Heat shock response ofStreptococcus pneumoniae: identification of immunoreactive stress proteins

Hamel, Josée; Martin, Denis; Brodeur, Bernard B.

doi:10.1006/mpat.1996.0124

Cited by 24 publications

(39 citation statements)

References 49 publications

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“…is in good agreement with previous data (14) and the data deduced from the DNA sequences of the dnaK locus of L. lactis (2) and S. pneumoniae (21). The partial N-terminal amino acid sequence of p65 (S-K-E-I-K-F-S-SDARSAMVRGVDI)showed 75% amino acid homology through its partial length with L. lactis (20), 70% with B. subtilis (23), and 50% with E. coli GroEL (16).…”

supporting

confidence: 91%

“…S. pneumoniae is carried in the nasopharynx of healthy contact carriers who constitute the major reservoir for pneumococcal infections and is subject to a number of environmental stresses in normal and infection processes. In S. pneumoniae, three HSPs were detected after heat shock (8,14) and a 104-kDa HSP was detected after ethanol shock (8). Also, the 72-kDa HSP was found to be a member of the DnaK family (14, 21) and a major immunogen (14).…”

mentioning

confidence: 99%

“…In S. pneumoniae, three HSPs were detected after heat shock (8,14) and a 104-kDa HSP was detected after ethanol shock (8). Also, the 72-kDa HSP was found to be a member of the DnaK family (14, 21) and a major immunogen (14). However, the effect of various stresses and/or clinical conditions on S. pneumoniae remains unclear, and other HSPs were not identified.…”

mentioning

confidence: 99%

“…Although 4 HSPs, 65-, 73-, 84-, and 104-kDa proteins (p65, p73, p84, and p104, respectively), were detected upon heat or ethanol shock, low molecular weight HSPs were not readily discernable and appeared not to be the major HSPs in pneumococcus (8,14). Therefore, we pursued only these 4 HSPs further.…”

mentioning

confidence: 99%

“…Once HSPs are induced, they may help challenge hostile environments and play some role in the host as antigen(s) and/or virulence factors. Recently, the major HSP, p73, a DnaK homologue, was found to be a major immunogen (14). Therefore, it is quite interesting to determine whether HSPs play a role in pathogenesis and virulence.…”

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confidence: 99%

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Limited Stress Response in Streptococcus pneumoniae

Choi

Shim

Kim

et al. 1999

Microbiology and Immunology

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In Streptococcus pneumoniae, heat shock induces the synthesis of 65-, 73-, and 84-kDa proteins, and ethanol shock induces a 104-kDa protein. In this study, the 65-, 84-, and 104-kDa proteins were identified as members of the GroEL, CIpL and alcohol dehydrogenase families, respectively, and the general properties of the stress response of S. pneumoniae to several other stresses were characterized. However, several stresses which are known to induce stress responses in Escherichia coli and Bacillus subtilis failed to induce any high molecular weight heat-shock proteins (HSPs) such as GroEL and DnaK homologues. A minor temperature shift from 30 to 37 C triggered induction of the homologues of DnaK and GroEL of E. coli. These features may provide a foundation for evaluating the role of heat-shock proteins relative to the physiology and pathogenesis of pneumococcus.

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supporting

confidence: 91%

mentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Limited Stress Response in Streptococcus pneumoniae

Choi

Shim

Kim

et al. 1999

Microbiology and Immunology

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Identification of chromosomally encoded membranal polypeptides of Bacillus anthracis by a proteomic analysis: Prevalence of proteins containing S‐layer homology domains

et al. 2004

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Bacillus anthracis is the causative agent of anthrax disease. Improvement of existing anthrax vaccines, which are currently based on the administration of Protective Antigen (the highly immunogenic nontoxic subunit of the bacterial toxin) may entail other bacterial immunogenic elements, part of which are predicted to reside on the surface of bacterial cells. In the present study, membranal proteins extracted from a stationary-phase culture of a nonvirulent B. anthracis strain, devoid of the native virulence plasmids pXO1 and pXO2, were separated by two-dimensional electrophoresis (2-DE) and a characteristic protein map was defined. The proteomic analysis allowed matrix-assisted laser desorption/ionization-time of flight mass spectrometry-assisted identification of 86 protein spots which represent the product of 30 individual open reading frames (ORF). Among these, a prevalent class of proteins was the S-layer proteins (which were found to represent more than 75% of the B. anthracis membranal fraction) and proteins containing S-layer homology (SLH)-membranal localization domains. Five novel SLH proteins, previously inferred only from bioinformatic ORF analysis (draft genome sequence), were identified and one was shown to be a highly abundant membranal protein. Western blots of the 2-DE gels were probed with sera from convalescent rabbits and guinea pigs infected with virulent B. anthracis (Vollum strain). This analysis revealed that B. anthracis immune animals exhibit antibodies against at least 14 distinct membranal proteins present in the 2-DE map, establishing that these proteins are expressed in vivo and are able to elicit an immune response. The identification of the protein components of the B. anthracis membranal fraction, as well as the establishment of their potential immunogenicity, underscore the strength of the proteomic approach for identifying molecules which may serve for further analysis of immune and protective abilities.

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Quantitative analysis of Streptococcus pneumoniae TIGR4 response to in vitro iron restriction by 2‐D LC ESI MS/MS

et al. 2008

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Understanding the growth of bacterial pathogens in a micronutrient restricted host environment can identify potential virulence proteins that help overcome this nutritional barrier to productive infection. In this study, we investigated the pneumococcal protein expression response to iron limitation using an in vitro model. We identified S. pneumoniae TIGR4 proteins by 2-D LC ESI MS/MS and determined significant changes in protein expression in response to iron restriction using computer-intensive random resampling methods. Differential protein expression was studied in the context of a S. pneumoniae TIGR4 protein interaction network using Pathway Studio. Our analysis showed that pneumococcal iron restriction response was marked by increased expression of known virulence factors like PsaA. It involved changes in the expression of stress response, and phase variation and biofilm formation proteins. The net effect of changes in all these biological processes could increase the virulence of S. pneumoniae TIGR4 during in vivo infection.

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Heat shock response ofStreptococcus pneumoniae: identification of immunoreactive stress proteins

Cited by 24 publications

References 49 publications

Limited Stress Response in Streptococcus pneumoniae

Limited Stress Response in Streptococcus pneumoniae

Identification of chromosomally encoded membranal polypeptides of Bacillus anthracis by a proteomic analysis: Prevalence of proteins containing S‐layer homology domains

Quantitative analysis of Streptococcus pneumoniae TIGR4 response to in vitro iron restriction by 2‐D LC ESI MS/MS

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