Dataset Information

Staphylococcus Aureus Surface Protein G is An Immunodominant Protein and a Possible Target in An Anti-Biofilm Drug Development.

ABSTRACT:

Background

Staphylococcus aureus is a Gram-positive bacterium that causes severe illnesses in the human population. The capacity of S. aureus strains to form biofilms on biotic and abiotic surfaces creates serious problems for treatment of hospital infections and has stimulated efforts to develop new means of specific protection or immunotherapy.

Material and methods

We found that rabbit serum raised against crude concentrated S. aureus liquid culture significantly decreased the development of staphylococcal biofilm in vitro. To discover the corresponding staphylococcal antigen, we used mass-spectrometry and molecular cloning and identified three major immunodominant proteins. They included α-haemolysin, serine proteinase SplB and S. aureus surface protein G, known as adhesin SasG.

Results

Although according to literature data, all these proteins represent virulence factors of S. aureus and play diverse and important roles in the pathogenesis of staphylococcal diseases, only SasG can be directly implicated into the biofilm formation because of its surface location on a staphylococcal cell. Indeed, rabbit serum directed against purified recombinant SasG, similar to serum against crude staphylococcal liquid culture, prevented the formation of a biofilm.

Conclusion

SasG can be considered as a target in an anti-biofilm drug development and a component of the vaccine or immunotherapeutic preparations directed against staphylococcal infections in humans.

SUBMITTER: Belyi Y

PROVIDER: S-EPMC5944129 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

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Publications

<i>Staphylococcus Aureus</i> Surface Protein G is An Immunodominant Protein and a Possible Target in An Anti-Biofilm Drug Development.

Belyi Yury Y Rybolovlev Ivan I Polyakov Nikita N Chernikova Alena A Tabakova Irina I Gintsburg Alexandre A

The open microbiology journal 20180430

<h4>Background</h4><i>Staphylococcus aureus</i> is a Gram-positive bacterium that causes severe illnesses in the human population. The capacity of <i>S. aureus</i> strains to form biofilms on biotic and abiotic surfaces creates serious problems for treatment of hospital infections and has stimulated efforts to develop new means of specific protection or immunotherapy.<h4>Material and methods</h4>We found that rabbit serum raised against crude concentrated <i>S. aureus</i> liquid culture signific ...[more]

PMID: 29785216

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Project description:The opportunistic pathogen Staphylococcus aureus has become a major threat for human health and well-being by developing resistance to antibiotics, and by its fast evolution into new lineages that rapidly spread within the healthy human population. This calls for the development of active or passive immunization strategies to prevent or treat acute phase infections. Since no such anti-staphylococcal immunization approaches are available as yet, the present studies were aimed at identifying new leads for their development. For this purpose, we thoroughly profiled the cell surface-exposed staphylococcal proteome by combining two surface shaving approaches. In parallel, non-covalently cell wall-bound proteins were extracted with KSCN and analyzed by gel-free proteomics, and also the exoproteome was analyzed through gel-free proteomics. Lastly, we screened a selection of the identified cell wall-attached proteins for binding of immunoglobulin G from patients that have been challenged with different types of S. aureus over extended periods of time due to chronic wound colonization. The combined results of these analyses highlight particular cell surface-exposed S. aureus proteins with highly immunogenic epitopes as potentially powerful targets for the development of protective anti-staphylococcal immunization strategies. Bioinformatics pipeline: Reduction and alkylation, desalting of the samples, mass spectrometric (MS) analysis and database searches were performed as previously described (PMID: 20662103). The strain-specific uniprot databases were used for the /S. aureus/ strains Newman and USA300, respectively including concatenated reversed databases with 5250 and 5298 entries. Validation of MS/MS-based peptide and protein identifications was performed with Scaffold (version Scaffold_2_04_00, Proteome Software Inc., Portland, OR). Peptide identifications were accepted if they exceeded the specific database search engine thresholds. Sequest identifications required at least deltaCn scores of greater than 0.10 and XCorr scores of greater than 1.9, 2.2, 3.8 and 3.8 for singly, doubly, triply and quadruply charged peptides, respectively. All experiments were conducted in independent triplicates. Peptides were only accepted as identified if they were detected in at least two out of the three replicates per sample set. With these filter parameters no false positive hits were obtained.