PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Streptococcus pneumoniae”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 55 records · Page 3Linked to original sources
PubMed2004

rexAB mutants in Streptococcus pneumoniae.

Streptococcus pneumoniae is a human pathogen that is naturally transformable. In this study a major component of the homologous recombination pathway, the RexAB exonuclease/helicase, was characterized. rexA and rexB insertional mutants were constructed using mariner mutagenesis and found to have identical phenotypes. Both rexAB mutants displayed poor cell viability, reduced double-strand exonuclease activity, UV sensitivity and a reduced level of gene conversion compared to the wild-type strain. No effect was observed on plasmid and chromosomal transformation efficiencies. These results indicate that in S. pneumoniae, RexAB is required for DNA repair, but not for chromosomal transformation and plasmid establishment.

DNA Helicases↗
PubMed1999

Transformation of a type 4 encapsulated strain of Streptococcus pneumoniae.

Streptococcus pneumoniae strain JNR.7/87 is a highly virulent, type 4 encapsulated Gram-positive bacterium whose transformability has not been tested previously, and whose genome is currently being sequenced. The strain was transformed at very low efficiency by addition of exogenous competence-stimulating peptide: However, the efficiency was too low and irreproducible to be useful in many genetic studies. Therefore, the effects on transformation efficiency of changing different components of competence-stimulating peptide-induced transformation have been examined. Screening of growth media was followed by optimization of pre-induction culture acidification, glycine concentration, and induction time. An optimized protocol was developed whereby S. pneumoniae strain JNR.7/87 was transformed reproducibly with a streptomycin resistance (SmR) marker at an efficiency of approximately 10(5) colony forming units per 10(8) cells.

Bacterial Proteins↗
PubMed2000

Mechanisms of antibiotic resistance and tolerance in Streptococcus pneumoniae.

Streptococcus pneumoniae is a major pathogen causing potentially life-threatening community-acquired diseases in both the developed and developing world. Since 1967, there has been a dramatic increase in the incidence of penicillin-resistant and multiply antibiotic-resistant pneumococci worldwide. Prevention of access of the antibiotic to the target, inactivation of the antibiotic and alteration of the target are mechanisms that S. pneumoniae has developed to resist antibiotics. Recent studies on antibiotic-tolerant pneumococcal mutants permitted development of a novel model for the control of bacterial cell death.

Anti-Bacterial Agents↗
PubMed2006

Deglycosylation of human glycoconjugates by the sequential activities of exoglycosidases expressed by Streptococcus pneumoniae.

Streptococcus pneumoniae produces three surface-associated exoglycosidases; a neuraminidase, NanA, a beta-galactosidase, BgaA, and a beta-N-acetylglucosaminidase, StrH. the proposed functions of NanA, which removes terminal sialic acid, include revealing receptors for adherence, affecting the function of glycosylated host clearance molecules, modifying the surface of other bacteria coinhabiting the same niche, and providing a nutrient source. However, it is unclear whether following desialylation S. pneumoniae can further deglycosylate human targets through the activity of BgaA or StrH. We demonstrate that NanA, BgaA and StrH act sequentially to remove sialic acid, galactose and N-acetylglucosamine and expose mannose on human glycoproteins that bind to the pneumococcus and protect the airway. In addition, both BgaA and NanA were shown to contribute to the adherence of unencapsulated pneumococci, to human epithelial cells. Despite these findings, triple exoglycosidase mutants colonized mice as well as their parental strains, suggesting that any effect of these genes on colonization and disease may be host species-specific. These studies highlight the importance of considering the complete ability of S. pneumoniae to deglycosylate human targets and suggest that in addition to NanA, BgaA and StrH also contribute to pneumococcal colonization and/or pathogenesis.

Bacterial Adhesion↗
PubMed1992

A case of bacteremia due to resistant Streptococcus pneumoniae.

Streptococcus pneumoniae isolates with varying degrees of resistance to penicillin have been described. Strains that are highly resistant to penicillin (MIC, greater than 1 microgram/mL) and that are resistant to multiple antibiotics have been reported primarily in South Africa and Spain. We report a case of an adult patient with bacteremia due to S. pneumoniae that was highly resistant to penicillin (MIC, 4 micrograms/mL) and resistant to erythromycin, clindamycin, chloramphenicol, and co-trimoxazole who was successfully treated with vancomycin.

