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

Détails

ID Serval
serval:BIB_F188454F68EC
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Unpuzzling Friunavirus-Host Interactions One Piece at a Time: Phage Recognizes Acinetobacter pittii via a New K38 Capsule Depolymerase.
Périodique
Antibiotics
Auteur⸱e⸱s
Domingues R., Barbosa A., Santos S.B., Pires D.P., Save J., Resch G., Azeredo J., Oliveira H.
ISSN
2079-6382 (Print)
ISSN-L
2079-6382
Statut éditorial
Publié
Date de publication
26/10/2021
Peer-reviewed
Oui
Volume
10
Numéro
11
Pages
1304
Langue
anglais
Notes
Publication types: Journal Article
Publication Status: epublish
Résumé
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.
Mots-clé
Acinetobacter baumannii, anti-virulence, bacteriophage, capsule, depolymerase, tailspike
Pubmed
Web of science
Open Access
Oui
Création de la notice
03/12/2021 12:01
Dernière modification de la notice
30/01/2024 8:20
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