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Gene Review

UL25  -  located on capsid near vertices; possibly...

Human herpesvirus 1

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Disease relevance of UL25

  • Structural characterization of the UL25 DNA-packaging protein from herpes simplex virus type 1 [1].
  • The distribution of UL17 and UL25 on B capsids was examined using immunogold labeling [2].
  • Evolutionary trace analysis of UL25 and its homologues in other herpesviruses was used to locate potentially important amino acids on the surface of the protein, leading to the identification of four putative docking regions for protein partners [1].
  • The UL25 packaging protein, which is also present in virions, was not found in significant amounts in L particles, indicating that it is associated only with the capsid [3].
  • The rabbit antiserum raised against HSV-1 UL25 protein immunoprecipitated a UL25-homologue of identical size from HSV-2-infected cells [4].

High impact information on UL25

  • Herpes simplex virus type 1 DNA-packaging protein UL17 is required for efficient binding of UL25 to capsids [2].
  • The herpes simplex virus type 1 UL25 protein is incorporated into the capsid during DNA packaging, and previous studies of a null mutant have demonstrated that its function is essential at the late stages of the head-filling process, either to allow packaging to proceed to completion or for retention of the viral genome within the capsid [1].
  • To clarify the functional role of UL25 we analyzed the homologous protein of the alphaherpesvirus pseudorabies virus (PrV) [5].
  • 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 [6].
  • Consistent with previous studies showing that UL6 and UL25 are minor protein constituents of the capsids, we detected these proteins in both B and C capsids [6].

Biological context of UL25


Other interactions of UL25


Analytical, diagnostic and therapeutic context of UL25


  1. Structural characterization of the UL25 DNA-packaging protein from herpes simplex virus type 1. Bowman, B.R., Welschhans, R.L., Jayaram, H., Stow, N.D., Preston, V.G., Quiocho, F.A. J. Virol. (2006) [Pubmed]
  2. Herpes simplex virus type 1 DNA-packaging protein UL17 is required for efficient binding of UL25 to capsids. Thurlow, J.K., Murphy, M., Stow, N.D., Preston, V.G. J. Virol. (2006) [Pubmed]
  3. The herpes simplex virus type 1 DNA packaging protein UL17 is a virion protein that is present in both the capsid and the tegument compartments. Thurlow, J.K., Rixon, F.J., Murphy, M., Targett-Adams, P., Hughes, M., Preston, V.G. J. Virol. (2005) [Pubmed]
  4. Characterization of an essential HSV-1 protein encoded by the UL25 gene reported to be involved in virus penetration and capsid assembly. Ali, M.A., Forghani, B., Cantin, E.M. Virology (1996) [Pubmed]
  5. The capsid-associated UL25 protein of the alphaherpesvirus pseudorabies virus is nonessential for cleavage and encapsidation of genomic DNA but is required for nuclear egress of capsids. Klupp, B.G., Granzow, H., Keil, G.M., Mettenleiter, T.C. J. Virol. (2006) [Pubmed]
  6. 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]
  7. The product of the herpes simplex virus type 1 UL25 gene is required for encapsidation but not for cleavage of replicated viral DNA. McNab, A.R., Desai, P., Person, S., Roof, L.L., Thomsen, D.R., Newcomb, W.W., Brown, J.C., Homa, F.L. J. Virol. (1998) [Pubmed]
  8. 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]
  9. Nucleotide sequence and transcriptional analysis of a portion of the bovine herpesvirus genome encoding genes homologous to HSV-1, UL25, UL26 and UL26.5. Haanes, E.J., Chen, C.C., Lowery, D.E. Virus Res. (1997) [Pubmed]
  10. Herpes simplex virus encodes a virion-associated protein which promotes long cellular processes in over-expressing cells. Takakuwa, H., Goshima, F., Koshizuka, T., Murata, T., Daikoku, T., Nishiyama, Y. Genes Cells (2001) [Pubmed]
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