Murein Hydrolase Activity in the Surface Layer of
            <i>Lactobacillus acidophilus</i>
            ATCC 4356

Acosta, Mariano; Palomino, María Mercedes; Allievi, Mariana C.; Rivas, Coralia I.; Ruzal, Sandra M.

doi:10.1128/aem.01712-08

Cited by 39 publications

(34 citation statements)

References 31 publications

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“…17 It has previously been reported that although deletion of the cell wall targeting domain of lysostaphin does not interfere Zymography is a method to detect cell wall hydrolase activity on dead cells impregnated in the SDS-PAGE. 37 Our observations of P301 demonstrating activity only on zymogram gel with no CFU reduction are similar to those of Sass and Bierbaum 38 and Raltson et al 39 for a phage endolysin. It is tempting to speculate that the zymogram positive reaction with the P301 protein could be due to the extended time of exposure (more than 16 h) of the protein to the impregnated substrate while the insignificant activity of P301 in the viability assay (CFU drop) ( Table 1) could be attributed to less exposure of the P301 protein to the live cells (1 h) during the viability assay experimental conditions.…”

Section: Discussionsupporting

confidence: 88%

Properties and mutation studies of a bacteriophage-derived chimeric recombinant staphylolytic protein P128

Saravanan¹,

Paul²,

George³

et al. 2013

Bacteriophage

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Section: Discussionsupporting

confidence: 88%

Properties and mutation studies of a bacteriophage-derived chimeric recombinant staphylolytic protein P128

Saravanan¹,

Paul²,

George³

et al. 2013

Bacteriophage

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“…Concerning the Gram-negative Salmonella enterica, a peculiar behavior was observed: while whole cells suspended in buffer were lysed by the sole presence of S-layer (17), no lytic effect was observed when exponentially growing cultures were treated even with both S-layer and nisin (data not shown). However, the S-layer protein remains intact after incubation with whole cells as observed by Western blotting after 8 h of incubation (Fig.…”

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confidence: 99%

“…For this purpose, the antibacterial activity of S-layer from Lactobacillus acidophilus ATCC 4356, either alone or in combination with nisin, was analyzed using three models of food-borne pathogenic bacteria: Salmonella enterica serovar Newport (10), Staphylococcus aureus ATCC 6538 (used as a representative of Gram-positive bacteria in standard medium tests; laboratory collection), and Bacillus cereus 6A1 (Bacillus Genetic Stock Center [BGSC]). The S-layer proteins were extracted as previously described (17) and conserved as a 1-mg/ml suspension in sterile distilled water at Ϫ20°C until use. Purity was determined by SDS-PAGE as a unique band and detected by Western blotting.…”

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confidence: 99%

Synergistic Effects of the Lactobacillus acidophilus Surface Layer and Nisin on Bacterial Growth

Prado-Acosta

Ruzal

Allievi

et al. 2010

Appl Environ Microbiol

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We have previously described a murein hydrolase activity for the surface layer (S-layer) of Lactobacillus acidophilus ATCC 4356. Here we show that, in combination with nisin, this S-layer acts synergistically to inhibit the growth of pathogenic Gram-negative Salmonella enterica and potential pathogenic Gram-positive bacteria, Staphylococcus aureus and Bacillus cereus. In addition, bacteriolytic effects were observed for the Gram-positive species tested. We postulate that the S-layer enhances the access of nisin into the cell membrane by enabling it to cross the cell wall, while nisin provides the sudden ion-nonspecific dissipation of the proton motive force required to enhance the S-layer murein hydrolase activity.

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“…S-layers have been shown to have roles in the determination and maintenance of cell shape as virulence factors, as mediators of cell adhesion, and as regulators of immature dendritic and T cells. Moreover, they can also function as a protective coat, molecular sieve, murein hydrolase, and ion trap (4,8,13,17,19,25,29).…”

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Surface Location of Individual Residues of SlpA Provides Insight into the Lactobacillus brevis S-Layer

et al. 2009

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Bacterial surface layer (S-layer) proteins are excellent candidates for in vivo and in vitro nanobiotechnological applications because of their ability to self-assemble into two-dimensional lattices that form the outermost layer of many Eubacteria and most Archaea species. Despite this potential, knowledge about their molecular architecture is limited. In this study, we investigated SlpA, the S-layer protein of the potentially probiotic bacterium Lactobacillus brevis ATCC 8287 by cysteine-scanning mutagenesis and chemical modification. We generated a series of 46 mutant proteins by replacing single amino acids with cysteine, which is not present in the wild-type protein. Most of the replaced amino acids were located in the self-assembly domain (residues 179 to 435) that likely faces the outer surface of the lattice. As revealed by electron microscopy, all the mutant proteins were able to form self-assembly products identical to that of the wild type, proving that this replacement does not dramatically alter the protein conformation. The surface accessibility of the sulfhydryl groups introduced was studied with two maleimide-containing marker molecules, TMM(PEG) 12 (molecular weight [MW], 2,360) and AlexaFluor488-maleimide (MW ‫؍‬ 720), using both monomeric proteins in solution and proteins allowed to self-assemble on cell wall fragments. Using the acquired data and available domain information, we assigned the mutated residues into four groups according to their location in the protein monomer and lattice structure: outer surface of the lattice (9 residues), inner surface of the lattice (9), protein interior (12), and protein-protein interface/pore regions (16). This information is essential, e.g., in the development of therapeutic and other health-related applications of Lactobacillus S-layers.Bacterial surface layers (S-layers) are cell envelope structures ubiquitously found in gram-positive and gram-negative bacteria as well as in Archaea. S-layers are composed of identical (glyco)protein subunits with a molecular mass in the range of 40 to 200 kDa. The proteins self-assemble into two-dimensional crystalline structures with oblique (p1, p2), square (p4), or hexagonal (p3, p6) symmetry, covering the entire cell surface. The subunits are held together and attached to the underlying cell wall by noncovalent interactions and they have an intrinsic ability to spontaneously form regular layers in solution and on solid supports (24). S-layers have been shown to have roles in the determination and maintenance of cell shape as virulence factors, as mediators of cell adhesion, and as regulators of immature dendritic and T cells. Moreover, they can also function as a protective coat, molecular sieve, murein hydrolase, and ion trap (4,8,13,17,19,25,29).S-layer proteins have several properties that make them an attractive target for the development of nanobiotechnological applications both in vivo and in vitro. In particular, a high number of protein subunits are displayed at the bacterial cell surface. Moreover, the prot...

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Murein Hydrolase Activity in the Surface Layer of Lactobacillus acidophilus ATCC 4356

Cited by 39 publications

References 31 publications

Properties and mutation studies of a bacteriophage-derived chimeric recombinant staphylolytic protein P128

Properties and mutation studies of a bacteriophage-derived chimeric recombinant staphylolytic protein P128

Synergistic Effects of the Lactobacillus acidophilus Surface Layer and Nisin on Bacterial Growth

Surface Location of Individual Residues of SlpA Provides Insight into the Lactobacillus brevis S-Layer

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