Siphophage 0105phi7-2 of Bacillus thuringiensis: Novel Propagation, DNA, and Genome-Implied Assembly
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Published:2023-05-18
Issue:10
Volume:24
Page:8941
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ISSN:1422-0067
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Container-title:International Journal of Molecular Sciences
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language:en
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Short-container-title:IJMS
Author:
Roberts Samantha M.1, Aldis Miranda1, Wright Elena T.2, Gonzales Cara B.3ORCID, Lai Zhao4, Weintraub Susan T.2, Hardies Stephen C.2, Serwer Philip2ORCID
Affiliation:
1. Department of Microbiology, Immunology and Molecular Genetics, UT Health, San Antonio, TX 78229, USA 2. Department of Biochemistry and Structural Biology, UT Health, San Antonio, TX 78229, USA 3. Department of Comprehensive Dentistry, UT Health, San Antonio, TX 78229, USA 4. Department of Molecular Medicine, UT Health, San Antonio, TX 78229, USA
Abstract
Diversity of phage propagation, physical properties, and assembly promotes the use of phages in ecological studies and biomedicine. However, observed phage diversity is incomplete. Bacillus thuringiensis siphophage, 0105phi-7-2, first described here, significantly expands known phage diversity, as seen via in-plaque propagation, electron microscopy, whole genome sequencing/annotation, protein mass spectrometry, and native gel electrophoresis (AGE). Average plaque diameter vs. plaque-supporting agarose gel concentration plots reveal unusually steep conversion to large plaques as agarose concentration decreases below 0.2%. These large plaques sometimes have small satellites and are made larger by orthovanadate, an ATPase inhibitor. Phage head–host-cell binding is observed by electron microscopy. We hypothesize that this binding causes plaque size-increase via biofilm evolved, ATP stimulated ride-hitching on motile host cells by temporarily inactive phages. Phage 0105phi7-2 does not propagate in liquid culture. Genomic sequencing/annotation reveals history as temperate phage and distant similarity, in a virion-assembly gene cluster, to prototypical siphophage SPP1 of Bacillus subtilis. Phage 0105phi7-2 is distinct in (1) absence of head-assembly scaffolding via either separate protein or classically sized, head protein-embedded peptide, (2) producing partially condensed, head-expelled DNA, and (3) having a surface relatively poor in AGE-detected net negative charges, which is possibly correlated with observed low murine blood persistence.
Funder
NIH-NCI NIH Shared Instrument CPRIT Core Facility Award UT Health, San Antonio University of Texas System Proteomics Core Network
Subject
Inorganic Chemistry,Organic Chemistry,Physical and Theoretical Chemistry,Computer Science Applications,Spectroscopy,Molecular Biology,General Medicine,Catalysis
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