Exploring the pan-surfome of Streptococcus suis: Looking for common protein antigens

Gómez-Gascón, Lídia; Luque, Inmaculada; Olaya-Abril, Alfonso; Jiménez-Munguía, Irene; Orbegozo-Medina, Ricardo A.; Peralbo, Esther; Tarradas, Carmen; Rodríguez-Ortega, Manuel J.

doi:10.1016/j.jprot.2012.07.025

Cited by 31 publications

(36 citation statements)

References 47 publications

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“…Many of these were also identified in a high proportion of adult clinical isolates (22). Our results show the enrichment of LPXTG-cell wall proteins when compared with their predicted figures from the genome, as already demonstrated in previous works for this and other pathogens (20,21,48,49,(51)(52)(53)(54). We decided to include also some cytoplasmic proteins, as for some of them their surface localization and immunogenicity/protective activity, are described, like Eno (55,56) or GAPDH (57).…”

Section: Figsupporting

confidence: 76%

A Pneumococcal Protein Array as a Platform to Discover Serodiagnostic Antigens Against Infection

Olaya-Abril

Jiménez-Munguía

Gómez-Gascón

et al. 2015

Molecular & Cellular Proteomics

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Pneumonia is one of the most common and severe diseases associated with Streptococcus pneumoniae infections in children and adults. Etiological diagnosis of pneumococcal pneumonia in children is generally challenging because of limitations of diagnostic tests and interference with nasopharyngeal colonizing strains. Serological assays have recently gained interest to overcome some problems found with current diagnostic tests in pediatric pneumococcal pneumonia. To provide insight into this field, we have developed a protein array to screen the antibody response to many antigens simultaneously. Proteins were selected by experimental identification from a collection of 24 highly prevalent pediatric clinical isolates in Spain, using a proteomics approach consisting of "shaving" the cell surface with proteases and further LC/ MS/MS analysis. Ninety-five proteins were recombinantly produced and printed on an array. We probed it with a collection of sera from children with pneumococcal pneumonia. From the set of the most seroprevalent antigens, we obtained a clear discriminant response for a group of three proteins (PblB, PulA, and PrtA) in children under 4 years old. We validated the results by ELISA and an immunostrip assay showed the translation to easy-to-use, affordable tests. Thus, the protein array here developed presents a tool for broad use in serodiagnostics. Molecular & Cellular

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Section: Figsupporting

confidence: 76%

A Pneumococcal Protein Array as a Platform to Discover Serodiagnostic Antigens Against Infection

Olaya-Abril

Jiménez-Munguía

Gómez-Gascón

et al. 2015

Molecular & Cellular Proteomics

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“…Several proteomic analyses have been carried out on the pneumococcus, targeting either the membrane fraction [31]–[33] or the cell wall-attached proteins [34], [35], but these biochemical fractionation-based methods have several limitations: they are relatively slow, membrane proteins are not always well resolved in polyacrylamide gels and topology information is lost [19], [36]. The “shaving” approach has become a powerful way to identify the set of surface proteins expressed on a given organism (the “surfome”), most of which are normally highly immunogenic as shown by different immunochemical techniques [15], [16], [37], and provides new candidates that elicit protective activity against infection [38]. We have previously set up this strategy in the pneumococcus [19], showing that the procedure enables to define the “pan-surfome” of a collection of clinical isolates, in order to select common proteins to all or most strains [37], [39].…”

Section: Resultsmentioning

confidence: 99%

“…The “shaving” approach has become a powerful way to identify the set of surface proteins expressed on a given organism (the “surfome”), most of which are normally highly immunogenic as shown by different immunochemical techniques [15], [16], [37], and provides new candidates that elicit protective activity against infection [38]. We have previously set up this strategy in the pneumococcus [19], showing that the procedure enables to define the “pan-surfome” of a collection of clinical isolates, in order to select common proteins to all or most strains [37], [39].…”

