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BtuB-Dependent Infection of the T5-like Yersinia Phage ϕR2-01.
Happonen, Lotta J; Pajunen, Maria I; Jun, Jin Woo; Skurnik, Mikael.
Affiliation
  • Happonen LJ; Division of Infection Medicine, Department of Clinical Sciences Lund, Lund University, 22184 Lund, Sweden.
  • Pajunen MI; Department of Bacteriology and Immunology, Medicum, Human Microbiome Research Program, Faculty of Medicine, University of Helsinki, 00290 Helsinki, Finland.
  • Jun JW; Department of Aquaculture, Korea National College of Agriculture and Fisheries, Jeonju 54874, Korea.
  • Skurnik M; Department of Bacteriology and Immunology, Medicum, Human Microbiome Research Program, Faculty of Medicine, University of Helsinki, 00290 Helsinki, Finland.
Viruses ; 13(11)2021 10 28.
Article in En | MEDLINE | ID: mdl-34834977
ABSTRACT
Yersinia enterocolitica is a food-borne Gram-negative pathogen responsible for several gastrointestinal disorders. Host-specific lytic bacteriophages have been increasingly used recently as an alternative or complementary treatment to combat bacterial infections, especially when antibiotics fail. Here, we describe the proteogenomic characterization and host receptor identification of the siphovirus vB_YenS_ϕR2-01 (in short, ϕR2-01) that infects strains of several Yersinia enterocolitica serotypes. The ϕR2-01 genome contains 154 predicted genes, 117 of which encode products that are homologous to those of Escherichia bacteriophage T5. The ϕR2-01 and T5 genomes are largely syntenic, with the major differences residing in areas encoding hypothetical ϕR2-01 proteins. Label-free mass-spectrometry-based proteomics confirmed the expression of 90 of the ϕR2-01 genes, with 88 of these being either phage particle structural or phage-particle-associated proteins. In vitro transposon-based host mutagenesis and ϕR2-01 adsorption experiments identified the outer membrane vitamin B12 receptor BtuB as the host receptor. This study provides a proteogenomic characterization of a T5-type bacteriophage and identifies specific Y. enterocolitica strains sensitive to infection with possible future applications of ϕR2-01 as a food biocontrol or phage therapy agent.
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Full text: 1 Database: MEDLINE Main subject: Membrane Transport Proteins / Bacterial Outer Membrane Proteins / Bacterial Proteins / Yersinia / Siphoviridae Language: En Journal: Viruses Year: 2021 Type: Article Affiliation country: Sweden

Full text: 1 Database: MEDLINE Main subject: Membrane Transport Proteins / Bacterial Outer Membrane Proteins / Bacterial Proteins / Yersinia / Siphoviridae Language: En Journal: Viruses Year: 2021 Type: Article Affiliation country: Sweden