Complete Genome Sequence of Bacteriophage BC-611 Specifically Infecting Enterococcus faecalis Strain NP-10011

Horiuchi, Tomohiro; Sakka, Makiko; Hayashi, Atsushi; Shimada, Takashi; Kimura, Tetsuya; Sakka, Kazuo

doi:10.1128/jvi.01424-12

Cited by 14 publications

(16 citation statements)

References 11 publications

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“…The Listeria phages and VD13 have the same aspect and approximately the same dimensions ( Table 2). The VD13 genome closely resembles those of two preliminarily described Enterococcus phages (38,39). Together, with a bootstrap support value of 100, these three Enterococcus phages form orthocluster VI (Fig.…”

Section: Genomes Of Newly Sequencedmentioning

confidence: 62%

“…For example, phages isolated in North America (sequenced in this study) clustered with phages isolated in Europe (A511, P100, and P70) (15,29,30) and in East Asia (SAP6 and BC-611) (38,39). Three orthoclusters (orthoclusters I, V, and VI, all lytic) each contained phages isolated on different continents.…”

Section: Discussionmentioning

confidence: 73%

“…Importantly, members of orthoclusters V and VI have been reported to be lytic phages (15,17,38,39). They may thus prove useful for phage-based applications, e.g., for the control and detection of L. monocytogenes and as potential therapeutics for E. faecalis.…”

Section: Discussionmentioning

confidence: 99%

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Comparative Genomic and Morphological Analyses of Listeria Phages Isolated from Farm Environments

Denes

Vongkamjan

Ackermann

et al. 2014

Appl Environ Microbiol

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The genus Listeria is ubiquitous in the environment and includes the globally important food-borne pathogen Listeria monocytogenes. While the genomic diversity of Listeria has been well studied, considerably less is known about the genomic and morphological diversity of Listeria bacteriophages. In this study, we sequenced and analyzed the genomes of 14 Listeria phages isolated mostly from New York dairy farm environments as well as one related Enterococcus faecalis phage to obtain information on genome characteristics and diversity. We also examined 12 of the phages by electron microscopy to characterize their morphology. These Listeria phages, based on gene orthology and morphology, together with previously sequenced Listeria phages could be classified into five orthoclusters, including one novel orthocluster. One orthocluster (orthocluster I) consists of largegenome (ϳ135-kb) myoviruses belonging to the genus "Twort-like viruses," three orthoclusters (orthoclusters II to IV) contain small-genome (36-to 43-kb) siphoviruses with icosahedral heads, and the novel orthocluster V contains medium-sized-genome (ϳ66-kb) siphoviruses with elongated heads. A novel orthocluster (orthocluster VI) of E. faecalis phages, with medium-sized genomes (ϳ56 kb), was identified, which grouped together and shares morphological features with the novel Listeria phage orthocluster V. This new group of phages (i.e., orthoclusters V and VI) is composed of putative lytic phages that may prove to be useful in phage-based applications for biocontrol, detection, and therapeutic purposes.

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Section: Genomes Of Newly Sequencedmentioning

confidence: 62%

Section: Discussionmentioning

confidence: 73%

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Comparative Genomic and Morphological Analyses of Listeria Phages Isolated from Farm Environments

Denes

Vongkamjan

Ackermann

et al. 2014

Appl Environ Microbiol

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“…Running BLASTN with whole genome sequence showed that the isolated IME-EF1 was highly homologous to Enterococcus phage SAP6 (GenBank Accession Number JF731128), with a coverage of 87%, and Enterococcus phage BC-611 (DDBJ Accession Number AB712291), with a coverage of 81%, both of which also belong to Siphoviridae family and were isolated in South Korea and Japan, respectively. Numerous studies on several other E. faecalis bacteriophage have been reported, such as EFAP-1, phiFL1-3, EFRM31, EfaCPT1 (Beheshti et al, GenBank Accession Number JX193904), EF24c, EF11, SAP6, and BC-611, which have been thoroughly genetically characterized [ 17 – 23 ]. However, IME-EF1 has high similarity to SAP6 and BC-611 ( Figure 2A ).…”

