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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 37 (2000), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Group B streptococcal (GBS) infections are the most common cause of bacterial sepsis in the immediate newborn period. Apart from the capsule, the factors required for survival of GBS in the host are not well defined. In this study, signature-tagged transposon mutagenesis (STM) was used to identify genes required for growth and survival of GBS in a neonatal rat sepsis infection model. Approximately 1600 transposon mutants were screened in pools of 80 mutants, and approximately 120 mutants defective for survival in the animal host were identified. We successfully cloned and sequenced DNA flanking the transposon insertions from 92 of the mutants. Fifty per cent of the mutants had transposon insertions in genes with homologues in the public databases, whereas the remaining 50% had transposon insertions in genes with unknown function. A significant proportion of the avirulent mutants had transposon insertions in genes encoding transport-associated or regulatory proteins or in genes involved in cell surface metabolism, emphasizing the significance of these functions for in vivo survival of GBS. Overall, STM analysis revealed GBS genomic loci that encode a wide variety of functional gene classes, underscoring the diversity of bacterial processes required for the infection process. Currently, the function of the genes identified during the screening can only be inferred by homology to previously described genes. However, a number of the genes identified in this study have been shown to correlate with virulence in other pathogens. Avirulence of a subset of mutants identified during the screening was confirmed by performing competitive index assays and lethal dose assays. This represents the first report of a genome-wide scan for virulence factors in GBS. The identified genes will further our understanding of the pathogenesis of GBS infections and may represent targets for intervention or lead to the development of novel therapies.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Group B streptococci (GBS) remain the most significant bacterial pathogen causing neonatal sepsis, pneumonia and meningitis in the USA despite CDC-recommended chemoprophylaxis strategies for preventing infection. To cause infection pathogens such as GBS must evade recognition and clearance by the host's immune system. Strategies for avoidance of opsonization and phagocytic killing include elaboration of antiopsonophagocytic capsules and surface proteins. During screening for mutants of GBS that were attenuated for virulence in a neonatal rat sepsis model, we identified a mutant with a transposon insertion in the ponA gene. ponA encodes an extra-cytoplasmic penicillin-binding protein PBP1a, a newly identified virulence trait for GBS that promotes resistance to phagocytic killing independent of capsular polysaccharide. Complementation analysis in vivo and in vitro confirmed that the altered phenotypes observed in the mutant were due to the transposon insertion in ponA. Deletion of PBP1a does not affect C3 deposition on GBS suggesting that mechanism by which PBP1a protects GBS from phagocytic killing is distinct from the antiopsonic activity of capsular polysaccharide. This is the first report describing expression of an antiphagocytic surface protein by GBS and represents a novel mechanism for evasion of immune recognition and clearance that may explain the decreased virulence observed in Gram-positive bacterial species for penicillin-binding protein mutants.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Bacterial virulence often depends on exported proteins. To identify genes encoding exported proteins in the neonatal pathogen, group B streptococcus, the transposon TnphoZ was constructed. Here, the coding sequence for the secretion-dependent enzyme alkaline phosphatase from Enterococcus faecalis was fused to the left terminal repeat of Tn917, generating TnphoZ. A collection of TnphoZ mutants was isolated and the DNA flanking the transposon insertion sites was sequenced. Sequence data correlated the expression of high AP activity with transposon insertion into genes encoding predicted exported proteins. It is anticipated that TnphoZ will be suitable for use in other Gram-positive hosts.
    Type of Medium: Electronic Resource
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  • 4
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    Unknown
    Springer
    In:  Antonie van Leeuwenhoek International Journal of General and Molecular Microbiology, 103 (5). pp. 1069-1078.
    Publication Date: 2017-08-28
    Description: A polyphasic analysis was carried out to clarify the taxonomic status of four marine actinomycete strains that share a phylogenetic relationship and phenotypic characteristics with the genus Salinispora. These strains formed a distinct lineage within the Salinispora 16S rRNA and gyrB trees and were found to possess a range of phenotypic properties and DNA:DNA hybridization values that distinguished them from the type strains of the two validly named species in this genus, Salinisporatropica (CNB-440T, ATCC BAA-916T) and Salinispora arenicola (CNH-643T, ATCC BAA-917T). The combined genotypic and phenotypic data support this conclusion. It is proposed that the strains be designated as Salinisporapacifica sp. nov., the type strain of which is CNR-114T (DSMZ YYYYT = KACC 17160T).
    Type: Article , PeerReviewed
    Format: text
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  • 5
    Publication Date: 2019-09-23
    Description: Albidopyrone, a new α-pyrone-containing secondary metabolite, was produced by Streptomyces sp. NTK 227, a strain isolated from Atlantic Ocean sediment and found to be a member of the Streptomyces albidoflavus 16S rRNA gene clade. The structure of the compound was determined by MS and NMR spectroscopy, and found to have a moderate inhibitory activity against protein-tyrosin phosphatase B.
    Type: Article , PeerReviewed
    Format: text
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