Genome Annotation and Intraviral Interactome for the Streptococcus pneumoniae Virulent Phage Dp-1

Author:

Sabri Mourad1,Häuser Roman23,Ouellette Marc4,Liu Jing5,Dehbi Mohammed56,Moeck Greg5,García Ernesto7,Titz Björn8,Uetz Peter3,Moineau Sylvain1

Affiliation:

1. Département de Biochimie, de Microbiologie et Bio-Informatiques, Faculté des Sciences et de Génie, Groupe de Recherche en Écologie Buccale, Faculté de Médecine Dentaire, Félix d'Hérelle Reference Center for Bacterial Viruses, Université Laval, Québec, Canada G1V 0A6

2. Institute of Toxicology and Genetics, Karlsruhe Institute for Technology, Karlsruhe, Germany

3. J. Craig Venter Institute, Rockville, Maryland

4. Centre de Recherche en Infectiologie de l'Université Laval, Centre Hospitalier Universitaire de Québec, Québec, Canada G1V 4G2

5. The Medicines Company, Ville St. Laurent, Quebec, Canada

6. Present address: Biochemistry & Molecular Biology Unit, Dasman Diabetes Institute, Dasman, Kuwait.

7. Centro de Investigaciones Biológicas, CSIC, Madrid, Spain

8. Crump Institute for Molecular Imaging, Los Angeles, California

Abstract

ABSTRACT Streptococcus pneumoniae causes several diseases, including pneumonia, septicemia, and meningitis. Phage Dp-1 is one of the very few isolated virulent S. pneumoniae bacteriophages, but only a partial characterization is currently available. Here, we confirmed that Dp-1 belongs to the family Siphoviridae . Then, we determined its complete genomic sequence of 56,506 bp. It encodes 72 open reading frames, of which 44 have been assigned a function. We have identified putative promoters, Rho-independent terminators, and several genomic clusters. We provide evidence that Dp-1 may be using a novel DNA replication system as well as redirecting host protein synthesis through queuosine-containing tRNAs. Liquid chromatography-mass spectrometry analysis of purified phage Dp-1 particles identified at least eight structural proteins. Finally, using comprehensive yeast two-hybrid screens, we identified 156 phage protein interactions, and this intraviral interactome was used to propose a structural model of Dp-1.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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