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  • 1
    Electronic Resource
    Electronic Resource
    Localization of the carbohydrate residue of the S-layer glycoprotein from Clostridium thermohydrosulfuricum L111-69 (1989)
    Springer
    Archives of microbiology 151 (1989), S. 416-420 
    Details
    ISSN: 1432-072X
    Keywords: Bacterial cell wall ; Crystalline surface layer (S-layer) ; Eubacterial glycoproteins ; Clostridium thermohydrosulfuricum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The location of the covalently attached carbohydrate residue of the S-layer glycoprotein from Clostridium thermohydrosulfuricum L111-69 was determined by electron microscopical procedures after converting the hydroxyl groups of the carbohydrate chains into carboxyl groups by succinylation. The introduction of carboxyl groups was examined by labelling with polycationized ferritin (PCF; a net positively charged topographical marker for electron microscopy). Cyanogen bromide was used for activating vicinal hydroxyl groups of the carbohydrate chains which could then react with amino groups of amino carbonic acids or ferritin. The amount of covalently bound ferritin was determined by freeze-etching and UV-measurement. Both, succinylation experiments and covalent attachment of ferritin confirmed that at least a considerable portion of the carbohydrate residue must be located on the S-layer surface.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00416600
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  • 2
    Electronic Resource
    Electronic Resource
    Structural and chemical characterization of S-layers of selected strains ofBacillus stearothermophilus andDesulfotomaculum nigrificans (1986)
    Springer
    Archives of microbiology 146 (1986), S. 19-24 
    Details
    ISSN: 1432-072X
    Keywords: Bacterial cell wall ; S-layer ; Crystalline surface layers ; Cell surface ; Glycoprotein ; Bacillaceae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The structures, amino acid- and neutral sugar compositions of the crystalline surface layers (S-layers) of four selected strains each ofBacillus stearothermophilus andDesulfotomaculum nigrificans were compared. Among the four strains of each species a remarkable diversity in the molecular weights of the S-layer subunits and in the geometry and constants of the S-layer lattices was apparent. The crystalline arrays included hexagonal (p6), square (p4) and oblique (p2) lattices. In vitro self-assembly of isolated S-layer subunits (or S-layer fragments) led to the formation of flat sheets or open-ended cylindrical assembly products. The amino acid composition of the S-layers exhibited great similarities and was predominantly acidic. With the exception of the S-layers of two strains ofB. stearothermophilus (where only traces of neutral sugars could be detected), all other S-layer proteins seemed to be glycosylated. Among these strains significant differences in the amount and composition of the glycan portions were found. Based on this diversity interesting questions may be asked about the biological significance of the carbohydrate units of glycoproteins in prokaryotic organisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00690152
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of S-layers from mesophilic bacillaceae and studies on their protective role towards muramidases (1990)
    Springer
    Archives of microbiology 153 (1990), S. 209-214 
    Details
    ISSN: 1432-072X
    Keywords: Crystalline surface layer ; S-layer ; Bacillaceae ; Lysozyme ; Mutanolysin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The structure of the S-layers from eight mesophilic Bacillaceae was investigated by freeze-etching of whole cells. The S-layer lattices from Bacillus alvei CCM 2051 and B. circulans CCM 1048 exhibited oblique symmetry. Square S-layer lattices were identified for B. polymyxa CCM 1459, B. circulans CCM 2048 and B. sphaericus strains CCM 2120 and CCM 2177. Two superimposed, structurally different S-layers were detected for B. brevis strains CCM 1089 and CCM 1463. In both organisms the outer S-layer lattice showed oblique and the inner S-layer lattice hexagonal symmetry. Labelling with polycationized ferritin (a net positively charged topographical marker for electron microscopy) revealed that the S-layer surface from all strains is not net negatively charged. In thin-section preparations all strains exhibited only a 5 nm thick peptidoglycan-containing layer. Whole cells from B. circulans CCM 2048 and from both B. brevis strains were rapidly lysed by the muramidases lysozyme (MW 14,600) and mutanolysine (MW 24,000) showing that their S-layers which allowed free passage for both enzymes must possess pores larger than 3.5 nm. By contrast, whole cells from B. circulans CCM 1048, B. alvei CCM 2051, B. polymyxa CCM 1459 and B. sphaericus strains CCM 2120 and CCM 2177 were resistant to both muramidases. It could be shown that these strains possess muramidase resistant peptidoglycan-containing layers. Therefore, the latter results did not confirm the claim in the literature that muramidase resistance of S-layer carrying mesophilic Bacillaceae is caused by the S-layer itself acting as a protective coat.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00249069
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  • 4
    Electronic Resource
    Electronic Resource
    Surface properties from the S-layer of Clostridium thermosaccharolyticum D120-70 and Clostridium thermohydrosulfuricum L111-69 (1988)
    Springer
    Archives of microbiology 149 (1988), S. 527-533 
    Details
