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  • 1
    Electronic Resource
    Electronic Resource
    An Enzyme-Linked ImmunoSorbent Assay (ELISA) for the Identification of Naegleria fowleri in Environmental Water Samples (2003)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 50 (2003), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . Naegleria fowleri, a free-living amoeba, is the causative agent of primary amoebic meningoencephalitis, a fatal human disease of the central nervous system often contracted after swimming in fresh water. Identifying sites contaminated by N. fowleri is important in order to prevent the disease. An Enzyme-Linked ImmunoSorbent Assay (ELISA) has been developed for the specific identification of N. fowleri in primary cultures of environmental water samples. Of 939 samples isolated from artificially heated river water and screened by ELISA, 283 were positive. These results were subsequently confirmed by isoelectric focusing, the established reference method. A sensitivity of 97. 4% and a specificity of 97% were obtained. These results indicate that this ELISA method is reliable and can be considered as a powerful tool for the detection of N. fowleri in environmental water samples.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.2003.tb00244.x
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  • 2
    Electronic Resource
    Electronic Resource
    Isolation of a Unique Membrane Protein from Naegleria fowleri (2001)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 48 (2001), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . Naegleria fowleri, an amoeboflagellate, is the causative agent of Primary Amoebic Meningoencephalitis, a fulminating disease of the central nervous system. In order to elucidate the mechanisms of pathogenicity of this amoeba, a cDNA expression library was prepared from N. fowleri RNA. A specific protein was found to be expressed from a cDNA clone designated Mp2CL5. Northern blot analysis showed that the Mp2CL5 mRNA was expressed in pathogenic N. fowleri but was not expressed in non-pathogenic Naegleria species nor in Acanthamoeba. Western blot analysis using anti-. N fowleri antiserum demonstrated that IPTG-induced Escherichia coli Mp2CL5 expressed a 23-kDa recombinant protein. The Mp2CL5 recombinant protein was histidine-tagged and purified to homogeneity from E. coli. A polyclonal rabbit antiserum was prepared against the purified Mp2CL5 recombinant protein. This antibody was used to further characterize the Mp2CL5 native protein expressed by Nfowleri. Western blot analysis in conjunction with immunofLuorescence microscopy demonstrated the presence of a native protein of 17 kDa on the plasma membrane of N. fowleri trophozoites. The native N. fowleri protein was expressed in the logarithmic phase of trophozoite growth and the production of this protein increased through the stationary phase of growth. Studies are in progress to examine further its role as a virulence factor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.2001.tb00208.x
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  • 3
    Electronic Resource
    Electronic Resource
    Species specificity of a monoclonal antibody produced to Naegleria fowleri and partial characterization of its antigenic determinant (2000)
    Springer
    Parasitology research 86 (2000), S. 634-641 
    Details
    ISSN: 1432-1955
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Monoclonal antibody (Mab) 5D12 against Naegleria fowleri was analyzed for species specificity. Mab 5D12 reacted with a ubiquitous epitope present on the membrane of N. fowleri but not with soluble antigens. The Mab did not react with N. lovaniensis, N. gruberi, N. australiensis, or Acanthamoeba castellanii. The decreased reactivity of Mab 5D12 with N. fowleri observed after periodate oxidation, after digestion of carbohydrate moieties by three glycosidases, or after treatment of amebas with tunicamycin strongly suggests that the antigenic determinant has a polysaccharide component. Inhibition of the reactivity of Mab 5D12 by soluble saccharides supports the idea that N-acetyl or amino groups may play an important role in the recognition of the carbohydrate component of the epitope by the Mab. The specificity of Mab 5D12 makes this an ideal reagent for the identification of N. fowleri in environmental samples or in clinical specimens.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00008544
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