Bacteremia↗
PubMed2002

New approaches towards the identification of antibiotic and vaccine targets in Streptococcus pneumoniae.

Streptococcus pneumoniae causes more than one million deaths every year, mostly of young children in developing countries, due to pneumonia, bacteremia and meningitis. The emergence and dissemination of drug-resistant pneumococcal strains, coupled to changing patterns of virulence and the inadequacy of available vaccines, calls for an aggressive search for novel targets for antibiotic and vaccine development. Microbial genomics techniques allow genetic and biochemical tools to be employed to tackle discovery, design and development of new anti-infective agents based on the identification of hundreds of new targets. In this review, novel approaches employed to identify potential antibiotic and vaccine targets in S. pneumoniae are highlighted. Recently identified virulence factors, as well as molecules essential for bacterial viability, cell wall integrity and infectivity, are discussed.

Anti-Bacterial Agents↗
PubMed2001

Isolated septic arthritis caused by penicillin-resistant Streptococcus pneumoniae.

Streptococcus pneumoniae is a common cause of infection in the pediatric population, as well as an important cause of septic arthritis. The increased prevalence of drug-resistant S pneumoniae in North America has renewed interest in the use of pneumococcal vaccines. We describe the case of a child with isolated acute septic arthritis caused by infection with penicillin-resistant S pneumoniae.

Acute Disease↗
PubMed1984

Ocular pathogenicity of Streptococcus pneumoniae.

Streptococcus pneumoniae is a Gram-positive organism that commonly is the etiologic agent for external ocular infections. The conjunctival response may be relatively mild or quite intense with abundant discharge. Pharmaceutical management with various topical antibiotics is extremely effective in resolving the infection.

Conjunctivitis↗
PubMed2004

[A case of association of atypical localisations of Streptococcus pneumoniae].

Streptococcus pneumoniae can be responsible for spinal, joints, pulmonary or infrequently cutaneous septic localisations. The association between different septic localisation is extremely rare with this microorganism. We describe the first case of concomitant spinal, joints and cutaneous septic localisations in a critically ill patient with S. pneumoniae septicaemia. This observation illustrates that heterogeneity of clinical features depends on the pathogen characteristic and its interaction with the host.

Critical Illness↗
PubMed1997

Characterization of hemin binding activity of Streptococcus pneumoniae.

Streptococcus pneumoniae is a causative agent of bacterial pneumonia, otitis media, meningitis, and bacteremia. It causes considerable morbidity and mortality throughout the world, especially among children, the elderly, and immunocompromised individuals. We have demonstrated previously that the growth of S. pneumoniae is limited under iron-depleted conditions and can be restored by the addition of either hemin or hemoglobin. In the present study, we showed that S. pneumoniae had the ability to bind hemin and that the level of hemin binding activity was not affected by supplementation of the growth medium with iron. Approximately 70 to 80% of the hemin binding activity was mediated by proteinase-resistant components, and the remainder was mediated by proteins. Hemin binding proteins were located in both soluble extract and envelope fractions of pneumococcal cells. By batch affinity chromatography, a major hemin binding polypeptide with an apparent molecular mass of 43 kDa was identified in the cell lysate of S. pneumoniae. Polyclonal antibodies against this polypeptide were raised. By immunoblot analysis, this hemin binding polypeptide was localized in the envelope and did not exhibit any variation in molecular weight among all serotypes tested. The subcellular distribution of hemin binding activity may have functional implications.

Carrier Proteins↗
PubMed1999

Emergence of vancomycin tolerance in Streptococcus pneumoniae.

Streptococcus pneumoniae, the pneumococcus, is the most common cause of sepsis and meningitis. Multiple-antibiotic-resistant strains are widespread, and vancomycin is the antibiotic of last resort. Emergence of vancomycin resistance in this community-acquired bacterium would be catastrophic. Antibiotic tolerance, the ability of bacteria to survive but not grow in the presence of antibiotics, is a precursor phenotype to resistance. Here we show that loss of function of the VncS histidine kinase of a two-component sensor-regulator system in S. pneumoniae produced tolerance to vancomycin and other classes of antibiotic. Bacterial two-component systems monitor environmental parameters through a sensor histidine-kinase/phosphatase, which phosphorylates/dephosphorylates a response regulator that in turn mediates changes in gene expression. These results indicate that signal transduction is critical for the bactericidal activity of antibiotics. Experimental meningitis caused by the vncS mutant failed to respond to vancomycin. Clinical isolates tolerant to vancomycin were identified and DNA sequencing revealed nucleotide alterations in vncS. We conclude that broad antibiotic tolerance of S. pneumoniae has emerged in the community by a molecular mechanism that eliminates sensitivity to the current cornerstone of therapy, vancomycin.