    ISSN: 1432-072X
    Keywords: Bacterial cell wall ; S-layer ; Crystalline surface layers ; Surface charge ; Surface hydrophobicity ; Clostridium thermohydrosulfuricum ; Clostridium thermosaccharolyticum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Labelling experiments using a positively charged topographical marker for electron microscopy, polycationized ferritin, showed that the S-layers of two closely related clostridia Clostridium thermohydrosulfuricum L111-69 and C. thermosaccharolyticum D120-70 do not exhibit a net negative charge, as usually observed for bacterial cell surfaces. Chemical modification of reactive sites confirmed that amino and carboxyl groups are exposed on the S-layer surface of both strains. Amino-specific, bifunctional agents crosslinked both S-layer lattices. Studies with carbodiimides revealed that only the S-layer surface of C. thermohydrosulfuricum L111-69 had amino and carboxyl groups closely enough aligned to permit electrostatic interactions between the constituent protomers. The regular structure of this S-layer lattice was lost upon converting the carboxyl groups into neutral groups by amidation. Disintegration of both S-layer lattices occurred upon N-acetylation or N-succinylation of the free amino groups. Adhesion experiments showed that in neutral and weakly alkaline environment whole cells of C. thermosaccharolyticum D120-70 exhibited a stronger tendency to bind to charged surfaces than whole cells of C. thermohydrosulfuricum L111-69, but showed a lower tendency to bind to hydrophobic materials.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446756
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  • 5
    Electronic Resource
    Electronic Resource
    Heterologous expression and self-assembly of the S-layer protein SbsA of Bacillus stearothermophilus in Escherichia coli (1996)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 19 (1996), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The cell surface of Bacillus stearothermophilus PV72 is covered by a regular surface layer (S-layer) composed of a single species of protein, SbsA, with a molecular weight of 130 000. Recently, the sequence of the corresponding gene (sbsA) has been determined. The SbsA coding region including the signal sequence was cloned as a polymerase chain reaction (PCR) product into a low-copy-number vector under the transcriptional control of the λpL promoter. Expression of sbsA was shown to be thermally inducible from the resulting vector pBK4 in a strain of Escherichia coli expressing the λcI857 from the chromosome. As shown by ultrathin sectioning of whole cells and immunogold labelling using SbsA-specific antibodies, expression of sbsA in E. coli led to accumulation of sheet-like self-assembling products of the protein in the cytoplasm. No SbsA protein was detected either in the periplasm or in the supernatant fractions. Long-term expression of sbsA from pBK4, including in the late stationary phase, did not lead to degradation of SbsA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1996.386918.x
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  • 6
    Electronic Resource
    Electronic Resource
    Self-assembly product formation of the Bacillus stearothermophilus PV72/p6 S-layer protein SbsA in the course of autolysis of Bacillus subtilis (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 172 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In order to achieve high level expression and to study the release of a protein capable of self-assembly, the gene encoding the crystalline cell surface (S-layer) protein SbsA of Bacillus stearothermophilus PV72/p6, including its signal sequence, was cloned and expressed in Bacillus subtilis. To obtain high level expression, a tightly regulated, xylose-inducible, stably replicating multicopy-plasmid vector was constructed. After induction of expression, the S-layer protein made up about 15% of the total cellular protein content, which was comparable to the SbsA content of B. stearothermophilus PV72/p6 cells. During all growth stages, SbsA was poorly secreted to the ambient cellular environment by B. subtilis. Extraction of whole cells with guanidine hydrochloride showed that in late stationary growth phase cells 65% of the synthesised SbsA was retained in the peptidoglycan-containing layer, indicating that the rigid cell wall layer was a barrier for efficient SbsA secretion. Electron microscopic investigation revealed that SbsA release from the peptidoglycan-containing layer started in the late stationary growth phase at distinct sites at the cell surface leading to the formation of extracellular self-assembly products which did not adhere to the cell wall surface. In addition, intracellular sheet-like SbsA self-assembly products which followed the curvature of the cell became visible in partly lysed cells. Intracellularly formed self-assembly products remained intact even after complete lysis of the rigid cell envelope layer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb13468.x
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  • 7
    Electronic Resource
    Electronic Resource
    Application Potential of 2D Protein Crystals (S-Layers) (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 745 (1994), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1994.tb44380.x
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  • 8
    Electronic Resource
    Electronic Resource
    V. Functions of S-layers (1997)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology reviews 20 (1997), S. 0 
    Details
    ISSN: 1574-6976
