Role of S-layer proteins in bacteria

Gerbino, Esteban; Carasi, Paula; Mobili, Pablo; Serradell, María de los Ángeles; Gómez-Zavaglia, Andrea

doi:10.1007/s11274-015-1952-9

Cited by 91 publications

(67 citation statements)

References 92 publications

(95 reference statements)

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“…It has been proposed that the S-layer plays a role as a protective sheath and that it may protect the bacterial cell from various environmental factors such as mechanical and osmotic stresses in Lactobacillus (Hynönen and Palva 2013;Gerbino et al 2015). The need for the cell to increase S-layer gene expression is related to the integrity of the cell envelope structure.…”

Section: Discussionmentioning

confidence: 99%

“…S-layers are arrays of a single protein that constitutes the outermost cell envelope and have been considered to function as protective coats, maintenance of cell shape, and adhesion to specific hosts (Avall-Jääskeläinen and Palva 2005; Hynönen and Palva 2013;Gerbino et al 2015). In addition, we have recently shown that the S-layer of Lactobacillus acidophilus has antibacterial endopeptidase activity and antiviral functions (Prado-Acosta et al 2008Martínez et al 2012).…”

Section: Introductionmentioning

confidence: 99%

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Influence of osmotic stress on the profile and gene expression of surface layer proteins in Lactobacillus acidophilus ATCC 4356

Palomino

Waehner

Martin

et al. 2016

Appl Microbiol Biotechnol

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In this work, we studied the role of surface layer (S-layer) proteins in the adaptation of Lactobacillus acidophilus ATCC 4356 to the osmotic stress generated by high salt. The amounts of the predominant and the auxiliary S-layer proteins SlpA and SlpX were strongly influenced by the growth phase and high-salt conditions (0.6 M NaCl). Changes in gene expression were also observed as the mRNAs of the slpA and slpX genes increased related to the growth phase and presence of high salt. A growth stage-dependent modification on the S-layer protein profile in response to NaCl was observed: while in control conditions, the auxiliary SlpX protein represented less than 10 % of the total S-layer protein, in high-salt conditions, it increased to almost 40 % in the stationary phase. The increase in S-layer protein synthesis in the stress condition could be a consequence of or a way to counteract the fragility of the cell wall, since a decrease in the cell wall thickness and envelope components (peptidoglycan layer and lipoteichoic acid content) was observed in L. acidophilus when compared to a non-S-layer-producing species such as Lactobacillus casei. Also, the stationary phase and growth in high-salt medium resulted in increased release of S-layer proteins to the supernatant medium. Overall, these findings suggest that pre-growth in high-salt conditions would result in an advantage for the probiotic nature of L. acidophilus ATCC 4356 as the increased amount and release of the S-layer might be appropriate for its antimicrobial capacity.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Influence of osmotic stress on the profile and gene expression of surface layer proteins in Lactobacillus acidophilus ATCC 4356

Palomino

Waehner

Martin

et al. 2016

Appl Microbiol Biotechnol

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“…S-layers provide a protective barrier for microorganisms, protecting them from a wide array of environmental threats, including high temperatures, low pHs, gamma radiation, and metals (23). The B. sphaericus strain JG-A12 S-layer has been shown to bind a wide range of metals cations, including U(VI).…”

Section: Discussionmentioning

confidence: 99%

A Highly Expressed High-Molecular-Weight S-Layer Complex of Pelosinus sp. Strain UFO1 Binds Uranium

