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Published on: December 29, 2015
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A prophage-encoded actin-like protein required for efficient viral DNA replication in bacteria
Catriona Donovan1, Antonia Heyer2, Eugen Pfeifer2
1Department of Biology I, Ludwig-Maximilians-University Munich, Großhaderner Str. 2-4, 82152 Planegg-Martinsried, Germany Institute for Biochemistry, University of Cologne, Zülpicherstr. 47, 50674 Cologne, Germany.
Nucleic Acids Research
|April 29, 2015
Summary
A newly discovered actin-like protein, AlpC, and its adaptor AlpA are essential for efficient viral replication in Corynebacterium glutamicum. These proteins organize phage DNA with actin filaments, mirroring eukaryotic viral strategies.
Area of Science:
- Microbiology
- Molecular Biology
- Structural Biology
Background:
- Viral replication relies on precise subcellular localization within host cells.
- Viruses utilize host cytoskeletal elements, like actin, for intracellular transport and positioning.
Purpose of the Study:
- To investigate the role of a prophage-encoded actin-like protein (AlpC) and its associated protein (AlpA) in viral replication.
- To elucidate the mechanism of intracellular organization during viral replication in Corynebacterium glutamicum.
Main Methods:
- Biochemical characterization of AlpC as an actin-like protein.
- Cell biological analysis of AlpC filament formation and AlpA-DNA interaction.
- Transcriptome and quantitative PCR (qPCR) analyses to assess gene expression and mutant phenotypes.
Main Results:
- AlpC functions as a bona fide actin-like protein, forming filaments upon prophage induction.
- AlpA links phage DNA to AlpC filaments, facilitating spatio-temporal organization.
- Both AlpA and AlpC are crucial for efficient prophage replication, with their genes being early induced.
Conclusions:
- The AlpAC system is vital for the spatio-temporal organization of viral replication in bacteria.
- This mechanism shares similarities with actin-mediated viral strategies in eukaryotes, suggesting conserved evolutionary principles in intracellular transport.
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