Novel Acinetobacter baumannii Myovirus TaPaz Encoding Two Tailspike Depolymerases: Characterization and Host-Recognition Strategy

Shchurova, Anastasia S; Shneider, Mikhail M.; Arbatsky, Nikolay P.; Shashkov, Alexander S.; Chizhov, Alexander O.; Skryabin, Yury P.; Mikhaylova, Yulia; Sokolova, Olga; Shelenkov, Andrey; Miroshnikov, Konstantin A.; Knirel, Yuriy A.; Popova, Anastasiya V.

doi:10.3390/v13060978

Cited by 10 publications

(28 citation statements)

References 35 publications

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“…Considering that bacteriophage Aristophanes forms plaques without visible halos, unlike other A. baumannii phages of the family Autographiviridae , and the purified protein Aristophanes_gp41 forms very weak halo on the bacterial lawn of the host strain in comparison with previously described tailspike depolymerases [ 4 , 5 , 7 , 8 , 9 , 10 , 11 ] we assumed that the mechanism of Aristophanes_gp41 interaction with K26 capsular polysaccharides is not based on total cleavage of CPS to monomers or oligomers of the K unit. To elucidate the exact mechanism of action of Aristophanes_gp41, K26 CPS of A. baumannii KZ1098 was treated with the purified protein, and the resultant modified polysaccharide (MPS) was studied by NMR spectroscopy.…”

Section: Resultsmentioning

confidence: 99%

“…A. baumannii strains can produce a vast variety of capsular polysaccharides (CPSs) which serve as primary receptors for the majority of phages that carry genes encoding polysaccharide-degrading enzymes [ 4 , 5 , 6 , 7 , 8 , 9 , 10 , 11 ]. The structures of A. baumannii CPSs are very diverse, comprising above 140 capsular types (K types) have been predicted bioinformatically (J.J. Kenyon, Queensland University of Technology, Brisbane, Australia, personal communication).…”

Section: Introductionmentioning

confidence: 99%

“…The structures of A. baumannii CPSs are very diverse, comprising above 140 capsular types (K types) have been predicted bioinformatically (J.J. Kenyon, Queensland University of Technology, Brisbane, Australia, personal communication). To date, there are descriptions of depolymerase-carrying bacteriophages specifically infecting A. baumannii strains belonging to 15 various K types [ 4 , 5 , 7 , 8 , 9 , 10 , 11 , 12 ].…”

Section: Introductionmentioning

confidence: 99%

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Novel Acinetobacter baumannii Bacteriophage Aristophanes Encoding Structural Polysaccharide Deacetylase

Timoshina

Shneider

Evseev

et al. 2021

Viruses

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Acinetobacter baumannii appears to be one of the most crucial nosocomial pathogens. A possible component of antimicrobial therapy for infections caused by extremely drug-resistant A. baumannii strains may be specific lytic bacteriophages or phage-derived enzymes. In the present study, we observe the biological features, genomic organization, and phage–host interaction strategy of novel virulent bacteriophage Aristophanes isolated on A. baumannii strain having K26 capsular polysaccharide structure. According to phylogenetic analysis phage Aristophanes can be classified as a representative of a new distinct genus of the subfamily Beijerinckvirinae of the family Autographiviridae. This is the first reported A. baumannii phage carrying tailspike deacetylase, which caused O-acetylation of one of the K26 sugar residues.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Novel Acinetobacter baumannii Bacteriophage Aristophanes Encoding Structural Polysaccharide Deacetylase

Timoshina

Shneider

Evseev

et al. 2021

Viruses

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“…Our hypothesis is that these small viruses (typically 40 Kb), need specialized enzymes (depolymerases) to reach the inner surface receptors and initiate the infection their otherwise too-small tails would not reach. Combining the experimental data of reported Acinetobacter Fri1-like tailspikes with depolymerase activities [6][7][8][9][10] and multiple sequence alignments of their domains, one can appreciate the vast diversity of capsular depolymerases that interact with Acinetobacter hosts, which is known to have 125 different capsule types (Figure 5B). Sequences grouped (cluster) by similarity are expected to behave similarly, while single sequences (like the K38 depolymerase) are unique (Figure 5B).…”

