Use of Lectins to Characterize the Receptor Sites for Bacteriophage PL-1 of Lactobacillus casei

Ishibashi, Kazuko; Takesue, Shigeshi; Watanabe, Kenji; Ōishi, Kunio

doi:10.1099/00221287-128-10-2251

Cited by 16 publications

(14 citation statements)

References 26 publications

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“…The uniform distribution of fluorescence suggests the ligands for gp16 binding are not localized in any particular part of the cell but regularly distributed on the cell surface. These observations are consistent with J-1 and PL-1 recognizing saccharide-containing receptors within the outer layer of the cell wall, including a role for L-rhamnose as noted previously (67)(68)(69).…”

Section: Resultssupporting

confidence: 79%

Exposing the Secrets of Two Well-Known Lactobacillus casei Phages, J-1 and PL-1, by Genomic and Structural Analysis

Dieterle

Bowman

Batthyány

et al. 2014

Appl Environ Microbiol

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c Bacteriophage J-1 was isolated in 1965 from an abnormal fermentation of Yakult using Lactobacillus casei strain Shirota, and a related phage, PL-1, was subsequently recovered from a strain resistant to J-1. Complete genome sequencing shows that J-1 and PL-1 are almost identical, but PL-1 has a deletion of 1.9 kbp relative to J-1, resulting in the loss of four predicted gene products involved in immunity regulation. The structural proteins were identified by mass spectrometry analysis. Similarly to phage A2, two capsid proteins are generated by a translational frameshift and undergo proteolytic processing. The structure of gene product 16 (gp16), a putative tail protein, was modeled based on the crystal structure of baseplate distal tail proteins (Dit) that form the baseplate hub in other Siphoviridae. However, two regions of the C terminus of gp16 could not be modeled using this template. The first region accounts for the differences between J-1 and PL-1 gp16 and showed sequence similarity to carbohydratebinding modules (CBMs). J-1 and PL-1 GFP-gp16 fusions bind specifically to Lactobacillus casei/paracasei cells, and the addition of L-rhamnose inhibits binding. J-1 gp16 exhibited a higher affinity than PL-1 gp16 for cell walls of L. casei ATCC 27139 in phage adsorption inhibition assays, in agreement with differential adsorption kinetics observed for both phages in this strain. The data presented here provide insights into how Lactobacillus phages interact with their hosts at the first steps of infection.

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Section: Resultssupporting

confidence: 79%

Exposing the Secrets of Two Well-Known Lactobacillus casei Phages, J-1 and PL-1, by Genomic and Structural Analysis

Dieterle

Bowman

Batthyány

et al. 2014

Appl Environ Microbiol

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“…EPS, specifically heteropolysaccharides, of lactobacilli have been reported to be involved in various biological functions, such as phage absorption (14,15), adhesion to human cells or to other bacteria (16,17), and immunomodulation (18,19). Various studies have employed gene deletion mutation of EPS-associated genes as a strategy to investigate the biological roles of EPS.…”

mentioning

confidence: 99%

Strain-Specific Features of Extracellular Polysaccharides and Their Impact on Lactobacillus plantarum-Host Interactions

Lee

Caggianiello

Swam

et al. 2016

Appl Environ Microbiol

110

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Lactobacilli are found in diverse environments and are widely applied as probiotic, health-promoting food supplements. Polysaccharides are ubiquitously present on the cell surface of lactobacilli and are considered to contribute to the species-and strainspecific probiotic effects that are typically observed. Two Lactobacillus plantarum strains, SF2A35B and Lp90, have an obvious ropy phenotype, implying high extracellular polysaccharide (EPS) production levels. In this work, we set out to identify the genes involved in EPS production in these L. plantarum strains and to demonstrate their role in EPS production by gene deletion analysis. A model L. plantarum strain, WCFS1, and its previously constructed derivative that produced reduced levels of EPS were included as reference strains. The constructed EPS-reduced derivatives were analyzed for the abundance and sugar compositions of their EPS, revealing cps2-like gene clusters in SF2A35B and Lp90 responsible for major EPS production. Moreover, these mutant strains were tested for phenotypic characteristics that are of relevance for their capacity to interact with the host epithelium in the intestinal tract, including bacterial surface properties as well as survival under the stress conditions encountered in the gastrointestinal tract (acid and bile stress). In addition, the Toll-like receptor 2 (TLR2) signaling and immunomodulatory capacities of the EPS-negative derivatives and their respective wild-type strains were compared, revealing strain-specific impacts of EPS on the immunomodulatory properties. Taken together, these experiments illustrate the importance of EPS in L. plantarum strains as a strain-specific determinant in host interaction. IMPORTANCEThis study evaluates the role of extracellular polysaccharides that are produced by different strains of Lactobacillus plantarum in the determination of the cell surface properties of these bacteria and their capacity to interact with their environment, including their signaling to human host cells. The results clearly show that the consequences of removal of these polysaccharides are very strain specific, illustrating the diverse and unpredictable roles of these polysaccharides in the environmental interactions of these bacterial strains. In the context of the use of lactobacilli as health-promoting probiotic organisms, this study exemplifies the importance of strain specificity.

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“…The cell walls were separated by disrupting the Lactobacillus casei cells and purified by differential centrifugation and enzyme treatment as described by Ishibashi et a1 5 ) Preparation of phage DNA and plasmid pBR322. Phage DNA was separated by the cold phenol method of Kirby,6) and the DNA concentration was determined by measuring the optical density at 260 nm.…”

Section: Methodsmentioning

confidence: 99%

Mechanism ofIn VitroInactivation ofLactobacillusPhage PL-1 byd-Glucosamine

Watanabe¹,

Sasaki²,

Kashige³

et al. 1985

Agricultural and Biological Chemistry

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Use of Lectins to Characterize the Receptor Sites for Bacteriophage PL-1 of Lactobacillus casei

Cited by 16 publications

References 26 publications

Exposing the Secrets of Two Well-Known Lactobacillus casei Phages, J-1 and PL-1, by Genomic and Structural Analysis

Exposing the Secrets of Two Well-Known Lactobacillus casei Phages, J-1 and PL-1, by Genomic and Structural Analysis

Strain-Specific Features of Extracellular Polysaccharides and Their Impact on Lactobacillus plantarum-Host Interactions

Mechanism ofIn VitroInactivation ofLactobacillusPhage PL-1 byd-Glucosamine

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