Genetic and biochemical characterization of the Lactobacillus delbrueckii subsp. lactis bacteriophage LL-H lysin

Vasala, Antti; Välkkilä, Merja; Caldentey, Javier; Alatossava, Tapani

doi:10.1128/aem.61.11.4004-4011.1995

Cited by 50 publications

(22 citation statements)

References 64 publications

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“…We searched the L. johnsoni genomic sequence dataset with bacteriophage sequences of known Lactobacillus, Lactococcus, Streptococcus, and Bacillus phages using the BLAST algorithm. As first screening probes we used bacteriophage LL-H, Accession Number M96254 (Vasala et al, 1995), bacteriophage SPP1 complete nucleotide sequence, X97918 (Becker et al, 1997), B. subtilis DNA (28-kb PBSX/skin element region) Z70177 (Krogh et al, 1996), Lactobacillus bacteriophage phig1e complete genomic DNA, X98106 (Kodaira et al, 1997), and S. thermophilus bacteriophage Sfi21, Sfi19, and Sfi11 complete genomes (Lucchini et al, 1999b).…”

Section: Sequence Analysismentioning

confidence: 99%

Comparative Genomics of the Late Gene Cluster from Lactobacillus Phages

2000

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Three prophage sequences were identified in the Lactobacillus johnsoni strain NCC533. Prophage Lj965 predicted a gene map very similar to those of pac-site Streptococcus thermophilus phages over its DNA packaging and head and tail morphogenesis modules. Sequence similarity linked the putative DNA packaging and head morphogenesis genes at the protein level. Prophage Lj965/S. thermophilus phage Sfi11/Lactococcus lactis phage TP901-1 on one hand and Lactobacillus delbrueckii phage LL-H/Lactobacillus plantarum phage phig1e/Listeria monocytogenes phage A118 on the other hand defined two sublines of structural gene clusters in pac-site Siphoviridae from low-GC Gram-positive bacteria. Bacillus subtilis phage SPP1 linked both sublines. The putative major head and tail proteins from Lj965 shared weak sequence similarity with phages from Gram-negative bacteria. A clearly independent line of structural genes in Siphoviridae from low-GC Gram-positive bacteria is defined by temperate cos-site phages including Lactobacillus gasseri phage adh, which also shared sequence similarity with phage D3 infecting a Gram-negative bacterium. A phylogenetic tree analysis demonstrated that the ClpP-like protein identified in four cos-site Siphoviridae from Lactobacillus, Lactococcus, Streptococcus, and Pseudomonas showed graded sequence relationships. The tree suggested that the ClpP-like proteins from the phages were not acquired by horizontal gene transfer from their corresponding bacterial hosts.

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Section: Sequence Analysismentioning

confidence: 99%

Comparative Genomics of the Late Gene Cluster from Lactobacillus Phages

2000

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“…c). The highest lytic activity was observed in the presences of 250 mM NaCl, similar to that seen with many other lysins (Vasala et al ., ; Loeffler et al ., ; Schmelcher et al ., ). This may be an advantage of this endolysin, as these ionic conditions correspond to the salt concentration of many food products.…”

Section: Resultsmentioning

confidence: 99%

Characterization of an endolysin, LysBPS13, from a Bacillus cereus bacteriophage

Park

Yun

Lim

et al. 2012

FEMS Microbiol Lett

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Use of bacteriophages as biocontrol agents is a promising tool for controlling pathogenic bacteria including antibiotic-resistant bacteria. Not only bacteriophages but also endolysins, the peptidoglycan hydrolyzing enzymes encoded by bacteriophages, have high potential for applications as biocontrol agents against food-borne pathogens. In this study, a putative endolysin gene was identified in the genome of the bacteriophage BPS13, which infects Bacillus cereus. In silico analysis of this endolysin, designated LysBPS13, showed that it consists of an N-terminal catalytic domain (PGRP domain) and a C-terminal cell wall binding domain (SH3_5 domain). Further characterization of the purified LysBPS13 revealed that this endolysin is an N-acetylmuramyl-l-alanine amidase, the activity of which was not influenced by addition of EDTA. In addition, LysBPS13 demonstrated remarkable thermostability in the presence of glycerol, and it retained its lytic activity even after incubation at 100 °C for 30 min. Taken together, these results indicate that LysBPS13 can be considered a favorable candidate for a new antimicrobial agent to control B. cereus.

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“…Most endolysins of lactic acid bacteria present lytic activity only to related species (Vasala et al. 1995).…”

Section: Discussionmentioning

confidence: 99%

Identification and characterization of the two-component cell lysis cassette encoded by temperate bacteriophageϕPYB5 ofLactobacillus fermentum

Wang

Kong

Zhang

2008

Journal of Applied Microbiology

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Aims: To characterize the two‐component cell lysis cassette comprised of holin (Hyb5) and endolysin (Lyb5) encoded by Lactobacillus fermentum temperate bacteriophage ϕPYB5, and illustrate the potential application of Lyb5 as therapeutic agents. Methods and Results: The hyb5–lyb5 cassette was cloned from the genome library of ϕPYB5, and the hyb5, lyb5 and hyb5–lyb5 cassette were expressed in E. coli BL21, respectively. The molecular weight of Hyb5 indicated by SDS‐PAGE was 19 kDa, and Lyb5 was 45 kDa. Both Hyb5 and Lyb5 protein could induce cell lysis alone, resulting in the leakage of β‐galactosidase. However, the Hyb5–Lyb5 cassette lysed the host cells more rapidly and extensively. By zymogram analysis, Lyb5 exhibited a broad lytic spectrum. Conclusions: Overexpression of hyb5, lyb5 and hyb5–lyb5 cassette were carried out in E. coli and Lyb5 exhibited a broad lytic spectrum. Significance and Impact of the Study: The Lyb5 produced in E. coli exhibited a broad lytic spectrum against Gram‐positive strains including Staphylococcus aureus as well as Gram‐negative strains such as Salmonella typhi, suggesting that Lyb5 provides a potential alternative of diagnostic tools and therapeutic agents.

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Genetic and biochemical characterization of the Lactobacillus delbrueckii subsp. lactis bacteriophage LL-H lysin

Cited by 50 publications

References 64 publications

Comparative Genomics of the Late Gene Cluster from Lactobacillus Phages

Comparative Genomics of the Late Gene Cluster from Lactobacillus Phages

Characterization of an endolysin, LysBPS13, from a Bacillus cereus bacteriophage

Identification and characterization of the two-component cell lysis cassette encoded by temperate bacteriophageϕPYB5 ofLactobacillus fermentum

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