Section: Discussionmentioning

confidence: 99%

“…Although Acinetobacter phages with capsular depolymerases have been found in different taxonomic groups, they were predominantly identified in Fri1virus -like phages. Currently, 17 distinct ACB complex K-specific depolymerases have been identified in phage proteomes (K1–2, K9, K19, K27, K30, K32, K37, K44–45, K47–48, K87, K89, K91, K93 and K116) [ 6 , 7 , 8 , 9 , 10 ].…”

Section: Introductionmentioning

confidence: 99%

Unpuzzling Friunavirus-Host Interactions One Piece at a Time: Phage Recognizes Acinetobacter pittii via a New K38 Capsule Depolymerase

et al. 2021

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Acinetobacter pittii is a species that belong to the Acinetobacter calcoaceticus-baumannii 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 Acinetobacter of different capsular types. Here, we report the isolation of the novel A. pittii-infecting Fri1-like phage vB_Api_3043-K38 (3043-K38) of the Podoviridae 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 Acinetobacter 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 Acinetobacter 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 Acinetobacter.

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Identification and characterization of the capsule depolymerase Dpo27 from phage IME-Ap7 specific to Acinetobacter pittii

Wang,

Liu,

Zhang

et al. 2024

Front. Cell. Infect. Microbiol.

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Among the Acinetobacter genus, Acinetobacter pittii stands out as an important opportunistic infection causative agent commonly found in hospital settings, which poses a serious threat to human health. Recently, the high prevalence of carbapenem-resistant A. pittii isolates has created significant therapeutic challenges for clinicians. Bacteriophages and their derived enzymes are promising therapeutic alternatives or adjuncts to antibiotics effective against multidrug-resistant bacterial infections. However, studies investigating the depolymerases specific to A. pittii strains are scarce. In this study, we identified and characterized a capsule depolymerase, Dpo27, encoded by the bacteriophage IME-Ap7, which targets A. pittii. A total of 23 clinical isolates of Acinetobacter spp. were identified as A. pittii (21.91%, 23/105), and seven A. pittii strains with various K locus (KL) types (KL14, KL32, KL38, KL111, KL163, KL207, and KL220) were used as host bacteria for phage screening. The lytic phage IME-Ap7 was isolated using A. pittii 7 (KL220) as an indicator bacterium and was observed for depolymerase activity. A putative tail fiber gene encoding a polysaccharide-degrading enzyme (Dpo27) was identified and expressed. The results of the modified single-spot assay showed that both A. pittii 7 and 1492 were sensitive to Dpo27, which was assigned the KL220 type. After incubation with Dpo27, A. pittii strain was susceptible to killing by human serum; moreover, the protein displayed no hemolytic activity against erythrocytes. Furthermore, the protein exhibited sustained activity across a wide pH range (5.0–10.0) and at temperatures between 20 and 50°C. In summary, the identified capsule depolymerase Dpo27 holds promise as an alternative treatment for combating KL220-type A. pittii infections.

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Novel Acinetobacter baumannii Myovirus TaPaz Encoding Two Tailspike Depolymerases: Characterization and Host-Recognition Strategy

Cited by 10 publications

References 35 publications

Novel Acinetobacter baumannii Bacteriophage Aristophanes Encoding Structural Polysaccharide Deacetylase

Novel Acinetobacter baumannii Bacteriophage Aristophanes Encoding Structural Polysaccharide Deacetylase

Unpuzzling Friunavirus-Host Interactions One Piece at a Time: Phage Recognizes Acinetobacter pittii via a New K38 Capsule Depolymerase

Identification and characterization of the capsule depolymerase Dpo27 from phage IME-Ap7 specific to Acinetobacter pittii

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