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Gene Review

UL29  -  contains a zinc-finger

Human herpesvirus 1

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Disease relevance of UL29

  • The UL28 protein of herpes simplex virus type 1 (HSV-1) is one of seven viral proteins required for the cleavage and packaging of viral DNA [1].
  • In order to define the functional domains of UL28 that are important for DNA cleavage/packaging, we constructed a series of HSV-1 mutants with linker insertion and nonsense mutations in UL28 [1].
  • 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].
  • The ICP18.5 gene (UL28) of herpes simplex virus type 1 is a member of a well-conserved gene family among herpesviruses and is thought to play a role in localization of viral glycoproteins [3].
  • To investigate the association of the UL6 protein with the UL15 and UL28 proteins, the three proteins were produced in large amounts in insect cells with the baculovirus expression system [4].

High impact information on UL29

  • Revertant viruses that formed plaques on Vero cells were detected for one of the lethal UL28 insertion mutants [1].
  • 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 [1].
  • 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].
  • Furthermore, this analysis, together with guanidine HCl extraction analysis of purified capsids, indicates that UL6, UL25, and UL28 are able to associate with B capsids in the absence of other DNA cleavage and packaging proteins [2].
  • Four of five transformants that supported the growth of the UL27 mutant also supported the growth of a UL27-UL28 double mutant [5].

Chemical compound and disease context of UL29

  • In the present study UL27 (glycoprotein gB) of herpes simplex virus type 1 (KOS) is the target gene for mutation transfer and the upstream gene UL28, which specifies the ICP18.5 polypeptide, is the marker-rescue gene [6].

Biological context of UL29

  • The herpes simplex virus type 1 UL28 gene contains a 785-amino-acid open reading frame that codes for an essential protein [7].
  • Vero cells were transformed with plasmid DNA that encoded ORF UL25 through UL28 and screened for their ability to support the growth of a mutant virus with a null mutation in UL27 (K082) [5].
  • Of the three UL28 mutant proteins that entered the nucleus with UL15, one containing an internal deletion of 13 amino acids was able to complement a UL28 null mutant in both DNA packaging and virus yield assays, demonstrating that this region of the protein is not essential for function [8].
  • These results demonstrate the functional equivalency of the cercopithecine monkey virus gB glycoproteins and genes (including transcriptional regulatory elements) in HSV1, the functional nature of HSV1/SA8 chimeric UL28 and UL26 genes/proteins, and that UL28, gB and/or p40 proteins may effect the pathogenicity of HSV1 [9].
  • We determined the nucleotide sequence of non-pathogenic Marek's disease virus serotype 2 (MDV2) strain HPRS24 glycoprotein B (gB) (UL27), ICP18.5 (UL28) and major DNA-binding protein (MDBP) (UL29) genes homologous to herpes simplex virus type 1 (HSV-1) [10].

Anatomical context of UL29


Associations of UL29 with chemical compounds

  • Utilizing co-transfection of DNA from glycoprotein gB- strain of HSV1 and cloned fragments of several simian alpha-herpesviruses containing the UL26, UL27 (gB glycoprotein), and UL28 gene homologs, replication-competent recombinant viruses were produced [9].

Enzymatic interactions of UL29

  • Interaction of the herpes simplex virus type 1 packaging protein UL15 with full-length and deleted forms of the UL28 protein [8].

Other interactions of UL29

  • Displacement of ICP35 from replication compartments was not observed in cells infected with cleavage/packaging mutants lacking UL28 and UL33 [12].
  • The MDV2 UL28 and UL29 genes have not been reported in other serotypes of MDV [10].

Analytical, diagnostic and therapeutic context of UL29

  • Analysis by cell surface immunofluorescence showed that the UL28 gene is not required for expression of viral glycoproteins on the surface of infected cells [7].


  1. 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]
  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. Overexpression in bacterial and identification in infected cells of the pseudorabies virus protein homologous to herpes simplex virus type 1 ICP18.5. Pederson, N.E., Enquist, L.W. J. Virol. (1991) [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. The size and symmetry of B capsids of herpes simplex virus type 1 are determined by the gene products of the UL26 open reading frame. Desai, P., Watkins, S.C., Person, S. J. Virol. (1994) [Pubmed]
  6. A genetic selection method for the transfer of HSV-1 glycoprotein B mutations from plasmid to the viral genome: preliminary characterization of transdominance and entry kinetics of mutant viruses. Desai, P., Homa, F.L., Person, S., Glorioso, J.C. Virology (1994) [Pubmed]
  7. Herpes simplex virus type 1 DNA cleavage and encapsidation require the product of the UL28 gene: isolation and characterization of two UL28 deletion mutants. Tengelsen, L.A., Pederson, N.E., Shaver, P.R., Wathen, M.W., Homa, F.L. J. Virol. (1993) [Pubmed]
  8. 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]
  9. Genetic and functional complementation of the HSV1 UL27 gene and gB glycoprotein by simian alpha-herpesvirus homologs. Eberle, R., Tanamachi, B., Black, D., Blewett, E.L., Ali, M., Openshaw, H., Cantin, E.M. Arch. Virol. (1997) [Pubmed]
  10. Identification of the Marek's disease virus serotype 2 genes homologous to the glycoprotein B (UL27), ICP18.5 (UL28) and major DNA-binding protein (UL29) genes of herpes simplex virus type 1. Kato, K., Jang, H.K., Izumiya, Y., Cai, J.S., Tsushima, Y., Miyazawa, T., Kai, C., Mikami, T. J. Vet. Med. Sci. (1999) [Pubmed]
  11. Resolution of genotypic and phenotypic properties of herpes simplex virus type 1 temperature-sensitive mutant (KOS) tsZ47: evidence for allelic complementation in the UL28 gene. Cavalcoli, J.D., Baghian, A., Homa, F.L., Kousoulas, K.G. Virology (1993) [Pubmed]
  12. The herpes simplex virus 1 UL 17 gene is required for localization of capsids and major and minor capsid proteins to intranuclear sites where viral DNA is cleaved and packaged. Taus, N.S., Salmon, B., Baines, J.D. Virology (1998) [Pubmed]
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