Section: Resultsmentioning

confidence: 99%

Characterization of Enterococcus faecalis Phage IME-EF1 and Its Endolysin

Zhang

Yin

et al. 2013

PLoS ONE

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Enterococcus faecalis is increasingly becoming an important nosocomial infection opportunistic pathogen. E. faecalis can easily obtain drug resistance, making it difficult to be controlled in clinical settings. Using bacteriophage as an alternative treatment to drug-resistant bacteria has been revitalized recently, especially for fighting drug-resistant bacteria. In this research, an E. faecalis bacteriophage named IME-EF1 was isolated from hospital sewage. Whole genomic sequence analysis demonstrated that the isolated IME-EF1 belong to the Siphoviridae family, and has a linear double-stranded DNA genome consisting of 57,081 nucleotides. The IME-EF1 genome has a 40.04% G+C content and contains 98 putative coding sequences. In addition, IME-EF1 has an isometric head with a width of 35 nm to 60 nm and length of 75 nm to 90 nm, as well as morphology resembling a tadpole. IME-EF1 can adsorb to its host cells within 9 min, with an absorbance rate more than 99% and a latent period time of 25 min. The endolysin of IME-EF1 contains a CHAP domain in its N-terminal and has a wider bactericidal spectrum than its parental bacteriophage, including 2 strains of vancomycin-resistant E. faecalis. When administrated intraperitoneally, one dose of IME-EF1 or its endolysin can reduce bacterial count in the blood and protected the mice from a lethal challenge of E. faecalis, with a survival rate of 60% or 80%, respectively. Although bacteriophage could rescue mice from bacterial challenge, to the best of our knowledge, this study further supports the potential function of bacteriophage in dealing with E. faecalis infection in vivo. The results also indicated that the newly isolated bacteriophage IME-EF1 enriched the arsenal library of lytic E. faecalis bacteriophages and presented another choice for phage therapy in the future.

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“…T ailed bacteriophages (Caudovirales) address the problem of enabling their progeny to exit the cells that they infect by synthesizing lytic enzymes (endolysins) that degrade the bacterial cell wall and lead to cell lysis (1)(2)(3)(4)(5)(6)(7) The bacteriophages that infect strains of Enterococcus faecalis are no exception. Of the more than forty tailed E. faecalis bacteriophages that have been described (8) (see Table S1 in the supplemental material), genomic sequencing analysis has enabled the presumptive identification of the genes coding for endolysins in eighteen: phages 1 (9), FL1A, FL1B, and FL1C (10), EFAP-1 (11), EF24C (12), Ef11 (13), EF62 (14), BC-611 (15), SAP6 (16), EfaCPT1 (GenBank accession no. AFO10817 [17]), F168/08 and F170/08 (18), IME-EF1 (19), IME-EF3 (20), EFC-1 (21), EFDG1 (22), and EFLK1 (23).…”

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confidence: 99%

Bacteriophage φEf11 ORF28 Endolysin, a Multifunctional Lytic Enzyme with Properties Distinct from All Other Identified Enterococcus faecalis Phage Endolysins

Zhang

Buttaro

Fouts

et al. 2019

Appl Environ Microbiol

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Ef11 is a temperate Siphoviridae bacteriophage that infects strains of Enterococcus faecalis. The Ef11 genome, encompassing 65 open reading frames (ORFs), is contained within 42,822 bp of DNA. Within this genome, a module of six lysis-related genes was identified. Based upon sequence homology, one of these six genes, ORF28, was predicted to code for an N-acetylmuramoyl-Lalanine amidase endolysin of 46.133 kDa, composed of 421 amino acids. The PCRamplified ORF28 was cloned and expressed, and the resulting gene product was affinity purified to homogeneity. The purified protein was obtained from a fusion protein that exhibited a molecular mass of 72.5 kDa, consistent with a 46.1-kDa protein combined with a fused 26.5-kDa glutathione S-transferase tag. It produced rapid, profound lysis in E. faecalis populations and was active against 73 of 103 (71%) E. faecalis strains tested. In addition, it caused substantial destruction of E. faecalis biofilms. The lysin was quite stable, retaining its activity for three years in refrigerated storage, was stable over a wide range of pHs, and was unaffected by the presence of a reducing agent; however, it was inhibited by increasing concentrations of Ca 2ϩ . Liquid chromatography-mass spectrometry analysis of E. faecalis cell wall digestion products produced by the ORF28 endolysin indicated that the lysin acted as an N-acetylmuramidase, an endo-␤-N-acetylglucosaminidase, and an endopeptidase, rather than an N-acetylmuramoyl-L-alanine amidase. The Ef11 ORF28 lysin shared 10% to 37% amino acid identity with the lytic enzymes of all other characterized E. faecalis bacteriophages. IMPORTANCE The emergence of multidrug-resistant pathogenic microorganisms has brought increasing attention to the urgent need for the development of alternative antimicrobial strategies. One such alternative to conventional antibiotics employs lytic enzymes (endolysins) that are produced by bacteriophages in the course of lytic infection. During lytic infection by a bacteriophage, these enzymes hydrolyze the cell wall peptidoglycan, resulting in the lysis of the host cell. However, external endolysin application can result in lysis from without. In this study, we have cloned, expressed, purified, and characterized an endolysin produced by a bacteriophage infecting strains of Enterococcus faecalis. The lysin is broadly active against most of the tested E. faecalis strains and exhibits multifunctional enzymatic specificities that differ from all other characterized endolysins produced by E. faecalis bacteriophages.

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Complete Genome Sequence of Bacteriophage BC-611 Specifically Infecting Enterococcus faecalis Strain NP-10011

Cited by 14 publications

References 11 publications

Comparative Genomic and Morphological Analyses of Listeria Phages Isolated from Farm Environments

Comparative Genomic and Morphological Analyses of Listeria Phages Isolated from Farm Environments

Characterization of Enterococcus faecalis Phage IME-EF1 and Its Endolysin

Bacteriophage φEf11 ORF28 Endolysin, a Multifunctional Lytic Enzyme with Properties Distinct from All Other Identified Enterococcus faecalis Phage Endolysins

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