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Unpuzzling Friunavirus-Host Interactions One Piece at a Time: Phage Recognizes via a New K38 Capsule Depolymerase. | LitMetric

AI Article Synopsis

  • The study focuses on a newly isolated phage called 3043-K38 that targets a specific capsule type (K38) in a species known for being resistant to antibiotics and often associated with hospital infections.
  • The phage carries a unique depolymerase enzyme that can break down the protective capsule, making the bacteria more vulnerable to immune attacks.
  • This research emphasizes the potential of using this phage and its depolymerase as a new strategy to combat drug-resistant bacterial infections in clinical settings.

Article Abstract

is a species that belong to the complex, increasingly recognized as major nosocomial bacterial pathogens, often associated with multiple drug-resistances. The capsule surrounding the bacteria represents a main virulence factor, helping cells avoid phage predation and host immunity. Accordingly, a better understanding of the phage infection mechanisms is required to efficiently develop phage therapy against of different capsular types. Here, we report the isolation of the novel -infecting Fri1-like phage vB_Api_3043-K38 (3043-K38) of the morphotype, from sewage samples. Its 41,580 bp linear double-stranded DNA genome harbours 53 open reading frames and 302 bp of terminal repeats. We show that all studied Fri1-like viruses have highly similar genomes, which differentiate only at the genes coding for tailspike, likely to adapt to different host receptors. The isolated phage 3043-K38 specifically recognizes an untapped K38 capsule type via a novel tailspike with K38 depolymerase activity. The recombinant K38 depolymerase region of the tailspike (center-end region) forms a thermostable trimer, and quickly degrades capsules. When the K38 depolymerase is applied to the cells, it makes them resistant to phage predation. Interestingly, while K38 depolymerase treatments do not synergize with antibiotics, it makes bacterial cells highly susceptible to the host serum complement. In summary, we characterized a novel phage-encoded K38 depolymerase, which not only advances our understanding of phage-host interactions, but could also be further explored as a new antibacterial agent against drug-resistant .

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8614642PMC
http://dx.doi.org/10.3390/antibiotics10111304DOI Listing

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