Analysis of S-layer proteins of<i>Lactobacillus brevis</i>

Yasui, Tetsuji; Yoda, Kumiko; Kamiya, Tomoya

doi:10.1111/j.1574-6968.1995.tb07881.x

Cited by 36 publications

(5 citation statements)

References 9 publications

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“…2). S-layer protein from L. brevis JCM 1059 was not stained, as (14) was expected for a non-glycosylated protein (Yasui et al 1995).…”

Section: Pas Stainingmentioning

confidence: 84%

“…We previously reported variations in molecular mass of S-layer proteins from 20 L. kefir strains isolated from kefir grains, with Mr ranging from 66 to 71 kDa (Garrote et al 2004), a common trait also found for S-layer proteins from different strains of Lactobacillus acidophilus (Masuda 1992), L. brevis (Yasui et al 1995) and Clostridium difficile (McCoubrey and Poxton 2001).…”

Section: Discussionmentioning

confidence: 97%

“…After that, gels were treated with 20 ml of Schiff's reagent until magenta bands appeared and then with 0.2% Na 2 S 2 O 5 in 5% acetic acid for 60 min. S-layer proteins from L. brevis JCM 1059 were used as non-glycosylated control (Yasui et al 1995).…”

Section: Periodic Acid-schiff (Pas) Reactionmentioning

confidence: 99%

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Heterogeneity of S-layer proteins from aggregating and non-aggregating Lactobacillus kefir strains

Mobili

Serradell

Trejo

et al. 2009

Antonie van Leeuwenhoek

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Since the presence of S-layer protein conditioned the autoaggregation capacity of some strains of Lactobacillus kefir, S-layer proteins from aggregating and non-aggregating L. kefir strains were characterized by immunochemical reactivity, MALDI-TOF spectrometry and glycosylation analysis. Two anti-S-layer monoclonal antibodies (Mab5F8 and Mab1F8) were produced; in an indirect enzyme-linked immunosorbent assay Mab1F8 recognized S-layer proteins from all L. kefir tested while Mab5F8 recognized only S-layer proteins from aggregating strains. Periodic Acid-Schiff staining of proteins after polyacrylamide gel electrophoresis under denaturing conditions revealed that all L. kefir S-layer proteins tested were glycosylated. Growth of bacteria in the presence of the N-glycosylation inhibitor tunicamycin suggested the presence of glycosydic chains O-linked to the protein backbone. MALDI-TOF peptide map fingerprint for S-layer proteins from 12 L. kefir strains showed very similar patterns for the aggregating strains, different from those for the non-aggregating ones. No positive match with other protein spectra in MSDB Database was found. Our results revealed a high heterogeneity among S-layer proteins from different L. kefir strains but also suggested a correlation between the structure of these S-layer glycoproteins and the aggregation properties of whole bacterial cells.

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“…2). S-layer protein from L. brevis JCM 1059 was not stained, as (14) was expected for a non-glycosylated protein (Yasui et al 1995).…”

Section: Pas Stainingmentioning

confidence: 84%

Section: Discussionmentioning

confidence: 97%

See 1 more Smart Citation

Heterogeneity of S-layer proteins from aggregating and non-aggregating Lactobacillus kefir strains

Mobili

Serradell

Trejo

et al. 2009

Antonie van Leeuwenhoek

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“…The presence of the S-layer protein decreases the susceptibility of L. helveticus ATCC 12046 to mutanolysin (Lortal et al 1992), the susceptibility of L. acidophilus M92 to gastric and pancreatic juice (Frece et al 2005) and the susceptibility of L. hilgardii wine isolate B706 to wine-related conditions like the presence of copper sulphate or tannic acid (Dohm et al 2011). On the other hand, the S-layer proteins of brewery isolates of L. brevis were deduced not to act as barriers for the hop bittering substance isohumulone (Yasui et al 1995). The auxiliary S-layer component SlpX of L. acidophilus NCFM probably affects the permeability of the S-layer as the slpX -negative mutant is more susceptible to SDS and more resistant to bile than the wild type (Goh et al 2009).…”

