S-Layer Protein Self-Assembly

Pum, Dietmar; Toca-Herrera, José L.; Sleytr, Uwe B.

doi:10.3390/ijms14022484

Cited by 111 publications

(107 citation statements)

References 95 publications

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“…S-layer proteins (SLPs) are endowed with a crystallization domain that, when purified and examined in isolation, promotes self-assembly of crystalline arrays (113, 124). A broad range of bacteria and archaea assemble S-layers as their outermost envelope component (4, 39, 133).…”

Section: Figurementioning

confidence: 99%

Assembly and Function of the Bacillus anthracis S-Layer

Missiakas

Schneewind

2017

Annu. Rev. Microbiol.

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Bacillus anthracis, the anthrax agent, is a member of the Bacillus cereus sensu lato group, which includes invasive pathogens of mammals or insects as well as nonpathogenic environmental strains. The genes for anthrax pathogenesis are located on two large virulence plasmids. Similar virulence plasmids have been acquired by other B. cereus strains and enable the pathogenesis of anthrax-like diseases. Among the virulence factors of B. anthracis is the S-layer-associated protein BslA, which endows bacilli with invasive attributes for mammalian hosts. BslA surface display and function are dependent on the bacterial S-layer, whose constituents assemble by binding to the secondary cell wall polysaccharide (SCWP) via S-layer homology (SLH) domains. B. anthracis and other pathogenic B. cereus isolates harbor genes for the secretion of S-layer proteins, for S-layer assembly, and for synthesis of the SCWP. We review here recent insights into the assembly and function of the S-layer and the SCWP.

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Section: Figurementioning

confidence: 99%

Assembly and Function of the Bacillus anthracis S-Layer

Missiakas

Schneewind

2017

Annu. Rev. Microbiol.

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“…[15][16][17][18] These biosupramolecular structures have already been studied in a wide range of environments and solid suports. [19][20][21][22][23][24] Moreover, S-layer technology has moved on in the last decade in the synthesis and development of S-layer fusion proteins, which represents a big step in nanobiotechnology 25,26 and constitutes a promising field in surface 2D nanofunctionalization. [27][28][29][30][31] The aim of our work was to investigate the interaction between some of the varieties of lactic acid based polymers of different physicochemical properties (e.g., crystallinity, mechanical properties, etc.)…”

Section: Introdutionmentioning

confidence: 99%

Making novel bio-interfaces through bacterial protein recrystallization on biocompatible polylactide derivative films

Lejardi

Eleta-Lopez

Sarasua

et al. 2013

The Journal of Chemical Physics

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Fabrication of novel bio-supramolecular structures was achieved by recrystallizing the bacterial surface protein SbpA on amorphous and semicrystalline polylactide derivatives. Differential scanning calorimetry showed that the glass transition temperature (T(g)) for (poly-L-lactide)-PLLA, poly(L,D-lactide)-PDLLA, poly(lactide-co-glycolide)-PLGA and poly(lactide-co-caprolactone)-PLCL was 63 °C, 53 °C, 49 °C and 15 °C, respectively. Tensile stress-strain tests indicated that PLLA, PLGA, and PDLLA had a glassy behaviour when tested below T(g). The obtained Young modulus were 1477 MPa, 1330 MPa, 1306 MPa, and 9.55 MPa for PLLA, PLGA, PDLLA, and PLCL, respectively. Atomic force microscopy results confirmed that SbpA recrystallized on every polymer substrate exhibiting the native S-layer P4 lattice (a = b = 13 nm, γ = 90°). However, the polymer substrate influenced the domain size of the S-protein crystal, with the smallest size for PLLA (0.011 μm(2)), followed by PDLLA (0.034 μm(2)), and PLGA (0.039 μm(2)), and the largest size for PLCL (0.09 μm(2)). quartz crystal microbalance with dissipation monitoring (QCM-D) measurements indicated that the adsorbed protein mass per unit area (~1800 ng cm(-2)) was independent of the mechanical, thermal, and crystalline properties of the polymer support. The slowest protein adsorption rate was observed for amorphous PLCL (the polymer with the weakest mechanical properties and lowest T(g)). QCM-D also monitored protein self-assembly in solution and confirmed that S-layer formation takes place in three main steps: adsorption, self-assembly, and crystal reorganization. Finally, this work shows that biodegradable polylactide derivatives films are a suitable support to form robust biomimetic S-protein layers.

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“…While SecA2 and SlaP are required for efficient secretion of mCherry hybrids encompassing the signal peptide and SLH domains of Sap, SlaQ functions to promote secretion of mCherry hybrids that include the C-terminal crystallization domain. Work with S-layer proteins from several different bacteria, including B. anthracis Sap, demonstrated the propensity of crystallization domains to rapidly assemble into two-dimensional paracrystalline lattices (4,5,57). Factors that promote the assembly of S-layer proteins have not yet been reported.…”

Section: Figmentioning

confidence: 99%

Bacillus anthracis SlaQ Promotes S-Layer Protein Assembly

Nguyen-Mau

Schneewind

et al. 2015

J Bacteriol

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Bacillus anthracis vegetative forms assemble an S-layer comprised of two S-layer proteins, Sap and EA1. A hallmark of S-layer proteins are their C-terminal crystallization domains, which assemble into a crystalline lattice once these polypeptides are deposited on the bacterial surface via association between their N-terminal S-layer homology domains and the secondary cell wall polysaccharide. Here we show that slaQ, encoding a small cytoplasmic protein conserved among pathogenic bacilli elaborating S-layers, is required for the efficient secretion and assembly of Sap and EA1. S-layer protein precursors cosediment with SlaQ, and SlaQ appears to facilitate Sap assembly. Purified SlaQ polymerizes and when mixed with purified Sap promotes the in vitro formation of tubular S-layer structures. A model is discussed whereby SlaQ, in conjunction with S-layer secretion factors SecA2 and SlaP, promotes localized secretion and S-layer assembly in B. anthracis. IMPORTANCES-layer proteins are endowed with the propensity for self-assembly into crystalline arrays. Factors promoting S-layer protein assembly have heretofore not been reported. We identified Bacillus anthracis SlaQ, a small cytoplasmic protein that facilitates S-layer protein assembly in vivo and in vitro.

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S-Layer Protein Self-Assembly

Cited by 111 publications

References 95 publications

Assembly and Function of the Bacillus anthracis S-Layer

Assembly and Function of the Bacillus anthracis S-Layer

Making novel bio-interfaces through bacterial protein recrystallization on biocompatible polylactide derivative films

Bacillus anthracis SlaQ Promotes S-Layer Protein Assembly

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