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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 10 (1971), S. 3574-3578 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Microbiology 37 (1983), S. 143-187 
    ISSN: 0066-4227
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Microbiology 54 (2000), S. 81-127 
    ISSN: 0066-4227
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Notes: Abstract Emerging pathogens in drinking water have become increasingly important during the decade. These include newly-recognized pathogens from fecal sources such as Cryptosporidium parvum, Campylobacter spp., and rotavirus, as well as pathogens that are able to grow in water distribution systems, like Legionella spp., mycobacteria, and aeromonads. To perform a risk analysis for the pathogens in drinking water, it is necessary to understand the ecology of these organisms. The ecology of the drinking-water distribution system has to be evaluated in detail, especially the diversity and physiological properties of water bacteria. The interactions between water bacteria and (potential) pathogens in such diverse habitats as free water and biofilms are essential for the survival or growth of hygienically relevant organisms in drinking water. Results of epidemiological studies together with ecological data are the basis for effective resource protection, water treatment, and risk assessment.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1574-6941
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The colonization of biofilms of a benzoate-degrading Gram-positive water bacterium, strain B4, by a pathogenic Escherichia coli was studied in a continuous flow reactor. E. coli added to a fixed bed reactor colonized by B4, was able to grow in the biofilms and subsequently re-enter the free water phase in high numbers. Mixed biofilms of strain B4 and E. coli were also grown on glass slides for detailed examination of the spatial order of the mixed population biofilm. Individual cells as well as microcolonies of E. coli were detected in the biofilms by hybridization with a fluorescently labeled 23S rRNA-targeted oligonucleotide probe. The spatial distribution of E. coli could be analyzed in all layers of even thick biofilms.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 51 (2004), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Fluorescence in situ hybridization (FISH) using rRNA targeted oligonucleotide probes is a standard method for identification of microorganisms in environmental samples. Apart from its value as a phylogenetic marker ribosomal RNA has always been the favoured target molecule for FISH because of its abundance in all cells, whereas plasmids and DNA were regarded as unsuitable targets because of their low copy number. Here we present an improved FISH technique, which is based on polynucleotide probes. It goes beyond the detection of high copy intracellular nucleic acids such as rRNA (up to 104−105 copies per cell) and allows for the first time the in situ detection of individual genes or gene fragments on plasmids (101−103 copies per cell) and chromosomal DNA (〈10 copies per cell) in a single cell. Using E. coli as model organism we were able to detect in situ cells harbouring the antibiotic resistance gene beta lactamase on high, medium and low copy plasmids as well as the chromosomal encoded housekeeping gene glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Furthermore, we detected the prepilin peptidase gene xpsO in the plant pathogen Xanthomonas campestris in situ. Because of the characteristic hybridization signal obtained with this method – a halo-like, ring-shaped concentration of fluorescence in the cell periphery – we coined the term RING-FISH (recognition of individual genes) to differentiate it from conventional FISH.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 100 (1992), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Microbial ecology has long been hampered by the fact that most microorganisms cannot be identified in situ because of the lack of morphological diversity. The immunofluorescence approach has yielded important insights into the spatial distribution of microorganisms but has its severe limitations. The recently introduced fluorescently labelled, ribosomal RNA-targeted oligonucleotide probes have successfully been applied for the detection and identification in situ of individual microbial cells and evade some of the principal problems of the fluorescent antibodies. The design and synthesis of these phylogenetically nested probes does not require cultivation and isolation of the target organism and can therefore be used to monitor the population distribution and dynamics of hitherto uncultured microorganisms.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Allergy 37 (1982), S. 0 
    ISSN: 1398-9995
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The nature and extent of bacterially induced allergies are difficult to define. Since peptidoglycan, the main component of the cell wall of almost all bacteria, has been available in a highly purified, chemically and immunologically well-defined form, investigation of the allergological significance of this cell component is feasible. Intracutaneous tests were carried out on 181 test, subjects with five different peptidoglycan (PG) preparations from Staphylococcus aureus, Staphylococcus epidermis and Staphylococcus pyogenes. The results of the investigation were compared with the result of determination of serum PG antibodies and serum IgE concentrations. It was shown that test subjects with dual and late reactions to three three different staphylococcal PGs displayed significantly higher PG antibody titers than test subjects with negative reactions. Such a relationship could not he found with the cutaneous reactions to streptococcal PG. The total serum IgE values were very much higher in test subjects with immediate reactions to staphylococcal PG than in test subjects with a negative reaction. Typical Arthus reaction or late granulomatous reactions were not observed. Humoral antibodies are involved at least in part in the elicitation of dual and late reactions. Thus, there are interesting parallels to allergy to fungal spores and organic dusts.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1432-1440
    Keywords: Shock ; endotoxin ; mucopeptide ; limulus-test ; Schock ; Endotoxin ; Mucopeptid ; Limulus-Test
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Nicht nur die Endotoxine gramnegativer Bakterien, sondern auch die Mucopeptide verschiedener grampositiver Erreger können eine Gelierung von Amöbocytenlysaten ausLimulus polyphemus (LPL) hervorrufen. Offenbar abhängig von dem Grad der Solubilisierung ist die Wirksamkeit der Mucopeptide zwischen 1000 und 100000mal geringer als die von Endotoxin. Im Gegensatz zu Endotoxin hat die Behandlung von Mucopeptid mit Lysozym eine Abnahme bzw. einen vollständigen Verlust seiner Aktivität im LPL-Test zur Folge. Ein so behandeltes Mucopeptid ist im einfachen Capillarpräcipitationstest unter Verwendung von Antiseren gegen Mucopeptid ebenfalls nicht mehr präcipitierbar. Die Möglichkeit, die LPL-Aktivität von Mucopeptid durch Vorbehandlung mit Lysozym aufzuheben, erlaubt eine Abgrenzung gegenüber der Endotoxin-bedingten LPL-Gelierung. Bei im LPL-Test positiven Blutproben von Patienten mit Verdacht auf Endotoxämie könnte also eine Mucopeptid-induzierte LPL-Reaktion durch Vorbehandlung mit Lysozym ausgeschlossen werden.
