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  • 1
    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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  • 2
    Electronic Resource
    Electronic Resource
    Crystalline bacterial cell surface layers (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 10 (1993), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Crystalline arrays of proteinaceous subunits forming surface layers (S-layers) are one of the most commonly observed prokaryotic cell envelope structures. They are ubiquitous amongst Gram-positive and Gram-negative archaeobacteria and eubacteria and, if present, account for the major protein species produced by the cells. S-layers can provide organisms with a selection advantage by providing various functions including protective coats, molecular sieves, ion traps and structures involved in cell surface interactions. S-layers were identified as contributing to virulence when present as a structural component of pathogens. In Gram-negative archaeobacteria they are involved in determining cell shape and cell division. The crystalline arrays reveal a broad-application potential in biotechnology, vaccine development and molecular nanotechnology.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1993.tb00962.x
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  • 3
    Electronic Resource
    Electronic Resource
    The three S-layer-like homology motifs of the S-layer protein SbpA of Bacillus sphaericus CCM 2177 are not sufficient for binding to the pyruvylated secondary cell wall polymer (2005)
    Oxford, UK : Blackwell Publishing Ltd.
    Molecular microbiology 55 (2005), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The S-layer protein SbpA of Bacillus sphaericus CCM 2177 recognizes a pyruvylated secondary cell wall polymer (SCWP) as anchoring structure to the peptidoglycan-containing layer. Data analysis from surface plasmon resonance (SPR) spectroscopy revealed the existence of three different binding sites with high, medium and low affinity for rSbpA on SCWP immobilized to the sensor chip. The shortest C-terminal truncation with specific affinity to SCWP was rSbpA31-318. Surprisingly, rSbpA31-202 comprising the three S-layer-like homology (SLH) motifs did not bind at all. Analysis of the SbpA sequence revealed a 58-amino-acid-long SLH-like motif starting 11 amino acids after the third SLH motif. The importance of this motif for reconstituting the functional SCWP-binding domain was further demonstrated by construction of a chimaeric protein consisting of the SLH domain of SbsB, the S-layer protein of Geobacillus stearothermophilus PV72/p2 and the C-terminal part of SbpA. In contrast to SbsB or its SLH domain which did not recognize SCWP of B. sphaericus CCM 2177 as binding site, the chimaeric protein showed specific affinity. Deletion of 213 C-terminal amino acids of SbpA had no impact on the square (p4) lattice structure, whereas deletion of 350 amino acids was linked to a change in lattice type from square to oblique (p1).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2004.04351.x
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  • 4
    Electronic Resource
    Electronic Resource
    Heterologous reattachment of regular arrays of glycoproteins on bacterial surfaces (1975)
    [s.l.] : Nature Publishing Group
    Nature 257 (1975), S. 400-402 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] I have examined the ability of isolated subunits to reattach to cell surfaces to understand more fully the mechanisms involved in the development and maintenance of a two-dimensional array of macromolecules on a growing cell surface, and to obtain evidence for the suggestion that the assembly of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/257400a0
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  • 5
    Electronic Resource
    Electronic Resource
    Synthesis of cadmium sulphide superlattices using self-assembled bacterial S-layers (1997)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 389 (1997), S. 585-587 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Methods for organizing materials at the nanometre scale have advanced tremendously in recent years,. One important objective is the synthesis of patterned arrays of inorganic nanocrystals, whose optical, electronic and magnetic properties might find technological uses, for example as memory ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/39287
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  • 6
    Electronic Resource
    Electronic Resource
    I. Basic and applied S-layer research: an overview (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: S-layers are crystalline monomolecular assemblies of protein or glycoprotein, which represent one of the most common cell surface structures in Archaea and Bacteria. As porous lattices completely covering the cell surface they can provide prokaryotic cells with selection advantages by functioning as protective coats, as structures involved in cell adhesion and surface recognition, as molecule or ion traps, and molecular sieves. In Archaea, which possess S-layers as exclusive cell wall component, the (glyco)protein lattices function as cell shape determining/maintaining framework. Studies on structure, chemistry, genetics, assembly and function of S-layers revealed a considerable application potential for the regular arrays in biotechnology, biomimetics, biomedicine and molecular nanotechnology.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6976.1997.tb00301.x
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  • 7
    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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  • 8
    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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  • 9
    Electronic Resource
    Electronic Resource
    Ultrafiltration membranes with uniform pores from crystalline bacterial cell envelope layers (1986)
    Springer
    Applied microbiology and biotechnology 25 (1986), S. 83-90 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01982829
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  • 10
    Electronic Resource
    Electronic Resource
    Reversible cross-linking of crystalline bacterial surface layer glycoproteins through their glycan chains (1993)
    Springer
    Applied microbiology and biotechnology 40 (1993), S. 7-11 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract After periodate oxidation and incubation with dithiodipropionic acid dihydrazide cross-linking of the crystalline surface layer (S-layer) glycoproteins of Clostridium thermohydrosulfuricum L111-69 and Bacillus alvei CCM 2051 was achieved specifically through the glycan chains. The cross-linked S-layers were used for the immobilization of chemically synthesized, spacer-linked, tumour-associated T-disaccharide [βGal(1→3)αGalNAc]. Electron microscopical evaluation of the resulting conjugates showed densely packed, multilayered S-layer structures loaded with the immobilized ligand. After reductive cleavage of the disulphide bond of dithiodipropionic acid by dithiothreitol, monomeric haptenated S-layer conjugates could be obtained. Both the cross-linked and the monomeric type of conjugate might be useful for assessment of specific immune responses, which, in general, can be elicited by those artificial antigens.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00170420
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