Section: Resultsmentioning

confidence: 99%

Identification of Potential New Protein Vaccine Candidates through Pan-Surfomic Analysis of Pneumococcal Clinical Isolates from Adults

et al. 2013

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Purified polysaccharide and conjugate vaccines are widely used for preventing infections in adults and in children against the Gram-positive bacterium Streptococcus pneumoniae, a pathogen responsible for high morbidity and mortality rates, especially in developing countries. However, these polysaccharide-based vaccines have some important limitations, such as being serotype-dependent, being subjected to losing efficacy because of serotype replacement and high manufacturing complexity and cost. It is expected that protein-based vaccines will overcome these issues by conferring a broad coverage independent of serotype and lowering production costs. In this study, we have applied the “shaving” proteomic approach, consisting of the LC/MS/MS analysis of peptides generated by protease treatment of live cells, to a collection of 16 pneumococcal clinical isolates from adults, representing the most prevalent strains circulating in Spain during the last years. The set of unique proteins identified in all the isolates, called “pan-surfome”, consisted of 254 proteins, which included most of the protective protein antigens reported so far. In search of new candidates with vaccine potential, we identified 32 that were present in at least 50% of the clinical isolates analyzed. We selected four of them (Spr0012, Spr0328, Spr0561 and SP670_2141), whose protection capacity has not yet been tested, for assaying immunogenicity in human sera. All of them induced the production of IgM antibodies in infected patients, thus indicating that they could enter the pipeline for vaccine studies. The pan-surfomic approach shows its utility in the discovery of new proteins that can elicit protection against infectious microorganisms.

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“…In 2004, a cell-associated DNase (112 kDa), encoded by the ssnA gene, has been identified in S. suis serotype 2 [15]. The recent pan-surfome analysis performed on S. suis and which concluded that the cell-associated DNase may represent one of the best vaccine candidates has revived the interest for this protein [16]. More specifically, it was found that the S. suis DNase is largely distributed among serotypes, and is highly immunogenic and accessible to antibodies [16].…”

Section: Introductionmentioning

confidence: 99%

“…The recent pan-surfome analysis performed on S. suis and which concluded that the cell-associated DNase may represent one of the best vaccine candidates has revived the interest for this protein [16]. More specifically, it was found that the S. suis DNase is largely distributed among serotypes, and is highly immunogenic and accessible to antibodies [16]. In addition, de Buhr et al [17] recently reported that S. suis DNase is involved in the degradation and escaping of neutrophil extracellular traps.…”

Section: Introductionmentioning

confidence: 99%

Characterization of DNase activity and gene in Streptococcus suis and evidence for a role as virulence factor

et al. 2014

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BackgroundThe Gram-positive bacterium Streptococcus suis serotype 2 is an important swine pathogen and emerging zoonotic agent. Multilocus sequence typing allowed dividing S. suis serotype 2 into sequence types (STs). The three major STs of S. suis serotype 2 from North America are 1 (most virulent), 25 (intermediate virulence) and 28 (less virulent). Although the presence of DNase activity in S. suis has been previously reported, little data is available. The aim of this study was to investigate DNase activity in S. suis according to STs, to characterize the activity and gene, and to provide evidence for a potential role in virulence.ResultsWe showed that ST1 and ST28 strains exhibited DNase activity that was absent in ST25 strains. The lack of activity in ST25 isolates was associated with a 14-bp deletion resulting in a shifted reading frame and a premature stop codon. The DNase of S. suis P1/7 (ST1) was cell-associated and active on linear DNA. A DNase-deficient mutant of S. suis P1/7 was found to be less virulent in an amoeba model. Stimulation of macrophages with the DNase mutant showed a decreased secretion of pro-inflammatory cytokines and matrix metalloproteinase-9 compared to the parental strain.ConclusionsThis study further expands our knowledge of S. suis DNase and its potential role in virulence.

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Exploring the pan-surfome of Streptococcus suis: Looking for common protein antigens

Cited by 31 publications

References 47 publications

A Pneumococcal Protein Array as a Platform to Discover Serodiagnostic Antigens Against Infection

A Pneumococcal Protein Array as a Platform to Discover Serodiagnostic Antigens Against Infection

Identification of Potential New Protein Vaccine Candidates through Pan-Surfomic Analysis of Pneumococcal Clinical Isolates from Adults

Characterization of DNase activity and gene in Streptococcus suis and evidence for a role as virulence factor

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