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

DOI to cite this document:

10.5283/epub.21445 Copy

Klingl, Andreas ; Moissl-Eichinger, Christine ; Wanner, Gerhard ; Zweck, Josef ; Huber, Harald ; Thomm, Michael ; Rachel, Reinhard

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Date of publication of this fulltext: 12 Jul 2011 05:46

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Details

Item type:	Article
Journal or Publication Title:	Archives of Microbiology
Publisher:	Springer Verlag
Page Range:	online
Date:	June 2011
Institutions:	Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) > Prof. Dr. Michael Thomm
Identification Number:	Value Type 10.1007/s00203-011-0720-y DOI
Keywords:	"Acidithiobacillus";Thiobacillus; Cell surface; S-layer; EPS; Pyrite; Electron microscopy; High-pressure freezing
Dewey Decimal Classification:	500 Science > 570 Life sciences
Status:	Published
Refereed:	Unknown
Created at the University of Regensburg:	Unknown
Item ID:	21445

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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 ...

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-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 Fe3+ ions, suggesting a role in the physiology of the microorganisms.

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Metadata last modified: 29 Sep 2021 07:38

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