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  • 1
    Electronic Resource
    Electronic Resource
    Insights into social insects from the genome of the honeybee Apis mellifera (2006)
    [s.l.] : Nature Publishing Group
    Nature 443 (2006), S. 931-949 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Here we report the genome sequence of the honeybee Apis mellifera, a key model for social behaviour and essential to global ecology through pollination. Compared with other sequenced insect genomes, the A. mellifera genome has high A+T and CpG contents, lacks major transposon families, evolves more ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature05260
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  • 2
    Electronic Resource
    Electronic Resource
    Colicins produced by the Escherichia fergusonii strains closely resemble colicins encoded by Escherichia coli (2002)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 208 (2002), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Plasmid DNA of six Escherichia fergusonii colicinogenic strains (three producers of colicin E1, two of Ib and one of Ia) was isolated and the colicin-encoding regions of the corresponding Col plasmids were sequenced. Two new variants of colicin E1, one of colicin Ib, and one of colicin Ia were identified as well as new variants of the colicin E1 and colicin Ib immunity proteins and the colicin E1 lysis polypeptide. The recombinant Escherichia coli producer harboring pColE1 from E. fergusonii strain EF36 (pColE1-EF36) was found to be only partially immune to E1 colicins produced by two other E. fergusonii strains suggesting that pColE1-EF36 may represent an ancestor ColE1 plasmid.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2002.tb11091.x
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  • 3
    Electronic Resource
    Electronic Resource
    Epidemiology of Staphylococcus aureus during space flight (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 16 (1996), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Abstract Staphylococcus aureus was isolated over 2 years from Space Shuttle mission crewmembers to determine dissemination and retention of bacteria. Samples before and after each mission were from nasal, throat, urine, and feces and from air and surface sampling of the Space Shuttle. DNA fingerprinting of samples by digestion of DNA with SmaI restriction endonuclease followed by pulsed-field gel electrophoresis showed S. aureus from each crewmember had a unique fingerprint and usually only one strain was carried by an individual. There was only one instance of transfer between crewmembers. Strains from interior surfaces after flight matched those of crewmembers, suggesting microbial fingerprinting may have forensic application.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1996.tb00146.x
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  • 4
    Electronic Resource
    Electronic Resource
    In vivo testing of an Enterococcus faecalis efaA mutant and use of efaA homologs for species identification (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 21 (1998), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Disruption of the previously described efaA (from Enterococcus faecalis antigen A) gene was generated in E. faecalis strain OG1RF and loss of an ∼37-kDa immunoreactive band from the mutant was demonstrated in Western blots. In a mouse peritonitis model, mice infected with the efaAfs (fs=from Enterococcus faecalis) mutant showed more prolonged survival than mice infected with the parent strain OG1RF. These results suggest that efaAfs encodes a function important for infection of mice by enterococci. An efaA-like gene was also identified in E. faecium DNA libraries and its deduced amino acid sequence showed 73% similarity to EfaA of E. faecalis and 42–63% similarities to a group of streptococcal virulence and adhesion associated proteins that are components of ATP-binding cassette transport systems. Intragenic probes representing efaAfs, recAfs, efaAfm (fm=from E. faecium) and gyrAfm were tested for their ability to identify E. faecalis and E. faecium using colony lysates of 133 enterococci and one Streptococcus sp. Probes of E. faecium and E. faecalis origin hybridized to all isolates of E. faecium and E. faecalis, respectively, regardless of their clinical source but not to any of 29 other enterococci. These results suggest that the use of gene probes may prove helpful in identification of isolates of E. faecium and E. faecalis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1998.tb01180.x
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  • 5
    Electronic Resource
    Electronic Resource
    The genome of Treponema pallidum: new light on the agent of syphilis (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology reviews 22 (1998), S. 0 
    Details
    ISSN: 1574-6976
