ArticleJournal of virology2004
Quantification of the DNA cleavage and packaging proteins U(L)15 and U(L)28 in A and B capsids of herpes simplex virus type 1.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed, 27 citations in OpenAlex.
- Duck Plague Virus Full-Length UL15 Protein Is a Multifunctional Enzyme Which Not Only Possesses Nuclease Activity but Also Exerts ATPase and DNA-Binding Activity.Veterinary sciences · 2025Article
- Mechanical Capsid Maturation Facilitates the Resolution of Conflicting Requirements for Herpesvirus Assembly.Journal of virology · 2022Article
- Role of HSV-1 Capsid Vertex-Specific Component (CVSC) and Viral Terminal DNA in Capsid Docking at the Nuclear Pore.Viruses · 2021Article
- The Ins and Outs of Herpesviral Capsids: Divergent Structures and Assembly Mechanisms across the Three Subfamilies.Viruses · 2021Review
- Role of the Herpes Simplex Virus CVSC Proteins at the Capsid Portal Vertex.Journal of virology · 2020Article
- Cryo-EM structure of the varicella-zoster virus A-capsid.Nature communications · 2020Article
- Structure of the herpes simplex virus type 2 C-capsid with capsid-vertex-specific component.Nature communications · 2018Article
- Herpesvirus Capsid Assembly and DNA Packaging.Advances in anatomy, embryology, and cell biology · 2017Review
- Intermolecular Complementation between Two Varicella-Zoster Virus pORF30 Terminase Domains Essential for DNA Encapsidation.Journal of virology · 2015Article
- The putative herpes simplex virus 1 chaperone protein UL32 modulates disulfide bond formation during infection.Journal of virology · 2015Article
- Isolation and characterization of the herpes simplex virus 1 terminase complex.Journal of virology · 2014Article
- A mutation in UL15 of herpes simplex virus 1 that reduces packaging of cleaved genomes.Journal of virology · 2011Article
- Identification of a spliced gene from duck enteritis virus encoding a protein homologous to UL15 of herpes simplex virus 1.Virology journal · 2011Article
- Susceptibilities of human cytomegalovirus clinical isolates and other herpesviruses to new acetylated, tetrahalogenated benzimidazole D-ribonucleosides.Antimicrobial agents and chemotherapy · 2009Article
- Other inhibitors of viral enzymes and functions.Handbook of experimental pharmacology · 2009Review
- Identification of acetylated, tetrahalogenated benzimidazole D-ribonucleosides with enhanced activity against human cytomegalovirus.Journal of virology · 2007Article
- A putative leucine zipper within the herpes simplex virus type 1 UL6 protein is required for portal ring formation.Journal of virology · 2007Article
- Putative terminase subunits of herpes simplex virus 1 form a complex in the cytoplasm and interact with portal protein in the nucleus.Journal of virology · 2007Article
- Viral capsids: mechanical characteristics, genome packaging and delivery mechanisms.Cellular and molecular life sciences : CMLS · 2007Review
- Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids.Virology · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The proteins produced by the herpes simplex virus type 1 (HSV-1) genes U(L)15 and U(L)28 are believed to form part of the terminase enzyme, a protein complex essential for the cleavage of newly synthesized, concatameric herpesvirus DNA and the packaging of the resultant genome lengths into preformed capsids. This work describes the purification of recombinant forms of pU(L)15 and pU(L)28, which allowed the calculation of the average number of copies of each protein in A and B capsids and in capsids lacking the putative portal encoded by U(L)6. On average, 1.0 (+/-0.29 [standard deviation]) copies of pU(L)15 and 2.4 (+/-0.97) copies of pU(L)28 were present in B capsids, 1.2 (+/-0.72) copies of pU(L)15 and 1.5 (+/-0.86) copies of pU(L)28 were found in mutant capsids lacking the putative portal protein pU(L)6, and approximately 12.0 (+/-5.63) copies of pU(L)15 and 0.6 (+/-0.32) copies of pU(L)28 were present in each A capsid. These results suggest that the packaging machine is partly comprised of approximately 12 copies of pU(L)15, as found in A capsids, with wild-type B and mutant U(L)6(-) capsids containing an incomplete complement of cleavage and packaging proteins. These results are consistent with observations that B capsids form by default in the absence of packaging machinery in vitro and in vivo. In contrast, A capsids may be the result of initiated but aborted attempts at DNA packaging, resulting in the retention of at least part of the DNA packaging machinery.
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