Abstract:We report the genome sequences of
Escherichia
phage C600M2 (length, 88,162 bp; G+C content, 38.98%) and
Escherichia
phage CL1 (length, 87,820 bp; G+C content, 41.32%), which were isolated from a wastewater treatment plant in Qatar. Both
Escherichia
phage C600M2 and
Escherichia
phage CL1 genomes contain 128 protein-coding genes and 26 tRNAs.
“…As summarized in Fig. 1 , in this study, we propose the identical lysin integral to two novel bacteriophages isolated from wastewater 26 as propitious “enzybiotic” with anti-bacterial potential by in silico analysis including molecular docking followed by experimental validation using turbidimetric reduction assay which may mark a new approach in the area of modern environmental biotechnology. Figure 1 Summary of the research study.…”
Lysin of bacteriophages isolated from a particular ecosystem could be inducted as a bio-controlling tool against the inhabiting pathogenic bacterial strains. Our study aims at both experimental and computational characterization of the identical lysin gene product inherent in the genomes of two novel Myoviridae bacteriophages, Escherichia Phage C600M2 (GenBank accession number OK040807, Protein ID: UCJ01465) and Escherichia Phage CL1 (GenBank Genome accession number OK040806.1, Protein ID: UCJ01321) isolated from wastewater collected from the main water treatment plant in Qatar. The lysin protein, evinced to be a globular N-acetyl-muramidase with intrinsic “cd00737: endolysin_autolysin” domain, was further expressed and purified to be experimentally validated by turbidimetric assay for its utility as an anti-bacterial agent. Comprehensive computational analysis revealed that the scrutinized lysin protein shared 85–98% sequence identity with 61 bacteriophages, all native to wastewater allied environments. Despite varied Host Recognition Components encoded in their genomes, the similitude of lysins, suggests its apparent significance in host–pathogen interactions endemic to wastewater environment. The present study substantiates the identical lysin from Escherichia Phage C600M2 and Escherichia Phage CL1 as propitious “enzybiotic”, a hybrid term to describe enzymes analogous to anti-biotics to combat antibiotic-resistant bacteria by in silico analysis and subsequent experimental validation.
“…As summarized in Fig. 1 , in this study, we propose the identical lysin integral to two novel bacteriophages isolated from wastewater 26 as propitious “enzybiotic” with anti-bacterial potential by in silico analysis including molecular docking followed by experimental validation using turbidimetric reduction assay which may mark a new approach in the area of modern environmental biotechnology. Figure 1 Summary of the research study.…”
Lysin of bacteriophages isolated from a particular ecosystem could be inducted as a bio-controlling tool against the inhabiting pathogenic bacterial strains. Our study aims at both experimental and computational characterization of the identical lysin gene product inherent in the genomes of two novel Myoviridae bacteriophages, Escherichia Phage C600M2 (GenBank accession number OK040807, Protein ID: UCJ01465) and Escherichia Phage CL1 (GenBank Genome accession number OK040806.1, Protein ID: UCJ01321) isolated from wastewater collected from the main water treatment plant in Qatar. The lysin protein, evinced to be a globular N-acetyl-muramidase with intrinsic “cd00737: endolysin_autolysin” domain, was further expressed and purified to be experimentally validated by turbidimetric assay for its utility as an anti-bacterial agent. Comprehensive computational analysis revealed that the scrutinized lysin protein shared 85–98% sequence identity with 61 bacteriophages, all native to wastewater allied environments. Despite varied Host Recognition Components encoded in their genomes, the similitude of lysins, suggests its apparent significance in host–pathogen interactions endemic to wastewater environment. The present study substantiates the identical lysin from Escherichia Phage C600M2 and Escherichia Phage CL1 as propitious “enzybiotic”, a hybrid term to describe enzymes analogous to anti-biotics to combat antibiotic-resistant bacteria by in silico analysis and subsequent experimental validation.
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