Section: Functions Of Lactobacillus S-layer Proteinsmentioning

confidence: 99%

Lactobacillus surface layer proteins: structure, function and applications

Hynönen

Palva

2013

Appl Microbiol Biotechnol

221

196

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Bacterial surface (S) layers are the outermost proteinaceous cell envelope structures found on members of nearly all taxonomic groups of bacteria and Archaea. They are composed of numerous identical subunits forming a symmetric, porous, lattice-like layer that completely covers the cell surface. The subunits are held together and attached to cell wall carbohydrates by non-covalent interactions, and they spontaneously reassemble in vitro by an entropy-driven process. Due to the low amino acid sequence similarity among S-layer proteins in general, verification of the presence of an S-layer on the bacterial cell surface usually requires electron microscopy. In lactobacilli, S-layer proteins have been detected on many but not all species. Lactobacillus S-layer proteins differ from those of other bacteria in their smaller size and high predicted pI. The positive charge in Lactobacillus S-layer proteins is concentrated in the more conserved cell wall binding domain, which can be either N- or C-terminal depending on the species. The more variable domain is responsible for the self-assembly of the monomers to a periodic structure. The biological functions of Lactobacillus S-layer proteins are poorly understood, but in some species S-layer proteins mediate bacterial adherence to host cells or extracellular matrix proteins or have protective or enzymatic functions. Lactobacillus S-layer proteins show potential for use as antigen carriers in live oral vaccine design because of their adhesive and immunomodulatory properties and the general non-pathogenicity of the species.

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“…First, spores were engineered to express bacterial adhesins at the spore surface by genetic fusion with CotB, a B. subtilis spore coat protein. Two previously known bacterial adhesins known to promote the colonization of the mammalian gastrointestinal tract were employed: the S-layer protein (SlpA) from Lactobacillus brevis and invasin (InvA) expressed by Yersinia pseudotuberculosis (14,15). In a second step, the spores were genetically modified to express at the cell stage a protein fragment (the P1 protein fragment from amino acids 39 to 512 [P1 ]) derived from the P1 antigen (also known as antigen I/II, Pac, or antigen B) and originally expressed by Streptococcus mutans, the causative agent of dental caries, but also found on the surface of different pathogenic streptococci (16)(17)(18).…”

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confidence: 99%

Gut Adhesive Bacillus subtilis Spores as a Platform for Mucosal Delivery of Antigens

et al. 2014

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Bacterial carriers for the mucosal delivery of antigens, particularly those capable of colonizing or invading through the mucosal epithelia, have been intensively investigated (1). Live bacterial vectors can be generated with attenuated pathogens, such as Salmonella and Listeria, or nonpathogenic commensal species, such as Lactococcus and Lactobacillus. Bacteria in the former group of are capable of inducing strong and long-lasting immune responses to passenger antigens but present serious safety concerns, whereas bacteria in the latter group are safer but typically induce much lower immune responses to the passenger antigens (1-3). As a safe nonpathogenic live bacterial vector, Bacillus subtilis, a spore-forming soil Gram-positive bacterial species, has been engineered to express antigens as either vegetative cells or spores (4, 5). As antigen carriers, B. subtilis spores have several attractive features, including a safe record of human and animal use as both probiotic and food additives, remarkable heat resistance, and rather easy genetic and bacteriological manipulation.Currently, two major genetic approaches have been proposed to generate recombinant B. subtilis spores as vaccine delivery vectors. The first approach relies on the expression of a heterologous protein genetically fused to surface-exposed spore coat proteins, such as CotB, CotC, or CotG (6, 7). Such a strategy would allow a better presentation of the passenger antigen to the mucosa-associated lymphoid tissue (MALT) afferent sites, leading to the induction of adaptive immune responses, such as mucosal secretory (IgA) or systemic (IgG) antigen-specific antibody responses (6-8). The second approach is based on a distinct rationale and has employed episomal vectors in which the target antigen is expressed under the control of a promoter (PgsiB) active only at the vegetative cell stage, which means immediately after spore germination (9-11). This antigen delivery approach relies on the fact that B. subtilis spores germinate during transit through the gastrointestinal tract and produce the target antigen at the intestinal lumen or inside the phagocytes of antigen-presenting cells (APCs), leading to the induction of antibody responses in the serum (IgG) and mucosa (fecal IgA) (9-11).However, in both cases, the administration of recombinant spores via mucosal routes typically confers immune responses to the passenger antigen lower than those achieved with delivery systems based on attenuated bacterial strains capable of colonizing the mammalian gastrointestinal tract. The reduced mucosal adjuvant effects of B. subtilis spores have been attributed to several factors, such as a previously established immunity generated by the frequent ingestion of spores, the reduced amount of expressed antigens, and the rapid transit through the gastrointestinal tract, which reduces the chances of a productive interaction with the gut-associated lymphoid tissue (GALT), such as M cells and APCs at Peyer's patches (PPs) (12, 13).In an attempt to improve the performance o...

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Analysis of S-layer proteins ofLactobacillus brevis

Cited by 36 publications

References 9 publications

Heterogeneity of S-layer proteins from aggregating and non-aggregating Lactobacillus kefir strains

Heterogeneity of S-layer proteins from aggregating and non-aggregating Lactobacillus kefir strains

Lactobacillus surface layer proteins: structure, function and applications

Gut Adhesive Bacillus subtilis Spores as a Platform for Mucosal Delivery of Antigens

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