Analysis of the surface proteins of Acidithiobacillus ferrooxidans strain SP5/1 and the new, pyrite-oxidizing Acidithiob
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ORIGINAL PAPER
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 Andreas Klingl • Christine Moissl-Eichinger • Gerhard Wanner • Josef Zweck • Harald Huber Michael Thomm • Reinhard Rachel
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Received: 3 December 2010 / Revised: 5 May 2011 / Accepted: 7 May 2011 / Published online: 23 June 2011 Ó Springer-Verlag 2011
Abstract 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-layerdeficient 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 Fe3? ions, suggesting a role in the physiology of the microorganisms. Keywords Acidithiobacillus Thiobacillus Cell surface S-layer EPS Pyrite Electron microscopy High-pressure freezing
Communicated by Erko Stackebrandt.
Electronic supplementary material The online version of this article (doi:10.1007/s00203-011-0720-y) contains supplementary material, which is available to authorized users. A. Klingl R. Rachel (&) Centre for Electron Microscopy at the Institute for Anatomy, University of Regensburg, Universita¨tsstr. 31, 93053 Regensburg, Germany e-mail: [email protected] C. Moissl-Eichinger H. Huber M. Thomm Institute for Microbiology and Archaea Center, University of Regensburg, Universita¨tsstr. 31, 93053 Regensburg, Germany G. Wanner Biocentre, University of Munich, Planegg-Martinsried, 82152 Munich, Germany J. Zweck Centre for EM at the Institute of Physics, University of Regensburg, Universita¨tsstr. 31, 93053 Regensburg, Germany
Introduction In general, an S-layer or a surface layer consists of a monolayer of regularly arranged identical protein subunits. Its assembly is driven by entropical processes and results in a protein lattice with p1-, p2-, p3-, p4-, or p6-symmetry (Sleytr et al. 1988; Eichler 2003). Symmetry and dimensio
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