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Gene Review

UL26.5  -  clipped near C terminus

Human herpesvirus 1

 
 
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Disease relevance of UL26.5

  • VP22a was shown to form the inner core of the B capsid, since in infections in which the UL26.5 gene was omitted the 100-nm capsids that formed lacked the inner core [1].
  • An essential step in assembly of herpes simplex virus (HSV) type 1 capsids involves interaction of the major capsid protein (VP5) with the C terminus of the scaffolding protein (encoded by the UL26.5 gene) [2].
  • In these studies, we tested whether the HCMV UL80.5 gene would substitute for the HSV UL26.5 gene in a baculovirus capsid assembly system that we have previously described (D. R. Thomsen et al., J. Virol. 68:2442-2457, 1994) [2].
  • Previous studies have shown that the bovine herpesvirus 1 (alphaherpesvirus) UL26.5 homolog will functionally substitute for the HSV UL26.5 gene (E. J. Haanes et al., J. Virol. 69:7375-7379, 1995) [2].
  • The homolog of the UL26.5 gene in the human cytomegalovirus (HCMV) genome is the UL80.5 gene [2].
 

High impact information on UL26.5

 

Biological context of UL26.5

 

Other interactions of UL26.5

References

  1. Assembly of herpes simplex virus (HSV) intermediate capsids in insect cells infected with recombinant baculoviruses expressing HSV capsid proteins. Thomsen, D.R., Roof, L.L., Homa, F.L. J. Virol. (1994) [Pubmed]
  2. Assembly of herpes simplex virus capsids using the human cytomegalovirus scaffold protein: critical role of the C terminus. Oien, N.L., Thomsen, D.R., Wathen, M.W., Newcomb, W.W., Brown, J.C., Homa, F.L. J. Virol. (1997) [Pubmed]
  3. Identification of a region in the herpes simplex virus scaffolding protein required for interaction with the portal. Singer, G.P., Newcomb, W.W., Thomsen, D.R., Homa, F.L., Brown, J.C. J. Virol. (2005) [Pubmed]
  4. Evidence for controlled incorporation of herpes simplex virus type 1 UL26 protease into capsids. Sheaffer, A.K., Newcomb, W.W., Brown, J.C., Gao, M., Weller, S.K., Tenney, D.J. J. Virol. (2000) [Pubmed]
  5. Second site mutations in the N-terminus of the major capsid protein (VP5) overcome a block at the maturation cleavage site of the capsid scaffold proteins of herpes simplex virus type 1. Desai, P., Person, S. Virology (1999) [Pubmed]
  6. The 25 amino acid residues at the carboxy terminus of the herpes simplex virus type 1 UL26.5 protein are required for the formation of the capsid shell around the scaffold. Kennard, J., Rixon, F.J., McDougall, I.M., Tatman, J.D., Preston, V.G. J. Gen. Virol. (1995) [Pubmed]
  7. 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]
  8. 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]
  9. Capsids are formed in a mutant virus blocked at the maturation site of the UL26 and UL26.5 open reading frames of herpes simplex virus type 1 but are not formed in a null mutant of UL38 (VP19C). Person, S., Desai, P. Virology (1998) [Pubmed]
 
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