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Phage Phenomics: Physiological Approaches to Characterize Novel Viral Proteins
Published on: June 11, 2015
Novel Acinetobacter baumannii Myovirus TaPaz Encoding Two Tailspike Depolymerases: Characterization and
Anastasia S Shchurova1,2, Mikhail M Shneider3, Nikolay P Arbatsky4
1Moscow Institute of Physics and Technology (National Research University), Institutskiy per. 9, Dolgoprudny, 141700 Moscow Region, Russia.
Abstract:
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.
Insights
A novel bacteriophage, TaPaz, was isolated and studied. Its tailspike depolymerases show potential for targeting specific Acinetobacter baumannii capsular polysaccharide types, offering new avenues for combating this nosocomial pathogen.
Area of Science:
- Microbiology
- Virology
- Biochemistry
Background:
- Acinetobacter baumannii is a major cause of hospital-acquired infections.
- Bacteriophages targeting A. baumannii are crucial for controlling infections.
- Capsular polysaccharides (CPSs) are key receptors for bacteriophages and influence bacterial virulence.
Purpose of the Study:
- To characterize the novel myovirus TaPaz infecting A. baumannii.
- To investigate the genomic organization and host interaction strategies of TaPaz.
- To identify and evaluate the function of TaPaz's polysaccharide-degrading enzymes.
Main Methods:
- Isolation and characterization of bacteriophage TaPaz.
- Genome sequencing and analysis of TaPaz.
- Purification and biochemical testing of recombinant tailspike depolymerases (TSDs).
Main Results:
- TaPaz possesses a 93,703 bp double-stranded DNA genome with 178 open reading frames.
- Two distinct tailspike depolymerase genes were identified within the TaPaz genome.
- One recombinant TSD specifically cleaved the K47 capsular polysaccharide of A. baumannii via hydrolysis.
Conclusions:
- The novel myovirus TaPaz offers insights into A. baumannii-phage interactions.
- TaPaz encodes specific polysaccharide-degrading enzymes with potential therapeutic applications.
- The characterized tailspike depolymerase demonstrates targeted activity against K47 A. baumannii strains.
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