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Treponema pallidum subsp. pallidum, the causative agent of the sexually transmitted disease syphilis, is a fastidious, microaerophilic obligate parasite of humans. This bacterium is one of the few prominent infectious agents that has not been cultured continuously in vitro and consequently relatively little is known about its virulence mechanisms at the molecular level. T. pallidum therefore represented an attractive candidate for genomic sequencing. The complete genome sequence of T. pallidum has now been completed and comprises 1 138 006 base pairs containing 1041 predicted protein coding sequences. An important goal of this project is to identify possible virulence factors. Analysis of the genome indicates a number of potential virulence factors including a family of 12 proteins related to the Msp protein of Treponema denticola, a number of putative hemolysins, as well as several other classes of proteins of interest. The results of this analysis are reviewed in this article and indicate the value of whole genome sequences for rapidly advancing knowledge of infectious agents.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6976.1998.tb00373.x
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  • 6
    Electronic Resource
    Electronic Resource
    Conditional adherence of Enterococcus faecalis to extracellular matrix proteins (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 21 (1998), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The adherence of 44 clinical isolates of Enterococcus faecalis, a common cause of endocarditis, and 13 Enterococcus faecium to substrates of six extracellular matrix (ECM) proteins was examined using 35S-labeled bacteria. One E. faecalis strain, isolated from a patient with endocarditis, adhered to collagen types I and IV and another E. faecalis strain adhered to laminin and to collagen types I and IV. However, most isolates showed little adherence (〈5% of added cells adhered) when grown at 37°C regardless of their source (endocarditis, urine or fecal sample). When grown at 46°C (but not when grown in CO2 or nutrient limited media), most isolates of E. faecalis increased their adherence to immobilized laminin, collagen types I and IV but not to fibronectin, fibrinogen or bovine serum albumin, whereas none of the E. faecium increased adherence when grown at 46°C or 50°C. The adherence of E. faecalis was eliminated by digestion with trypsin, suggesting that a protein is somehow important, directly or indirectly, for adherence to occur. Pre-incubation of bacteria with soluble collagen types I and IV inhibited the adherence to these ECM proteins. These results demonstrate that in E. faecalis, adherence to ECM proteins is produced during routine in vitro growth conditions by occasional isolates and can be produced during certain stressful growth conditions by others. Whether this adherence relates to the propensity of E. faecalis to cause endocarditis remains to be determined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1998.tb01176.x
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  • 7
    Electronic Resource
    Electronic Resource
    Clinical isolates of Enterococcus faecium exhibit strain-specific collagen binding mediated by Acm, a new member of the MSCRAMM family (2003)
    Oxford, UK : Blackwell Science, Ltd
    Molecular microbiology 47 (2003), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A collagen-binding adhesin of Enterococcus faecium, Acm, was identified. Acm shows 62% similarity to the Staphylococcus aureus collagen adhesin Cna over the entire protein and is more similar to Cna (60% and 75% similarity with Cna A and B domains respectively) than to the Enterococcus faecalis collagen-binding adhesin, Ace, which shares homology with Acm only in the A domain. Despite the detection of acm in 32 out of 32 E. faecium isolates, only 11 of these (all clinical isolates, including four vancomycin-resistant endocarditis isolates and seven other isolates) exhibited binding to collagen type I (CI). Although acm from three CI-binding vancomycin-resistant E. faecium clinical isolates showed 100% identity, analysis of acm genes and their promoter regions from six non-CI-binding strains identified deletions or mutations that introduced stop codons and/or IS elements within the gene or the promoter region in five out of six strains, suggesting that the presence of an intact functional acm gene is necessary for binding of E. faecium strains to CI. Recombinant Acm A domain showed specific and concentration-dependent binding to collagen, and this protein competed with E. faecium binding to immobilized CI. Consistent with the adherence phenotype and sequence data, probing with Acm-specific IgGs purified from anti-recombinant Acm A polyclonal rabbit serum confirmed the surface expression of Acm in three out of three collagen-binding clinical isolates of E. faecium tested, but in none of the strains with a non-functional pseudo acm gene. Introduction of a functional acm gene into two non-CI-binding natural acm mutant strains conferred a CI-binding phenotype, further confirming that native Acm is sufficient for the binding of E. faecium to CI. These results demonstrate that acm, which encodes a potential virulence factor, is functional only in certain infection-derived clinical isolates of E. faecium, and suggest that Acm is the primary adhesin responsible for the ability of E. faecium to bind collagen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2003.03417.x
