Journal
VIRUSES-BASEL
Volume 13, Issue 6, Pages -Publisher
MDPI
DOI: 10.3390/v13060978
Keywords
bacteriophage; Acinetobacter baumannii; tailspike depolymerase; glycosidase; capsular polysaccharide; capsular type
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Funding
- Russian Science Foundation [20-75-10113]
- Russian Science Foundation [20-75-10113] Funding Source: Russian Science Foundation
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Acinetobacter baumannii is a significant nosocomial pathogen capable of producing structurally diverse capsular polysaccharides, which are targeted by bacteriophages encoding polysaccharide-degrading enzymes. A newly isolated myovirus, TaPaz, was found to infect A. baumannii strains with K47 capsular polysaccharide structure, containing genes for two tailspike depolymerases. One of these depolymerases was shown to specifically cleave the K47 CPS through a hydrolytic mechanism.
Acinetobacter baumannii, one of the most significant nosocomial pathogens, is capable of producing structurally diverse capsular polysaccharides (CPSs) which are the primary receptors for A. baumannii bacteriophages encoding polysaccharide-degrading enzymes. To date, bacterial viruses specifically infecting A. baumannii strains belonging to more than ten various capsular types (K types) were isolated and characterized. In the present study, we investigate the biological properties, genomic organization, and virus-bacterial host interaction strategy of novel myovirus TaPaz isolated on the bacterial lawn of A. baumannii strain with a K47 capsular polysaccharide structure. The phage linear double-stranded DNA genome of 93,703 bp contains 178 open reading frames. Genes encoding two different tailspike depolymerases (TSDs) were identified in the phage genome. Recombinant TSDs were purified and tested against the collection of A. baumannii strains belonging to 56 different K types. One of the TSDs was demonstrated to be a specific glycosidase that cleaves the K47 CPS by the hydrolytic mechanism.
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