Identification of a newly isolated lytic bacteriophage against K24 capsular type, carbapenem resistant Klebsiella pneumoniae isolates.


Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
03 04 2020
Historique:
received: 07 07 2019
accepted: 17 03 2020
entrez: 5 4 2020
pubmed: 5 4 2020
medline: 15 12 2020
Statut: epublish

Résumé

The increasing incidence of carbapenemase-producing K. pneumoniae strains (CP-Kps) in the last decade has become a serious global healthcare problem. Therapeutic options for the treatment of emerging hospital clones have drastically narrowed and therefore novel approaches must be considered. Here we have isolated and characterized a lytic bacteriophage, named vB_KpnS_Kp13, that was effective against all Verona integron-encoded metallo-β-lactamase (VIM) producing K. pneumoniae isolates originating from hospital samples (urine, blood, sputum and faeces), belonging to the ST15 clonal lineage and expressing the K24 capsule. Morphological characterization of vB_KpnS_Kp13 showed that the newly identified phage belonged to the Siphoviridae family, and phylogenetic analysis showed that it is part of a distinct clade of the Tunavirinae subfamily. Functional analysis revealed that vB_KpnS_Kp13 had relatively short latent period times (18 minutes) compared to other K. pneumoniae bacteriophages and could degrade biofilm by more than 50% and 70% in 24 and 48 hours respectively. Complete in vivo rescue potential of the new phage was revealed in an intraperitoneal mouse model where phages were administered intraperitoneally 10 minutes after bacterial challenge. Our findings could potentially be used to develop specific anti-CP-Kps bacteriophage-based therapeutic strategies against major clonal lineages and serotypes.

Identifiants

pubmed: 32246126
doi: 10.1038/s41598-020-62691-8
pii: 10.1038/s41598-020-62691-8
pmc: PMC7125228
doi:

Substances chimiques

Anti-Bacterial Agents 0
Bacterial Proteins 0
Carbapenems 0
beta-Lactamases EC 3.5.2.6
carbapenemase EC 3.5.2.6

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

5891

Références

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Auteurs

Marianna Horváth (M)

Department of Medical Biology and Central Electron Microscope Laboratory, University of Pécs, Medical School, Pécs, Hungary.
Department of Medical Microbiology and Immunology, University of Pécs, Medical School, Pécs, Hungary.

Tamás Kovács (T)

Department of Biotechnology, Nanophagetherapy Center, Enviroinvest Corporation, Pécs, Hungary.

Sarshad Koderivalappil (S)

Department of Biotechnology, University of Szeged, Szeged, Hungary.

Hajnalka Ábrahám (H)

Department of Medical Biology and Central Electron Microscope Laboratory, University of Pécs, Medical School, Pécs, Hungary.

Gábor Rákhely (G)

Department of Biotechnology, University of Szeged, Szeged, Hungary.
Institute of Biophysics, Biological Research Center, Szeged, Hungary.

György Schneider (G)

Department of Medical Microbiology and Immunology, University of Pécs, Medical School, Pécs, Hungary. schneider.gyorgy@pte.hu.

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