Animals↗
PubMed2006

A functional dlt operon, encoding proteins required for incorporation of d-alanine in teichoic acids in gram-positive bacteria, confers resistance to cationic antimicrobial peptides in Streptococcus pneumoniae.

Streptococcus pneumoniae is one of the few species within the group of low-G +C gram-positive bacteria reported to contain no d-alanine in teichoic acids, although the dltABCD operon encoding proteins responsible for d-alanylation is present in the genomes of two S. pneumoniae strains, the laboratory strain R6 and the clinical isolate TIGR4. The annotation of dltA in R6 predicts a protein, d-alanine-d-alanyl carrier protein ligase (Dcl), that is shorter at the amino terminus than all other Dcl proteins. Translation of dltA could also start upstream of the annotated TTG start codon at a GTG, resulting in the premature termination of dltA translation at a stop codon. Applying a novel integrative translation probe plasmid with Escherichia coli 'lacZ as a reporter, we could demonstrate that dltA translation starts at the upstream GTG. Consequently, S. pneumoniae R6 is a dltA mutant, whereas S. pneumoniae D39, the parental strain of R6, and Rx, another derivative of D39, contained intact dltA genes. Repair of the stop codon in dltA of R6 and insertional inactivation of dltA in D39 and Rx yielded pairs of dltA-deficient and dltA-proficient strains. Subsequent phenotypic analysis showed that dltA inactivation resulted in enhanced sensitivity to the cationic antimicrobial peptides nisin and gallidermin, a phenotype fully consistent with those of dltA mutants of other gram-positive bacteria. In addition, mild alkaline hydrolysis of heat-inactivated whole cells released d-alanine from dltA-proficient strains, but not from dltA mutants. The results of our study suggest that, as in many other low-G+C gram-positive bacteria, teichoic acids of S. pneumoniae contain d-alanine residues in order to protect this human pathogen against the actions of cationic antimicrobial peptides.

Alanine↗
PubMed2001

PsaA (pneumococcal surface adhesin A) and PspA (pneumococcal surface protein A) DNA vaccines induce humoral and cellular immune responses against Streptococcus pneumoniae.

Streptococcus pneumoniae is one of the most important human pathogens and improvement of the currently used polysaccharide vaccines is being pursued. We constructed DNA vaccine vectors containing either the full-length psaA (pneumococcal surface adhesin A) or a truncated pspA (pneumococcal surface protein A--pspA') gene. Both constructs showed transient expression of the antigens in vertebrate cells and induced significant antibody response to the pneumococcal antigens in BALB/c mice injected intramuscularly (i.m.). Fusion with an N-terminal cytoplasmatic SV40 T-antigen (CT-Ag), which was previously shown to stabilize poorly expressed antigens through association with Hsp73, also induced anti-PspA antibody response. The induction of antibodies with a low IgG1:IgG2a ratio and elevated gamma interferon (IFN-gamma) production by spleen cells elicited by DNA vaccination indicate preferential priming of Th1 immunity. Since induction of antibodies against both PsaA and PspA was previously shown to correlate with protection against fatal infection with S. pneumoniae and cell-mediated immune responses could contribute to protection, further evaluation of PsaA and PspA as antigens for a DNA vaccine against S. pneumoniae could be promising.

Adhesins, Bacterial↗
PubMedDate not supplied

Virulence factors and the pathogenesis of disease caused by Streptococcus pneumoniae.

Streptococcus pneumoniae is a major pathogen of man causing diseases such as pneumonia, meningitis and otitis media. The mechanisms by which this organism causes these diseases are still largely unknown. The use of molecular approaches to identifying and studying putative virulence factors in combination with the application of animal models has allowed some of the mechanisms of the disease process to be defined.

Animals↗