Klingl, Andreas and Moissl-Eichinger, Christine and Wanner, Gerhard and Zweck, Josef and Huber, Harald and Thomm, Michael and Rachel, Reinhard (2011) Analysis of the surface proteins of Acidithiobacillus ferrooxidans strain SP5/1 and the new, pyrite-oxidizing Acidithiobacillus isolate HV2/2, and their possible involvement in pyrite oxidation. ARCHIVES OF MICROBIOLOGY, 193 (12). pp. 867-882. ISSN 0302-8933,
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Two strains of rod-shaped, pyrite-oxidizing acidithiobacilli, their cell envelope structure and their interaction with pyrite were investigated in this study. Cells of both strains, Acidithiobacillus ferrooxidans strain SP5/1 and the moderately thermophilic Acidithiobacillus sp. strain HV2/2, were similar in size, with slight variations in length and diameter. Two kinds of cell appendages were observed: flagella and pili. Besides a typical Gram-negative cell architecture with inner and outer membrane, enclosing a periplasm, both strains were covered by a hitherto undescribed, regularly arranged 2-D protein crystal with p2-symmetry. In A. ferrooxidans, this protein forms a stripe-like structure on the surface. A similar surface pattern with almost identical lattice vectors was also seen on the cells of strain HV2/2. For the surface layer of both bacteria, a direct contact to pyrite crystals was observed in ultrathin sections, indicating that the S-layer is involved in maintaining this contact site. Observations on an S-layer-deficient strain show, however, that cell adhesion does not strictly depend on the presence of the S-layer and that this surface protein has an influence on cell shape. Furthermore, the presented data suggest the ability of the S-layer protein to complex Fe(3+) ions, suggesting a role in the physiology of the microorganisms.
Item Type: | Article |
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Uncontrolled Keywords: | EXTRACELLULAR POLYMERIC SUBSTANCES; S-LAYER; CELL-ENVELOPE; THIOBACILLUS-FERROOXIDANS; 3-DIMENSIONAL STRUCTURE; IGNICOCCUS-HOSPITALIS; THERMOPROTEUS-TENAX; IRON COMPLEXATION; GLYCOPROTEIN; BACTERIA; Acidithiobacillus; Thiobacillus; Cell surface; S-layer; EPS; Pyrite; Electron microscopy; High-pressure freezing |
Subjects: | 500 Science > 530 Physics 500 Science > 570 Life sciences |
Divisions: | Physics > Institute of Experimental and Applied Physics > Chair Professor Back > Group Josef Zweck Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) > Prof. Dr. Michael Thomm |
Depositing User: | Dr. Gernot Deinzer |
Date Deposited: | 26 May 2020 10:06 |
Last Modified: | 26 May 2020 10:06 |
URI: | https://pred.uni-regensburg.de/id/eprint/19760 |
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