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Penetration of membrane-containing double-stranded-DNA bacteriophage PM2 into Pseudoalteromonas hosts
Hanna M Kivelä1, Rimantas Daugelavicius, Riina H Hankkio
1Faculty of Biosciences and Institute of Biotechnology, University of Helsinki, Finland.
Abstract:
The icosahedral bacteriophage PM2 has a circular double-stranded DNA (dsDNA) genome and an internal lipid membrane. It is the only representative of the Corticoviridae family. How the circular supercoiled genome residing inside the viral membrane is translocated into the gram-negative marine Pseudoalteromonas host has been an intriguing question. Here we demonstrate that after binding of the virus to an abundant cell surface receptor, the protein coat is most probably dissociated. During the infection process, the host cell outer membrane becomes transiently permeable to lipophilic gramicidin D molecules proposing fusion with the viral membrane. One of the components of the internal viral lipid core particle is the integral membrane protein P7, with muralytic activity that apparently aids the process of peptidoglycan penetration. Entry of the virion also causes a limited depolarization of the cytoplasmic membrane. These phenomena differ considerably from those observed in the entry process of bacteriophage PRD1, a dsDNA virus, which uses its internal membrane to make a cell envelope-penetrating tubular structure.
Insights
Bacteriophage PM2 infection involves protein coat dissociation and viral membrane fusion with the host cell outer membrane. The P7 protein aids peptidoglycan penetration, differing from other dsDNA viruses like PRD1.
Area of Science:
- Microbiology
- Virology
- Molecular Biology
Background:
- Bacteriophage PM2, the sole member of the Corticoviridae family, possesses a unique icosahedral structure with a circular double-stranded DNA genome and an internal lipid membrane.
- The mechanism of genome translocation into gram-negative marine Pseudoalteromonas hosts remains poorly understood.
Purpose of the Study:
- To elucidate the entry mechanism of bacteriophage PM2 into its host cell.
- To investigate the roles of viral components and host cell interactions during infection.
Main Methods:
- Observational studies on viral binding and host cell interactions.
- Analysis of membrane permeability changes using lipophilic molecules like gramicidin D.
- Assessment of cytoplasmic membrane depolarization.
- Comparative analysis with bacteriophage PRD1 entry.
Main Results:
- Viral binding to cell surface receptors triggers protein coat dissociation.
- Host outer membrane transiently becomes permeable, suggesting viral-host membrane fusion.
- Integral membrane protein P7 exhibits muralytic activity, facilitating peptidoglycan penetration.
- Virion entry induces limited cytoplasmic membrane depolarization.
Conclusions:
- Bacteriophage PM2 employs a distinct entry mechanism involving membrane fusion and specific protein-mediated penetration.
- This mechanism differs significantly from the tubular structure formation used by bacteriophage PRD1.
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