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  • 8
    Electronic Resource
    Electronic Resource
    Isolation of enterococcal antigen-encoding genes from genomic libraries (1998)
    Springer
    Methods in cell science 20 (1998), S. 95-106 
    Details
    ISSN: 1573-0603
    Keywords: Antigen ; Cosmid ; Immunoscreening ; Library construction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have devised a procedure using immune sera to identify antigen-encoding genes of strains of Enterococcus faecalis. First, genomic cosmid libraries containing large inserts were constructed and screened with sera from patients with enterococcal infectious endocarditis and with serum from a rabbit immunized with surface proteins of an enterococcal endocarditis isolate. Immunopositive cosmid clones were analyzed by restriction enzyme digestions and clones containing distinct inserts were chosen for subcloning. Sublibraries were screened with one of the five sera, and immunopositive subclones were subjected to DNA sequencing. BLASTX and BLASTN at NCBI were used to search for database similarities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009847127291
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  • 9
    Electronic Resource
    Electronic Resource
    Targeted mutagenesis of enterococcal genes (1998)
    Springer
    Methods in cell science 20 (1998), S. 21-33 
    Details
    ISSN: 1573-0603
    Keywords: Conjugation ; Electroporation ; Enterococcus ; mγδ ; Targeted mutagenesis ; Transposon
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A series of methods was developed for targeted mutagenesis in enterococci. First, a transposon mutagenesis system, miniγδ-200 (mγδ), which was used previously to make insertion mutants in streptococci, was shown to be useful for generation of mutants in enterococci. After mutagenesis of cosmid clones carrying enterococcal DNA inserts in Escherichia coli with mγδ, we were able to isolate the mutants by phenotype or to screen for them by immunoblotting or comparison of restriction digestion patterns. Clones with mγδ insertions in targeted enterococcal genes were then introduced into enterococci by electroporation to generate targeted disruption mutations. Allelic replacement en masse, that is, electroporation of enterococci with DNA from a pool of mutagenized cosmid clones, was shown to be an efficient method to obtain mutations in genes with detectable phenotypes in enterococci. We next constructed a vector for mutagenesis using small intragenic fragments of enterococcal genes to disrupt targeted genes. This vector was modified from pBluescript SK (−) by cloning the kanamycin resistance determinant from mγδ into the ScaI site internal to the ampicillin resistance gene. It was then used to generate insertion mutants in Enterococcus faecalis with an intragenic fragment as small as about 500 bp. A third method, based on the conjugation system reported by Trieu-Cuot et al. [1], was developed in order to circumvent difficulties in the electroporation of some enterococcal strains and to improve the efficiency with which targeted mutations can be generated in enterococci. This system was capable of mobilizing both small plasmids and large cosmids into enterococci by conjugation, and produced disruption mutations by homologous recombination.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009803328200
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  • 10
    Electronic Resource
    Electronic Resource
    Mutation of the promoter and LexA binding sites of cea, the gene encoding colicin E1 (1989)
    Springer
    Molecular genetics and genomics 215 (1989), S. 483-489 
    Details
    ISSN: 1617-4623
    Keywords: SOS response ; ColE1 plasmid ; Catabolite repression ; Gene fusion ; RecA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Three mutations were introduced into the cea promoter using oligonucleotide directed mutagenesis. The resulting mutant promoter has the Escherichia coli consensus sequences at its-35 and-10 positions, separated by the optimal spacing. In addition, a plasmid with a mutation in one of the two LexA repressor binding sites in the cea regulatory region was isolated that decreases homology with the consensus LexA binding site. The effects of these mutations on cea expression were studied in cea-lacZ protein fusions. The promoter-up mutant, when present in a multicopy plasmid, showed a shorter induction lag when compared to the wild-type cea gene, and there was less of an effect of the catabolite repression system on cea expression. However, when present in a single copy in the bacterial chromosome, catabolite repression and an induction delay were observed, despite the increased strength of the promoter. The operator mutant showed a slightly higher basal level of expression, but was still repressible. Induction occurred with a shortened lag period, but the effects were not as great as with the promoter mutant. These results support the idea that tight repression by LexA contributes to the delay in cea induction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00427047
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