ArticleJournal of virology2012
Identification of a divalent metal cation binding site in herpes simplex virus 1 (HSV-1) ICP8 required for HSV replication.
Article in Journal of virology, 2012. 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, 34 citations in OpenAlex.
- Herpes simplex virus infected cell protein 8 is required for viral inhibition of the cGAS pathway.Virology · 2023Article
- Article
- Berberine Inhibits Herpes Simplex Virus 1 Replication in HEK293T Cells.Computational and mathematical methods in medicine · 2022Article
- Importance of lipophilicity for potent anti-herpes simplex virus-1 activity of α-hydroxytropolones.MedChemComm · 2019Article
- The HIV Integrase Inhibitor Raltegravir Inhibits Felid Alphaherpesvirus 1 Replication by Targeting both DNA Replication and Late Gene Expression.Journal of virology · 2018Article
- Antifungal drug ciclopirox olamine reduces HSV-1 replication and disease in mice.Antiviral research · 2018Article
- Broad anti-herpesviral activity of α-hydroxytropolones.Veterinary microbiology · 2018Article
- The SP100 component of ND10 enhances accumulation of PML and suppresses replication and the assembly of HSV replication compartments.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Gene sharing between Epstein-Barr virus and human immune response genes.Immunologic research · 2017Review
- Adenovirus-mediated shRNA interference against HSV-1 replication in vitro.Journal of neurovirology · 2016Article
- Synthetic α-Hydroxytropolones Inhibit Replication of Wild-Type and Acyclovir-Resistant Herpes Simplex Viruses.Antimicrobial agents and chemotherapy · 2016Article
- Article
- Inhibition of O-Linked N-Acetylglucosamine Transferase Reduces Replication of Herpes Simplex Virus and Human Cytomegalovirus.Journal of virology · 2015Article
- Inhibitors of nucleotidyltransferase superfamily enzymes suppress herpes simplex virus replication.Antimicrobial agents and chemotherapy · 2014Article
- Article
- Epstein-Barr virus-host cell interactions: an epigenetic dialog?Frontiers in genetics · 2014Article
- Details of ssDNA annealing revealed by an HSV-1 ICP8-ssDNA binary complex.Nucleic acids research · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Herpes simplex virus 1 (HSV-1) ICP8 is a single-stranded DNA-binding protein that is necessary for viral DNA replication and exhibits recombinase activity in vitro. Alignment of the HSV-1 ICP8 amino acid sequence with ICP8 homologs from other herpesviruses revealed conserved aspartic acid (D) and glutamic acid (E) residues. Amino acid residue D1087 was conserved in every ICP8 homolog analyzed, indicating that it is likely critical for ICP8 function. We took a genetic approach to investigate the functions of the conserved ICP8 D and E residues in HSV-1 replication. The E1086A D1087A mutant form of ICP8 failed to support the replication of an ICP8 mutant virus in a complementation assay. E1086A D1087A mutant ICP8 bound DNA, albeit with reduced affinity, demonstrating that the protein is not globally misfolded. This mutant form of ICP8 was also recognized by a conformation-specific antibody, further indicating that its overall structure was intact. A recombinant virus expressing E1086A D1087A mutant ICP8 was defective in viral replication, viral DNA synthesis, and late gene expression in Vero cells. A class of enzymes called DDE recombinases utilize conserved D and E residues to coordinate divalent metal cations in their active sites. We investigated whether the conserved D and E residues in ICP8 were also required for binding metal cations and found that the E1086A D1087A mutant form of ICP8 exhibited altered divalent metal binding in an in vitro iron-induced cleavage assay. These results identify a novel divalent metal cation-binding site in ICP8 that is required for ICP8 functions during viral replication.
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