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  • 1
    In: International Journal of Systematic and Evolutionary Microbiology, Microbiology Society, Vol. 71, No. 7 ( 2021-07-13)
    Abstract: A novel, spore-forming, acidophilic and metal-resistant sulfate-reducing bacterium, strain OL T , was isolated from a microbial mat in a tailing dam at a gold ore mining site. Cells were slightly curved immotile rods, 0.5 µm in diameter and 2.0–3.0 µm long. Cells were stained Gram-negative, despite the Gram-positive cell structure revealed by electron microscopy of ultrathin layers. OL T grew at pH 4.0–7.0 with an optimum at 5.5. OL T utilised H 2 , lactate, pyruvate, malate, formate, propionate, ethanol, glycerol, glucose, fructose, sucrose, peptone and tryptone as electron donors for sulfate reduction. Sulfate, sulfite, thiosulfate, nitrate and fumarate were used as electron acceptors in the presence of lactate. Elemental sulfur, iron (III), and arsenate did not serve as electron acceptors. The major cellular fatty acids were C 16:1 ω7 c (39.0 %) and C 16 : 0 (12.1 %). The draft genome of OL T was 5.29 Mb in size and contained 4909 protein-coding genes. The 16S rRNA gene sequence placed OL T within the phylum Firmicutes , class Clostridia , family Peptococcaceae , genus Desulfosporosinus. Desulfosporosinus nitroreducens 59.4B T was the closest relative with 97.6 % sequence similarity. On the basis of phenotypic and phylogenetic characteristics, strain OL T represents a novel species within the genus Desulfosporosinus , for which we propose the name Desulfosporosinus metallidurans sp. nov. with the type strain OL T (=DSM 104464 T =VKM В−3021 T ).
    Type of Medium: Online Resource
    ISSN: 1466-5026 , 1466-5034
    Language: English
    Publisher: Microbiology Society
    Publication Date: 2021
    detail.hit.zdb_id: 215062-1
    detail.hit.zdb_id: 2056611-6
    SSG: 12
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  • 2
    Online Resource
    Online Resource
    Microbiology Society ; 2011
    In:  International Journal of Systematic and Evolutionary Microbiology Vol. 61, No. 11 ( 2011-11-01), p. 2697-2701
    In: International Journal of Systematic and Evolutionary Microbiology, Microbiology Society, Vol. 61, No. 11 ( 2011-11-01), p. 2697-2701
    Abstract: A novel obligately anaerobic, extremely thermophilic, organotrophic bacterium, strain 1445t T , was isolated from a hot spring on Kunashir Island (Kuril Islands, Russia). Cells were motile rods (0.4–0.5×1.0–3.0 µm). The temperature range for growth at pH 7.8 was 46–80 °C, with optimum growth at 65 °C. The pH range for growth at 65 °C was pH 5.7–9.0, with optimum growth at pH 7.8. Growth was not observed at or below 40 °C, at or above 84 °C, at or below pH 5.4 or at or above pH 9.5. The isolate degraded a wide range of substrates including starch, cellulose and cellulose derivatives. Elemental sulfur stimulated growth, but sodium sulfate, sulfite and thiosulfate did not. DNA G+C content was 31 mol%. Phylogenetic analysis of 16S rRNA gene sequences showed that strain 1445t T belonged to the genus Fervidobacterium . 16S rRNA gene sequence similarities with strains of other species of the genus Fervidobacterium were 94.9–98.3 %; the type strain of Fervidobacterium gondwanense was the closest relative of strain 1445t T . DNA–DNA hybridization of strain 1445t T and F. gondwanense AB39 T revealed a relatedness value of 20 %. Based on phylogenetic data and physiological properties of the isolate, a novel species, designated Fervidobacterium riparium sp. nov., is proposed with strain 1445t T ( = DSM 21630 T  = VKM B-2549 T ) as the type strain.
    Type of Medium: Online Resource
    ISSN: 1466-5026 , 1466-5034
    Language: English
    Publisher: Microbiology Society
    Publication Date: 2011
    detail.hit.zdb_id: 215062-1
    detail.hit.zdb_id: 2056611-6
    SSG: 12
    Location Call Number Limitation Availability
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  • 3
    In: Journal of General Virology, Microbiology Society, Vol. 90, No. 7 ( 2009-07-01), p. 1730-1733
    Abstract: The locations of amino acid positions relevant to antigenic variation in the nucleoprotein (NP) of influenza virus are not conclusively known. We analysed the antigenic structure of influenza A virus NP by introducing site-specific mutations at amino acid positions presumed to be relevant for the differentiation of strain differences by anti-NP monoclonal antibodies. Mutant proteins were expressed in a prokaryotic system and analysed by performing ELISA with monoclonal antibodies. Four amino acid residues were found to determine four different antibody-binding sites. When mapped in a 3D X-ray model of NP, the four antigenically relevant amino acid positions were found to be located in separate physical sites of the NP molecule.
    Type of Medium: Online Resource
    ISSN: 0022-1317 , 1465-2099
    RVK:
    RVK:
    Language: English
    Publisher: Microbiology Society
    Publication Date: 2009
    detail.hit.zdb_id: 2007065-2
    SSG: 12
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  • 4
    In: Journal of General Virology, Microbiology Society, Vol. 93, No. 2 ( 2012-02-01), p. 400-407
    Abstract: We reported recently that RNA-free spherical particles (SPs) generated by thermal remodelling of tobacco mosaic virus (TMV) are capable of binding GFP to their surface. Here, we show that SPs represent a universal particle platform that can form compositions by binding a diversity of various foreign proteins/epitopes of viral and non-viral origin to their surface. Numerous molecules of a foreign protein linked to the SP surface were revealed by immunogold electron microscopy. Several SP-based compositions were obtained containing one of the following foreign antigens: antigenic determinant A of rubella virus E1 glycoprotein; a recombinant protein containing the M2e epitope of influenza virus A protein M2; a recombinant antigen consisting of three epitopes of influenza virus A haemagglutinin; potato virus X (PVX) coat protein (CP); BSA; and PVX CP fused with the epitope of plum pox virus CP. The ‘mixed’ compositions could be also assembled by binding two different foreign antigens to each of the SPs. Immunogenicity of foreign antigens adsorbed or linked covalently to SPs in the SP-based compositions was examined. The antigenic specificity of foreign antigens was retained, whereas their immunogenicity increased significantly. It was inferred that SPs exhibit immunopotentiating activity, in particular in the form of compositions comprising SP and foreign antigen linked covalently to their surface by formaldehyde.
    Type of Medium: Online Resource
    ISSN: 0022-1317 , 1465-2099
    RVK:
    RVK:
    Language: English
    Publisher: Microbiology Society
    Publication Date: 2012
    detail.hit.zdb_id: 2007065-2
    SSG: 12
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