA). The isolates were grown under iron- and oxygen-limiting conditions in RPMI 1640 medium. Bacterial cells were isolated at the early stationary phase and used for preparation of surface-associated proteins by applying a surface-shaving and a surface-biotinylation approach. Proteins were identified by gelfree (surface-shaving approach) and GeLC-MS/MS (biotinylation approach) analyses.

2021-08-14 | PXD025013 | Pride

Secreted Factors from Staphylococcus aureus Biofilm and Planktonic Cultures Differentially Impact Human Keratinocytes, in vitro

Project description:Interactions between human keratinocytes and secreted factors from Staphylococcus aureus biofilm and planktonic cultures were investigated using microarray analysis. Relative to planktonic secreted factors, biofilm secreted factors up regulated cytokine and chemokine genes in keratinocytes. Genes associated with DNA damage and oxidative stress were also induced in keratinocytes treated with secreted factors from S. aureus biofilm. Here we show that secreted factors from S. aureus planktonic (PCM) and biofilm (BCM) cultures differentially impact several aspects of wound healing processes. Secreted factors from S. aureus biofilm and planktonic cultures with equivalent population sizes were placed in contact with human foreskin keratinocytes for 4 hours. Keratinocytes were grown to ~90% confluency between passages 4-10.

2011-08-30 | E-GEOD-24118 | biostudies-arrayexpress

Comparative exoproteome profiling of an invasive and a commensal Staphylococcus haemolyticus isolate

Project description:Staphylococcus haemolyticus is a skin commensal emerging as an opportunistic pathogen. Nosocomial isolates of S. haemolyticus are the most antibiotic resistant members of the coagulase negative staphylococci (CoNS), but information about other S.haemolyticus virulence factors is scarce. Bacterial virulence is mediated by membrane vesicles (MVs) which enable secretion and long distance delivery of bacterial effector molecules while protecting the cargo from proteolytic degradation from the environment. We wanted to determine if the MV protein cargo of S.haemolyticus is strain specific and enriched in certain MV associated proteins compared to the totalsecretome. The present study shows that both clinical and commensal S. haemolyticus isolates produce membrane vesicles. The MV cargo of both strains was enriched in proteins involved in adhesion and in acquisition of iron. The MV cargo of the clinical strain was further enriched in antimicrobial resistance proteins.

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Preeclampsia causes sex-specific transcriptional and proteomic changes in foetal erythroid cells

Project description:Preeclampsia (PE) has been associated with placental dysfunction, resulting in foetal hypoxia, accelerated erythropoiesis and increased erythroblast count in the umbilical cord blood (UCB). Although the detailed effects remain unknown, placental dysfunction can also cause inflammation, nutritional and oxidative stress in the fetus that can affect erythropoiesis. Here, we compared the expression of surface adhesion molecules and erythroid differentiation capacity of UCB hematopoietic stem/ progenitor cells (HSPCs), UCB erythroid profiles along with transcriptome and proteome of these cells between male and female foetuses from PE and normotensive pregnancies. While no significant differences were observed in UCB HSPC migration/ homing and in vitro erythroid colony differentiation, the UCB HSPC transcriptome and the proteomic profile of the in vitro differentiated erythroid cells differed between PE vs normotensive samples. Accordingly, despite absence of significant differences in the UCB erythroid populations in male or female foetuses from PE or normotensive pregnancies, transcriptional changes were observed during erythropoiesis, particularly affecting male foetuses. Pathway analysis suggested deregulation in mTORC1/AMPK signaling pathways controlling cell cycle, differentiation and protein synthesis. These results associate PE with transcriptional and proteomic changes in foetal HSPCs and erythroid cells that may underlie the higher erythroblast count in the UCB in PE.

2019-06-20 | PXD010364 | Pride

Growth condition-dependent cell surface proteome analysis of Enterococcus faecium

Project description:Using a proteolytic shaving approach we identified differentially expressed surface exposed proteins of E. faecium cells after growth in different conditions.

2015-07-07 | MSV000079184 | MassIVE

Surface proteome of Lactobacillus casei GCRL163 under heat adaptation – LiCl Sucrose

Project description:Cell surface proteins are constantly impacted by environmental stresses. To understand the impact of heat adaptation on the Lactobacillus casei GCRL163, trypsin shaving technique was used to extract the surface proteins of the strain and the protein fraction obtained analysed using gel-free proteomics.

2022-03-01 | PXD009591 | Pride

Surface proteome of Lactobacillus casei GCRL163 under heat adaptation – extracellular fluid

2022-03-01 | PXD009638 | Pride

Surface proteome of Lactobacillus casei GCRL163 under heat adaptation

Project description:Cell surface proteins are constatntly impacted by environmental stresses. To understand the imapct of heat adaptation on the Lactobacillus casei GCRL163, trypsin shaving technique was used to extract the surface proteins of the strain and the protein fraction obtained analysed using gel-free proteomics.

2022-03-01 | PXD009468 | Pride

Characterization of the surfaceome of the metal-reducing bacterium Desulfotomaculum reducens

Project description:Desulfotomaculum reducens strain MI-1 is a Gram-positive, sulfate-reducing bacterium also capable of reducing Fe(III). Metal reduction in Gram-positive bacteria is poorly understood. Here, we investigated Fe(III) reduction with lactate, a non-fermentable substrate, as the electron donor. Lactate consumption is concomitant to Fe(III) reduction, but does not support significant growth, suggesting that little energy can be conserved from this process and that it may occur fortuitously. D. reducens can reduce both soluble (Fe(III)-citrate) and insoluble (hydrous ferric oxide, HFO) Fe(III). Because physically inaccessible HFO was not reduced, we concluded that reduction requires direct contact under these experimental conditions. This implies the presence of a surface exposed reductase capable of transferring electrons from the cell to the extracellular electron acceptor. With the goal of identifying candidate Fe(III) reductases, we carried out an investigation of the surface proteome (surfaceome) of D. reducens. Cell surface exposed proteins were extracted by trypsin cell shaving or by lysozyme treatment, and analyzed by liquid chromatography-tandem mass spectrometry.

2014-07-31 | PXD001072 | Pride

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