DNA Replication Mechanisms in Viral Systems
Summary
DNA replication in viral systems encompasses a remarkable variety of strategies that exploit or mimic cellular machinery. Small DNA viruses often encode a multifunctional helicase–primase complex that recognises a discrete origin of replication, unwinds duplex DNA and synthesises RNA primers or directly primes synthesis via a covalently attached protein. Larger DNA viruses, such as herpesviruses and poxviruses, encode their own multi-subunit replisomes that include dedicated polymerases, processivity factors and specialised nuclease activities. In contrast, protein-primed viruses such as adenovirus and bacteriophage φ29 initiate DNA synthesis by using a terminal protein as primer, thereby bypassing the need for conventional RNA primase. Throughout these systems, single-stranded DNA binding proteins stabilise unwound strands, topoisomerases relieve torsional stress and host factors are often co-opted to regulate initiation, elongation and termination. The interplay between viral and host enzymes determines replication speed, fidelity and genome maintenance, with direct consequences for pathogenicity and immune evasion. Insights into these mechanisms have informed antiviral drug discovery, guided the engineering of viral vectors for gene therapy and contributed to fundamental understanding of eukaryotic replication.
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DNA Replication Mechanisms in Viral Systems publication trend
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Technical terms
Origin of replication: A specific DNA sequence at which viral or cellular proteins assemble to initiate DNA synthesis.
Helicase: An enzyme that unwinds double-stranded DNA ahead of the replication fork by hydrolysing nucleotide triphosphates.
Primase: An RNA polymerase that synthesises short RNA primers on single-stranded DNA to provide a 3′ hydroxyl group for DNA polymerase extension.
Okazaki fragments: Short DNA segments synthesised discontinuously on the lagging strand, later processed and ligated into a continuous strand.
Processivity factor: A protein (for example proliferating cell nuclear antigen) that encircles DNA to increase the association time of DNA polymerases during elongation.
Single-stranded DNA-binding protein (RPA): A host or viral protein that binds and stabilises exposed single-stranded DNA to prevent secondary structure formation and nuclease attack.
References
- Proteomics Analysis of the Polyomavirus DNA Replication Initiation Complex Reveals Novel Functional Phosphorylated Residues and Associated Proteins. International Journal of Molecular Sciences (2024).
- Identification of cellular proteins required for simian virus 40 DNA replication. Journal of Biological Chemistry (1989).
- Complete enzymatic synthesis of DNA containing the SV40 origin of replication.. Journal of Biological Chemistry (1988).
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