Thorgersen

Lancaster

Rajeev

et al. 2017

Appl Environ Microbiol

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Cell suspensions of Pelosinus sp. strain UFO1 were previously shown, using spectroscopic analysis, to sequester uranium as U(IV) complexed with carboxyl and phosphoryl group ligands on proteins. The goal of our present study was to characterize the proteins involved in uranium binding. Virtually all of the uranium in UFO1 cells was associated with a heterodimeric protein, which was termed the uranium-binding complex (UBC). The UBC was composed of two S-layer domain proteins encoded by UFO1_4202 and UFO1_4203. Samples of UBC purified from the membrane fraction contained 3.3 U atoms/heterodimer, but significant amounts of phosphate were not detected. The UBC had an estimated molecular mass by gel filtration chromatography of 15 MDa, and it was proposed to contain 150 heterodimers (UFO1_4203 and UFO1_4202) and about 500 uranium atoms. The UBC was also the dominant extracellular protein, but when purified from the growth medium, it contained only 0.3 U atoms/heterodimer. The two genes encoding the UBC were among the most highly expressed genes within the UFO1 genome, and their expressions were unchanged by the presence or absence of uranium. Therefore, the UBC appears to be constitutively expressed and is the first line of defense against uranium, including by secretion into the extracellular medium. Although S-layer proteins were previously shown to bind U(VI), here we showed that U(IV) binds to S-layer proteins, we identified the proteins involved, and we quantitated the amount of uranium bound.IMPORTANCE Widespread uranium contamination from industrial sources poses hazards to human health and to the environment. Herein, we identified a highly abundant uranium-binding complex (UBC) from Pelosinus sp. strain UFO1. The complex makes up the primary protein component of the S-layer of strain UFO1 and binds 3.3 atoms of U(IV) per heterodimer. While other bacteria have been shown to bind U(VI) on their S-layer, we demonstrate here an example of U(IV) bound by an S-layer complex. The UBC provides a potential tool for the microbiological sequestration of uranium for the cleaning of contaminated environments.KEYWORDS contamination, uranium sequestration, uranium-binding protein U ranium is highly toxic and is also a radionuclide with a long half-life (1). Uranium mining, milling, and other anthropogenic industrial activities have led to widespread environmental contamination with associated hazards to human health and to the environment (2). In the United States, the U.S. Department of Energy (DOE) oversees the monitoring and restoration of waste sites at 12 facilities contaminated with uranium (3). Uranium is present in oxic fresh water as highly soluble U(VI). At pH values lower than 5.0, U(VI) is predominantly found as the free uranyl ion (UO 2 2ϩ ), and between pH values of 5.0 and 7.5, U(VI) is predominantly complexed with carbonate. At pH values

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“…S-layers are arrays of a single protein that constitutes the outermost cell envelope and have been considered to function as protective coats, maintenance of cell shape, and adhesion to specific hosts [1][2][3]. These proteins are present in some Lactobacillus species that are normal inhabitants of the oral and genital cavities and the gastrointestinal tract of humans and animals and also have been isolated from plants and food products.…”

Section: Accepted Manuscript Introductionmentioning

confidence: 99%

“…These lattices could function as protective agents against a hostile environment, as molecular sieves and ion traps, as structures involved in cell adhesion, surface recognition and inhibition of pathogens [1][2][3].…”

Section: Accepted Manuscript Introductionmentioning

confidence: 99%

A glycoproteomic approach reveals that the S-layer glycoprotein of Lactobacillus kefiri CIDCA 83111 is O- and N-glycosylated

Cavallero

Malamud

Casabuono

et al. 2017

Journal of Proteomics

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In Gram-positive bacteria, such as lactic acid bacteria, general glycosylation systems have not been documented so far. The aim of this work was to characterize in detail the glycosylation of the S-layer protein of Lactobacillus kefiri CIDCA 83111. A reductive elimination treatment followed by anion exchange high performance liquid chromatography analysis was useful to characterize the O-glycosidic structures. MALDI-TOF mass spectrometry analysis confirmed the presence of oligosaccharides bearing from 5 to 8 glucose units carrying galacturonic acid. Further nanoHPLC-ESI analysis of the glycopeptides showed two O-glycosylated peptides: the peptide sequence SSASSASSA already identified as a signature glycosylation motif in L. buchneri, substituted on average with eight glucose residues and decorated with galacturonic acid and another Oglycosylated site on peptide 471-476, with a Glc 5-8 GalA 2 structure. As ten characteristic sequons (Asn-X-Ser/Thr) are present in the S-layer amino acid sequence, we performed a PNGase F digestion to release N-linked oligosaccharides. Anion exchange chromatography analysis showed mainly short N-linked chains. NanoHPLC-ESI in the positive and negative ion modes were useful to determine two different peptides substituted with short N-glycan structures. To our knowledge, this is the first description of the structure of N-glycans in Slayer glycoproteins from Lactobacillus species.

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Role of S-layer proteins in bacteria

Cited by 91 publications

References 92 publications

Influence of osmotic stress on the profile and gene expression of surface layer proteins in Lactobacillus acidophilus ATCC 4356

Influence of osmotic stress on the profile and gene expression of surface layer proteins in Lactobacillus acidophilus ATCC 4356

A Highly Expressed High-Molecular-Weight S-Layer Complex of Pelosinus sp. Strain UFO1 Binds Uranium

A glycoproteomic approach reveals that the S-layer glycoprotein of Lactobacillus kefiri CIDCA 83111 is O- and N-glycosylated

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