Crystalline Bacterial Cell Surface Layers (S Layers): From Supramolecular Cell Structure to Biomimetics and Nanotechnology

Sleytr, Uwe B.; Messner, Paul; Pum, Dietmar; Sára, Margit

doi:10.1002/(sici)1521-3773(19990419)38:8<1034::aid-anie1034>3.0.co;2-#

Cited by 413 publications

(274 citation statements)

References 108 publications

(144 reference statements)

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“…The strong evidence suggesting that the Dgp products are S-layer glycoproteins reveals a very significant role for these molecules to the bacteria. S-layers are believed to have evolved as a consequence of different and changing ecological conditions, likely providing a selective advantage (9). Indeed, the ability to synthesize a vast assortment of S-layer glycoproteins, coupled with the ability to rapidly and reversibly turn their synthesis ON and OFF, likely provides a survival advantage to these organisms during their lifelong association with the host.…”

Section: Discussionmentioning

confidence: 99%

Phase-variable expression of a family of glycoproteins imparts a dynamic surface to a symbiont in its human intestinal ecosystem

Fletcher

Coyne

Bentley

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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The recent report of the synthesis of glycoproteins by the abundant intestinal symbionts Bacteroides showed that these organisms use a novel bacterial enzyme to decorate their surfaces with a sugar residue derived from their environment. As a first step in understanding the importance of these glycoproteins to the bacteria and to the bacterial-host symbiosis, we identified and characterized the abundant glycoproteins of Bacteroides distasonis Using lectin-affinity purification followed by tandem mass spectrometry, we identified a family of at least nine glycoproteins, similar only to the S-layer glycoproteins of Tannerella forsythia. Analysis of one of these purified glycoproteins demonstrated that the glycan is primarily a polymer of xylose, a monosaccharide rarely found in bacterial glycans. Even more unexpected was the finding that seven of nine of the glycoprotein promoters undergo DNA inversion, a process that we show is active in their endogenous human environment. Using cross-species functional assays, we show that a single serine family site-specific recombinase globally mediates the inversions of these glycoprotein promoters. This regulatory mechanism is similar to that of the Bacteroides fragilis capsular polysaccharides and establishes DNA inversion as a general and ancient means of regulation of glycan-containing surface molecules of these important human intestinal symbionts.

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Section: Discussionmentioning

confidence: 99%

Phase-variable expression of a family of glycoproteins imparts a dynamic surface to a symbiont in its human intestinal ecosystem

Fletcher

Coyne

Bentley

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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“…Crystalline-cell surface layers (S-layers) of prokaryotic organisms are a very potent self-assembly system, which can be used in bottom-up processes as a patterning element for a "biomolecular construction kit". [1][2][3][4][5] The unique property of isolated S-layer protein subunits (monomers) to reassemble into two-dimensional (2D) crystals that are identical to those found on intact bacterial cells, either in suspension, on diverse solid supports, on liposomes, or on various interfaces, opens a wide range of S-layer-based applications. [6][7][8][9] In previous studies, it has been demonstrated that several functional domains introduced into S-layer proteins at distinct positions by genetic engineering do not interfere with the intrinsic self-assembly property of the S-layer system, while simultaneously fully retaining their specific biological properties.…”

Section: Introductionmentioning

confidence: 99%

Recombinant Glycans on an S‐Layer Self‐Assembly Protein: A New Dimension for Nanopatterned Biomaterials

Steiner

Hanreich

Kainz

et al. 2008

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Crucial biological phenomena are mediated through carbohydrates that are displayed in a defined manner and interact with molecular scale precision. We lay the groundwork for the integration of recombinant carbohydrates into a "biomolecular construction kit" for the design of new biomaterials, by utilizing the self-assembly system of the crystalline cell surface (S)-layer protein SgsE of Geobacillus stearothermophilus NRS 2004/3a. SgsE is a naturally O-glycosylated protein, with intrinsic properties that allow it to function as a nanopatterned matrix for the periodic display of glycans. By using a combined carbohydrate/protein engineering approach, two types of S-layer neoglycoproteins are produced in Escherichia coli. Based on the identification of a suitable periplasmic targeting system for the SgsE self-assembly protein as a cellular prerequisite for Europe PMC Funders Author ManuscriptsEurope PMC Funders Author Manuscripts protein glycosylation, and on engineering of one of the natural protein O-glycosylation sites into a target for N-glycosylation, the heptasaccharide from the AcrA protein of Campylobacter jejuni and the O7 polysaccharide of E. coli are co-or post-translationally transferred to the S-layer protein by the action of the oligosaccharyltransferase PglB. The degree of glycosylation of the Slayer neoglycoproteins after purification from the periplasmic fraction reaches completeness. Electron microscopy reveals that recombinant glycosylation is fully compatible with the S-layer protein self-assembly system. Tailor-made ("functional") nanopatterned, self-assembling neoglycoproteins may open up new strategies for influencing and controlling complex biological systems with potential applications in the areas of biomimetics, drug targeting, vaccine design, or diagnostics.

