ArticleJournal of virology2018
Crystal Structure of the Dimerized N Terminus of Porcine Circovirus Type 2 Replicase Protein Reveals a Novel Antiviral Interface.
Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- Isolation and characterization of two porcine circovirus type 2 strains from Heilongjiang Province and Inner Mongolia Autonomous Region.Journal of veterinary science · 2026Article
- EZH2 enhances PCV2 replication through inhibition of MMP1 and MMP12 transcription activity.Veterinary research · 2026Article
- Annexin A2 facilitates porcine circovirus type 2 infection by mediating viral attachment to host cells and interacting with the capsid protein.Veterinary research · 2025Article
- Circovirus Rep evades immune restriction by disrupting cGAS oligomerization and phase separation.PLoS pathogens · 2025Article
- The replication protein of duck circovirus unwinds dsDNA in an ATP-driven and metal ion-dependent manner from 3' to 5'.Frontiers in veterinary science · 2025Article
- Enzymatic characterization and dominant sites of foot-and-mouth disease virus 2C protein.Heliyon · 2024Article
- Analysis of the anti-PCV2 mechanism ofFrontiers in microbiology · 2024Article
- Novel cycloviruses identified by mining human blood metagenomic data show close relationship to those from animals.Frontiers in microbiology · 2024Article
- The crystal structure of the human smacovirus 1 Rep domain.Acta crystallographica. Section F, Structural biology communications · 2023Article
- Vertebrate-tropism of a cressdnavirus lineage implicated by poxvirus gene capture.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- A Structural Perspective of Reps from CRESS-DNA Viruses and Their Bacterial Plasmid Homologues.Viruses · 2021Article
- Porcine Circovirus 2 Manipulates the PERK-ERO1α Axis of the Endoplasmic Reticulum To Favor Its Replication by Derepressing Viral DNA from HMGB1 Sequestration within Nuclei.Journal of virology · 2021Article
- Article
- Displaying epitope B and epitope 7 of porcine reproductive and respiratory syndrome virus on virus like particles of porcine circovirus type 2 provides partial protection to pigs.The Journal of veterinary medical science · 2021Article
- Molecular underpinnings of ssDNA specificity by Rep HUH-endonucleases and implications for HUH-tag multiplexing and engineering.Nucleic acids research · 2021Article
- Apoptosis Triggered by ORF3 Proteins of theFrontiers in cellular and infection microbiology · 2020Review
- Crystal structure of the Wheat dwarf virus Rep domain.Acta crystallographica. Section F, Structural biology communications · 2019Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two replicase (Rep) proteins, Rep and Rep', are encoded by porcine circovirus (PCV) ORF1; Rep is a full ORF1 transcript, and Rep' is a truncated transcript generated by splicing. These two proteins are crucial for the rolling-circle replication (RCR) of PCV. The N-terminal sequences of Rep and Rep' are identical and interact to form homo- or heterodimers. The three types of dimers perform different functions during replication. A structural examination of the interfacing termini has not been performed. In this study, a crystal structure of dimerized Rep protein N termini was resolved at 2.7 Å. The dimerized protein was maintained by nine intermolecular hydrogen bonds and 15 pairs of hydrophobic interactions. The amino acid residue Ile37 participates in 11 of the hydrophobic interactions, mostly with its side chain. To find the predominant sites for protein dimerization and virus replication, a series of mutant proteins and virus replicons were generated by alanine substitution. Of all the single amino acid substitutions, the mutation at Ile37 showed the greatest effect on protein dimerization and virus replication. A double mutation at Leu35 and Ile37 almost eliminated protein dimerization and had the greatest negative effect on virus replication. These studies demonstrate that Leu35 and Ile37 are the most important residues for protein dimerization and are crucial for virus replication. Our results also show that PCV replication can be decreased by disrupting the dimerization of Rep or Rep' at the N terminus, suggesting that the structural interface responsible for dimerization offers a promising antiviral target.
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