    Notes: Summary Gelation of amebocyte lysate fromLimulus polyphemus (LPL) is induced not only by endotoxins of gramnegative bacteria but also by mucopeptides of various grampositive organisms. Solubilization considerably increases mucopeptide LPL-activity. Total activity of mucopeptide, however, is about 1000-100 000 times smaller than that of endotoxin. In contrast to endotoxin, treatment of mucopeptide with lysozyme causes decrease or complete loss of LPL-activity. Also mucopeptide thus handled does not react any more in the capillary precipitin test. The possibility to destroy mucopeptide LPL-activity by pretreatment with lysozyme permits differentiation from LPL-gelation by endotoxin. In blood specimens of patients with suspected endotoxemia and positive LPL-test mucopeptide induced LPL-reaction therefore can be excluded by pretreatment with lysozyme.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 62 (1968), S. 198-208 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Description / Table of Contents: Zusammenfassung Das Murein eines aus Milch isolierten Stammes von Staphylococcus epidermidis weist folgende Molverhältnisse auf (auf- bzw. abgerundete Zahlen): Mur:GlcNH2:Ala:Glu:Lys:Gly=1:1:3:1:1:4. Das Verhältnis D-Ala:L-Ala ist 1:2,03. Die Glutaminsäure liegt in der D-Konfiguration und als Amid vor. Durch die Isolierung und Identifizierung der Peptide des Partialhydrolysats des Mureins konnte die Aminosäuresequenz erschlossen werden. Die Sequenz des an die Muraminsäure gebundenen Tetrapeptides (L-Ala-D-GluNH2-L-Lys-D-Ala) stimmt mit dem der meisten anderen Bakterien überein. Die Quervernetzung wird durch das Peptid (Gly)4–5-L-Ala hergestellt, das mit dem N-terminalen Glycin an die Carboxylgruppe des D-Alanins und mit dem C-terminalen L-Alanin an die ε-Aminogruppe des Lysins zweier benachbarter Tetrapeptide gebunden ist. Die Dinitrophenylierung des Mureins ergab, daß 2% des Lysins (ε-Aminogruppe), 3% des gesamten Alanins und 7% des gesamten Glycins N-terminal vorliegen. Demnach ist die Quervernetzung nur zu rund 60% realisiert. Neben unvernetzten mehr oder weinger vollständigen Interpeptidbrücken kommen auch unvollständige Peptide vor, bei denen nur L-Alanin an die ε-Aminogruppe des Lysins gebunden ist. In mindestens 2% der Fälle fehlt die Interpeptidkette völlig.
