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Gene Review

UL15  -  contains an ATPase domain

Human herpesvirus 1

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Disease relevance of UL15


High impact information on UL15

  • In contrast, all of the UL28 insertion mutants were found to interact with UL15 but the interaction was reduced with mutants that failed to react with UL33 [3].
  • DNA sequence analysis, in combination with genetic complementation assays, demonstrated that a second-site mutation in the UL15 gene restored the ability of the revertant to cleave and package viral DNA [3].
  • The UL15 protein interacts with the UL28 protein, and both are strong candidates for subunits of the viral terminase, a key component of the molecular motor that drives the DNA into the capsid [4].
  • Herpes simplex virus type 1 portal protein UL6 interacts with the putative terminase subunits UL15 and UL28 [4].
  • Herpes simplex virus type 1 (HSV-1) gene UL14 is located between divergently transcribed genes UL13 and UL15 and overlaps the promoters for both of these genes [5].

Biological context of UL15

  • Previous results indicated that UL28 interacts with UL15 and UL33 to form a protein complex (terminase) that is presumed to cleave concatemeric DNA into genome lengths [3].
  • This report concerns the isolation of a temperature-sensitive mutant with a mutation mapping in the UL15 open reading frame [6].
  • Thus, UL15 may play a direct role in the cleavage of viral DNA replication intermediates into monomers [2].
  • In this study, we detected two UL15 gene products of 81 and 30 kDa in HSV-1-infected cells, using a polyclonal antibody raised against a maltose binding protein fusion construct containing UL15 exon 2 [1].
  • Surprisingly, three of the mutants prevented the UL15 protein from localizing to the cell nucleus, and these were not functional in a transient DNA packaging assay [7].

Associations of UL15 with chemical compounds

  • Last, we constructed a UL15 mutant, UL15C(G263A), in which the invariant Gly263 in the Walker box A of the ATP binding motif (GKT) was substituted with an alanine [8].

Enzymatic interactions of UL15

  • Interaction of the herpes simplex virus type 1 packaging protein UL15 with full-length and deleted forms of the UL28 protein [7].

Other interactions of UL15

  • In addition, the UL28 protein was found predominantly in B but not C capsids in a distribution similar to that of the 81-kDa version of UL15 [2].
  • In agreement with previous results, UL15, when expressed alone, entered the nucleus but UL28 remained cytoplasmic [7].
  • Typing was done by restriction of the UL30 and UL15 amplicons with Ava II and Hpa II enzymes, respectively [9].
  • The UL16 gene of herpes simplex virus maps within the intron of the UL 15 gene [10].
  • The genes UL 15 of HSV and UL 42 of VZV share the highest degree of homology within the two genomes [11].

Analytical, diagnostic and therapeutic context of UL15

  • In this report, immunofluorescence was used to show that UL15 localizes to the nucleus in the absence of any other viral proteins; this indicates that UL15 contains its own nuclear localization signal [8].
  • Furthermore, we have shown that plasmids containing a UL15.5 knockout mutation still complement the growth of UL15 insertion mutant viruses, indicating that UL15.5 is not required for viral growth in cell culture [8].


  1. Characterization of ICP6::lacZ insertion mutants of the UL15 gene of herpes simplex virus type 1 reveals the translation of two proteins. Yu, D., Sheaffer, A.K., Tenney, D.J., Weller, S.K. J. Virol. (1997) [Pubmed]
  2. Herpes simplex virus type 1 cleavage and packaging proteins UL15 and UL28 are associated with B but not C capsids during packaging. Yu, D., Weller, S.K. J. Virol. (1998) [Pubmed]
  3. Linker Insertion Mutations in the Herpes Simplex Virus Type 1 UL28 Gene: Effects on UL28 Interaction with UL15 and UL33 and Identification of a Second-Site Mutation in the UL15 Gene That Suppresses a Lethal UL28 Mutation. Jacobson, J.G., Yang, K., Baines, J.D., Homa, F.L. J. Virol. (2006) [Pubmed]
  4. Herpes simplex virus type 1 portal protein UL6 interacts with the putative terminase subunits UL15 and UL28. White, C.A., Stow, N.D., Patel, A.H., Hughes, M., Preston, V.G. J. Virol. (2003) [Pubmed]
  5. Herpes simplex virus type 1 gene UL14: phenotype of a null mutant and identification of the encoded protein. Cunningham, C., Davison, A.J., MacLean, A.R., Taus, N.S., Baines, J.D. J. Virol. (2000) [Pubmed]
  6. Characterization of a temperature-sensitive mutant of the UL15 open reading frame of herpes simplex virus 1. Poon, A.P., Roizman, B. J. Virol. (1993) [Pubmed]
  7. Interaction of the herpes simplex virus type 1 packaging protein UL15 with full-length and deleted forms of the UL28 protein. Abbotts, A.P., Preston, V.G., Hughes, M., Patel, A.H., Stow, N.D. J. Gen. Virol. (2000) [Pubmed]
  8. Genetic analysis of the UL 15 gene locus for the putative terminase of herpes simplex virus type 1. Yu, D., Weller, S.K. Virology (1998) [Pubmed]
  9. Comparison of two methods of PCR followed by enzymatic restriction digestion for detection and typing of herpes simplex viruses isolated from patients with mucocutaneous or cutaneous lesions. Herrera-Mart??nez, E., Ondarza-Aguilera, R., Estrada-Parra, S., P??rez, G., Barr??n, B.L. Rev. Latinoam. Microbiol. (2005) [Pubmed]
  10. The UL 16 gene product of herpes simplex virus 1 is a virion protein that colocalizes with intranuclear capsid proteins. Nalwanga, D., Rempel, S., Roizman, B., Baines, J.D. Virology (1996) [Pubmed]
  11. Evaluation of a new general primer pair for rapid detection and differentiation of HSV-1, HSV-2, and VZV by polymerase chain reaction. Baron, J.M., Rübben, A., Grussendorf-Conen, E.I. J. Med. Virol. (1996) [Pubmed]
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