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Although S-layers are being increasingly identified on Bacteria and Archaea, it is enigmatic that in most cases S-layer function continues to elude us. In a few instances, S-layers have been shown to be virulence factors on pathogens (e.g. Campylobacter fetus ssp. fetus and Aeromonas salmonicida), protective against Bdellovibrio, a depository for surface-exposed enzymes (e.g. Bacillus stearothermophilus), shape-determining agents (e.g. Thermoproteus tenax) and nucleation factors for fine-grain mineral development (e.g. Synechococcus GL 24). Yet, for the vast majority of S-layered bacteria, the natural function of these crystalline arrays continues to be evasive. The following review up-dates the functional basis of S-layers and describes such diverse topics as the effect of S-layers on the Gram stain, bacteriophage adsorption in lactobacilli, phagocytosis by human polymorphonuclear leukocytes, the adhesion of a high-molecular-mass amylase, outer membrane porosity, and the secretion of extracellular enzymes of Thermoanaerobacterium. In addition, the functional aspect of calcium on the Caulobacter S-layer is explained.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6976.1997.tb00305.x
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  • 9
    Electronic Resource
    Electronic Resource
    IV. Molecular biology of S-layers (1997)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology reviews 20 (1997), S. 0 
    Details
    ISSN: 1574-6976
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In this chapter we report on the molecular biology of crystalline surface layers of different bacterial groups. The limited information indicates that there are many variations on a common theme. Sequence variety, antigenic diversity, gene expression, rearrangements, influence of environmental factors and applied aspects are addressed. There is considerable variety in the S-layer composition, which was elucidated by sequence analysis of the corresponding genes. In Corynebacterium glutamicum one major cell wall protein is responsible for the formation of a highly ordered, hexagonal array. In contrast, two abundant surface proteins form the S-layer of Bacillus anthracis. Each protein possesses three S-layer homology motifs and one protein could be a virulence factor. The antigenic diversity and ABC transporters are important features, which have been studied in methanogenic archaea. The expression of the S-layer components is controlled by three genes in the case of Thermus thermophilus. One has repressor activity on the S-layer gene promoter, the second codes for the S-layer protein. The rearrangement by reciprocal recombination was investigated in Campylobacter fetus. 7–8 S-layer proteins with a high degree of homology at the 5′ and 3′ ends were found. Environmental changes influence the surface properties of Bacillus stearothermophilus. Depending on oxygen supply, this species produces different S-layer proteins. Finally, the molecular bases for some applications are discussed. Recombinant S-layer fusion proteins have been designed for biotechnology.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6976.1997.tb00304.x
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  • 10
    Electronic Resource
    Electronic Resource
    VI. Applications of S-layers (1997)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology reviews 20 (1997), S. 0 
    Details
    ISSN: 1574-6976
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The wealth of information existing on the general principle of S-layers has revealed a broad application potential. The most relevant features exploited in applied S-layer research are: (i) pores passing through S-layers show identical size and morphology and are in the range of ultrafiltration membranes; (ii) functional groups on the surface and in the pores are aligned in well-defined positions and orientations and accessible for binding functional molecules in very precise fashion; (iii) isolated S-layer subunits from many organisms are capable of recrystallizing as closed monolayers onto solid supports at the air-water interface, on lipid monolayers or onto the surface of liposomes. Particularly their repetitive physicochemical properties down to the subnanometer scale make S-layers unique structures for functionalization of surfaces and interfaces down to the ultimate resolution limit. The following review focuses on selected applications in biotechnology, diagnostics, vaccine development, biomimetic membranes, supramolecular engineering and nanotechnology. Despite progress in the characterization of S-layers and the exploitation of S-layers for the applications described in this chapter, it is clear that the field lags behind others (e.g. enzyme engineering) in applying recent advances in protein engineering. Genetic modification and targeted chemical modification would allow several possibilities including the manipulation of pore permeation properties, the introduction of switches to open and close the pores, and the covalent attachment to surfaces or other macromolecules through defined sites on the S-layer protein. The application of protein engineering to S-layers will require the development of straightforward expression systems, the development of simple assays for assembly and function that are suitable for the rapid screening of numerous mutants and the acquisition of structural information at atomic resolution. Attention should be given to these areas in the coming years.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6976.1997.tb00306.x
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