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“…Such a result is consistent with previous reports that deep UV radiation (~190 nm) can be used to degrade organosliane monolayers, 35,36 polysaccharides, 37 and S-layer proteins. 38 It should be noted that the small peak near 280 nm typically found in spectra from bulk BSA solutions does not appear to be present in Figure 3. This is probably due to the very small number of molecules measured at the surface compared with bulk assays.…”

Section: Resultsmentioning

confidence: 96%

“…[31][32][33][34] Additionally, deep UV radiation had been employed to pattern organosilane monolayers, 35,36 polysaccharides, 37 and S-layer proteins. 38 In this paper, we extend this idea to patterning sacrificial adsorbed protein layers at the liquid/solid interface. We show that it is possible to deposit films made from bovine serum albumin (BSA).…”

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confidence: 99%

Multiplexing Ligand−Receptor Binding Measurements by Chemically Patterning Microfluidic Channels

2008

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A method has been designed for patterning supported phospholipid bilayers (SLBs) on planar substrates and inside microfluidic channels. To do this, bovine serum albumin (BSA) monolayers were formed via adsorption at the liquid/solid interface. Next, this interfacial protein film was selectively patterned by using deep UV lithography. Subsequently, SLBs could be deposited in the patterned locations by vesicle fusion. By cycling through this process several times, spatially addressed bilayer arrays could be formed with intervening protein molecules serving as twodimensional corrals. By employing this method, phospholipid bilayers containing various concentrations of ganglioside GM1 were addressed along the length of individual microfluidic channels. Therefore, the binding of GM1 with pentameric cholera toxin B (CTB) subunits could be probed. A seven-channel microfluidic device was fabricated for this purpose. Each channel was simultaneously patterned with four chemically distinct SLBs containing 0, 0.2, 0.5, and 2.0 mol % GM1, respectively. Varying concentrations of CTB were then introduced into each of the channels. With the use of total internal reflection fluorescence microscopy, it was possible to simultaneously abstract multiple equilibrium dissociation constants as a function of ligand density for the CTB-GM1 system in a single shot.Multivalent ligand-receptor interactions are ubiquitous on cell surfaces. They have a wide variety of consequences including the modulation of equilibrium dissociation constants, high receptor selectivity, and receptor clustering. 1 Multivalency can also play a direct role in signal transduction processes. 2 Examination of the underlying thermodynamics of ligandreceptor binding may lead to a greater understanding of its biological role and could provide insight into biomedical applications involving inhibitory drug design. 1,3,4 Unfortunately, high-throughput, low-protein consumption assays are not presently well enough developed in this field to afford rapid, systematic studies of binding data at two-dimensionally fluid bilayer interfaces. 5 In previous work it has been demonstrated that microfluidic devices can be designed for measuring binding affinities in multivalent systems. [5][6][7][8][9][10][11][12][13][14] In our previous setup, ligands were incorporated into supported lipid bilayers (SLBs) coated on the walls and floors of polydimethylsiloxane/glass microchannels. Linear arrays of channels were then monitored by total internal reflection fluorescence microscopy (TIRFM) 15 to obtain equilibrium dissociation constants in one-shot assays. This could be done by using the same surface chemistry in each microchannel while varying the solution concentration of the aqueous proteins. Such a setup made these assays relatively rapid, afforded high accuracy, and used only a few microliters of protein solution. Nevertheless, such platforms could be markedly improved by measuring multiple binding constants with various membrane chemistries simultaneously. This could be achie...

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Crystalline Bacterial Cell Surface Layers (S Layers): From Supramolecular Cell Structure to Biomimetics and Nanotechnology

Cited by 413 publications

References 108 publications

Phase-variable expression of a family of glycoproteins imparts a dynamic surface to a symbiont in its human intestinal ecosystem

Phase-variable expression of a family of glycoproteins imparts a dynamic surface to a symbiont in its human intestinal ecosystem

Recombinant Glycans on an S‐Layer Self‐Assembly Protein: A New Dimension for Nanopatterned Biomaterials

Multiplexing Ligand−Receptor Binding Measurements by Chemically Patterning Microfluidic Channels

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