    Notes: Summary A strain of Staphylococcus epidermidis was isolated from raw milk. Its murein contained muramic acid, glucosamine, alanine, D-glutamic acid, L-lysine and glucine at a molar ratio of about 1:1:3:1:1:4. The ratio D-Ala: L-Ala is 1:2.03. D-glutamic acid is present as an amide. By partial acid hydrolysis of the cell wall and subsequent isolation and identification of the peptides the amino acid sequence of the murein was elucidated. The tetrapeptide, bound to muramic acid is identical with that of most bacteria: L-Ala-D-GluNH2-L-Lys-D-Ala. The crosslinking of the murein is performed by the peptide (Gly)4–5-L-Ala. L-Ala is attached to the ε-aminogroup of lysine, while the N-terminal glycine is bound to the C-terminal D-alanine of an adjacent tetrapeptide. About 2% of lysine, 3% of alanine and 7% of glycine of the murein are dinitrophenylizable, indicating that about 2% of the tetrapeptides are not substituted by an interpeptide chain, and that 40% of the interpeptide chains are more or less incomplete (10% consist of L-alanine only) and are not bound to a C-terminal D-alanine.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 71 (1970), S. 271-282 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Description / Table of Contents: Zusammenfassung Die quantitative Aminosäurezusammensetzung des Mureins von M. flavum, M. thermosphactum, M. lacticum und M. liquefaciens wurder untersucht. Das Murein von M. flavum und M. thermosphactum weist folgende Molverhältnisse auf (auf- bzw. abgerundete Zahlen): DAP:Glu:Ala=1:1:1,5-1,7. Außerdem konnten 1,8 Mol Ammoniak pro Mol Glutaminsäure gefunden werden, was für ein Vorliegen von Glu und DAP als Amid spricht. Für das Murein von M. lacticum und M. liquifaciens ergeben sich folgende auf- bzw. abgerundete Molverhältnisse: M. lacticum: Hyg + Glu:Gly:L-Lys:D-Ala=1:2:2:1; M. liquefaciens: Hyg + Glu:Gly:hsr:D-Orn:D-Ala=1:2:1:1:1. Die Aminosäuresequenz des Mureins von M. liquefaciens konnte durch die Analyse der in den sauren Partialhydrolysaten der Zellwände auftretenden Peptide bestimmt werden. Das Murein von M. liquefaciens weist eine ähnliche Aminosäuresequenz wie das Murein von M. lacticum auf. Das an die Muraminsäure gebundene Tetrapeptid zeigt die Sequenz: Gly-Hyg(Glu)-Hsr-D-Ala. Die an der Quervernetzung beteiligte Interpeptidbrücke Nδ-Gly-D-Orn ist mit seinem Glycinende an die α-Carboxylgruppe der Hyg (Glu) und mit der α-Aminogruppe des D-Orn an das D-Ala einer benachbarten Peptiduntereinheit gebunden. Die Primärstruktur des Mureins von M. flavum und M. thermosphactum dagegen gleicht der des Mureins von Corynebacterium diphtheriae, wie aufgrund der quantitativen Aminosäurezusammensetzung und der „Fingerprints” von Partialhydrolysaten gefolgert werden konnte. M. flavum und M. thermosphactum unterscheiden sich aber nicht nur in ihrem Mureinaufbau, sondern auch in ihrer Morphologie und bestimmten physiologischen Merkmalen von M. lacticum und M. liquefaciens. Sie gleichen mehr den menschen- und tierpathogenen Corynebakterien und sollen daher aus der Gattung Microbacterium eliminiert werden. M. lacticum und M. liquefaciens zeigen dagegen eine weitgehende Ähnlichkeit mit bestimmten pflanzenpathogenen Corynebakterien.
    Notes: Summary The quantitative amino acid composition of the murein of M. flavum, M. thermosphactum, M. lacticum and M. liquefaciens was determined. The murein of M. flavum and M. thermosphactum contains DAP, Blu and Ala at a molar ratio of about 1:1:1,5-1,7. In addition, 1,8 moles of ammonia were found per mole of glutamic acid, indicating, that both DAP and Glu are present as amides. The murein of M. lacticum and M. liquefaciens showed the following molar ratios. M. lacticum: Hyg1+Glu:Gly:L-Lys:D-Ala=1:2:2:1; M. liquefaciens: Hyg+Glu:Gly:Hsr: D-Orn:D-Ala=1:2:1:1:1. The amino acid sequence of the murein of M. liquefaciens was determined by analysing the various peptides from acid partial hydrolysates of the cell walls. The murein of M. liquefaciens resembles the murein of M. lacticum. The tetrapeptide bound to the muramic acid has the sequence: Gly-Hyg(Glu)-Hsr-D-Ala. The cross-linkage is performed in the same way as in M. lacticum. The interpeptide bridge Nδ-Gly-D-Orn is bound by its glycine end to the α-carboxyl group of Hyg(Glu) and by the α-amino group of D-Orn to D-Ala of an adjacent peptide subunit. The primary structure of the murein of M. flavum and M. thermosphactum is similar to that of the murein of Corynebacterium diphtheriae as has been shown by the quantitative amino acid composition and the fingerprints of the partial hydrolysates of the cell walls. M. flavum and M. thermosphactum can be distinguished from M. lacticum and M. liquefaciens not only by murein type but also in morphology and certain physiological characteristics. They are closely related to the human and animal pathogenic corynebacteria and should be removed from the genus Microbacterium. M. lacticum and M. liquefaciens, on the other hand, differ significantly from human and animal pathogenic corynebacteria and show greatest similarity to certain plant pathogenic corynebacteria.
    Type of Medium: Electronic Resource
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