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|dc.contributor.author||MacKennon K.E. Egan||en_US|
|dc.contributor.author||Htut Htut Htoo||en_US|
|dc.contributor.author||Jason F. Nideffer||en_US|
|dc.contributor.other||Division of Biological Sciences||en_US|
|dc.identifier.citation||Scientific Reports. Vol.10, No.1 (2020)||en_US|
|dc.description.abstract||© 2020, The Author(s). Since the emergence of deadly pathogens and multidrug-resistant bacteria at an alarmingly increased rate, bacteriophages have been developed as a controlling bioagent to prevent the spread of pathogenic bacteria. One of these pathogens, disease-causing Vibrio parahaemolyticus (VPAHPND) which induces acute hepatopancreatic necrosis, is considered one of the deadliest shrimp pathogens, and has recently become resistant to various classes of antibiotics. Here, we discovered a novel vibriophage that specifically targets the vibrio host, VPAHPND. The vibriophage, designated Seahorse, was classified in the family Siphoviridae because of its icosahedral capsid surrounded by head fibers and a non-contractile long tail. Phage Seahorse was able to infect the host in a broad range of pH and temperatures, and it had a relatively short latent period (nearly 30 minutes) in which it produced progeny at 72 particles per cell at the end of its lytic cycle. Upon phage infection, the host nucleoid condensed and became toroidal, similar to the bacterial DNA morphology seen during tetracycline treatment, suggesting that phage Seahorse hijacked host biosynthesis pathways through protein translation. As phage Seahorse genome encodes 48 open reading frames with many hypothetical proteins, this genome could be a potential untapped resource for the discovery of phage-derived therapeutic proteins.||en_US|
|dc.title||A novel vibriophage exhibits inhibitory activity against host protein synthesis machinery||en_US|
|Appears in Collections:||Scopus 2020|
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