Location: Produce Safety and Microbiology Research
Title: Characterization of a newly isolated Dhillonviruses bacteriophage vB_EcoS-UDS3lw with antimicrobial potential against E. coli O157:H7Author
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Liao, Yen-Te |
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ARELLANO, ABIGAIL - Hispanic Association Of Colleges & Universities (HACU) |
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Zhang, Yujie |
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Wu, Vivian |
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Submitted to: BMC Research Notes
Publication Type: Peer Reviewed Journal Publication Acceptance Date: 4/28/2026 Publication Date: N/A Citation: N/A Interpretive Summary: Escherichia coli O157:H7 is a major foodborne pathogen that causes severe illness and remains difficult to eliminate, particularly when it forms a biofilm (aggregated bacterial cells). Therefore, controlling this pathogen in the food industry poses a significant challenge. Lytic bacteriophages (phages) are viruses that kill bacteria and have been recognized as an alternative antimicrobial solution for biofilm control. This study focused on the genomic and biological approaches to characterize a lytic phage, known as vB_EcoS_UDS3lw, against E. coli O157:H7. UDS3lw is a tailed phage with a long non-contractile tail and harbors no lysogenic or toxin genes in its genome. UDS3lw demonstrated enzyme activities against various E. coli O157:H7 strains and generic E. coli. The phage-derived enzyme could enhance the antimicrobial efficacy of biofilm control. These findings suggest UDS3lw has antimicrobial potential for the development of phage-based interventions. Technical Abstract: The complete genome sequence of Escherichia phage vB EcoS UDS3lw consists of double-stranded DNA, with a genome length of 44,071 base pairs and GC content of 54.67%. The phylogenetic analysis on the nucleotide level revealed that a UDS3lw shared a close evolutionary relationship with Escherichia phage SM S22, belonging to the Dhillonvirus genus. Phage UDS3lw has a small burst size of 2.4 PFU/CFU and a narrow spectrum of antimicrobial activity against E. coli O157:H7 and some generic E. coli strains. However, the phage exhibits depolymerase enzyme activity upon infection against most of these E. coli strains; the enzyme, likely deriving from the tail fiber protein (ORF 31), could be further developed as a potential anti-biofilm agent. |
