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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):

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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Project description:Staphylococcus aureus is a pathogen which can cause a wide range of infections. To find new targets for diagnostics and treatment as well as understanding host-pathogen interactions, many studies have focused on the bacterial surface proteins. In the study presented here, bacterial cell surface-shaving, using Lipid-based Protein Immobilization (LPI), followed by tandem mass tag (TMT) protocols for performing relative quantitative mass spectrometry proteomics, was performed to examine the surface proteome (surfaceome) of selected strains of S. aureus. The study included analyses of surface protein-deficient mutants compared to the wildtype S. aureus strain Newman, as well strain isolates of different clinical associations. Quantitative proteomics were applied in the analysis of the surface proteome of Staphylococcus aureus. In study 1, the differential abundance of proteins in the mutant strains ΔClfA, ΔSrtAΔSrtB and ΔSpa was compared to those in the Newman parental strain. All together 7880 peptides were identified in Study 1 corresponding to 1290 proteins, and the results clearly showed that the mutant strains were deficient in the knocked-out genes. The Clinical strains study (Study 2) included the Newman strain, the reference strains LS-1 and SH1000 and three clinical isolates, two from invasive infections and one from mild skin infection. A total of 4949 peptides were identified in Study 2 corresponding to 919 proteins. For each strain, approximately 20 proteins showed higher or lower abundance (fold changes) when compared to the Newman strain. The results indicate that surface shaving of intact bacteria by LPI in combination with protocols for performing quantitative proteomics makes it possible to distinguish differences in protein abundance of the surfaceome, including virulence factors, between S. aureus strains.

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

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