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Gene Review

UL35  -  located externally on capsid hexons;...

Cercopithecine herpesvirus 2

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Disease relevance of UL35

  • By comparing capsids assembled with and without the expression of gene UL35, we have confirmed the presence of six copies of its product, VP26 (12 kDa), around each hexon tip [1].
  • The UL35 open reading frame (ORF) of herpes simplex virus type 1 (HSV-1) has been predicted from DNA sequence analysis to encode a small polypeptide with a molecular weight of 12,095 [2].
  • Furthermore, the anti-NC7 serum was also found to react with the TrpE-UL35 chimeric protein isolated from E. coli, providing additional evidence that the UL35 gene encodes p12 [2].
  • The 12-kDa protein recognized by the TrpE-UL35 antiserum was associated with purified HSV-1 virions and type A and B capsids, suggesting that the UL35 ORF may encode the 12-kDa capsid protein variably designated p12, NC7, or VP26 [2].

High impact information on UL35

  • Here we report that the herpes simplex virus outer capsid protein VP26 interacts with dynein light chains RP3 and Tctex1 and is sufficient to mediate retrograde transport of viral capsids in a cellular model [3].
  • By utilizing the TrpE-UL35 antiserum, the kinetics of synthesis of the UL35 gene product was examined, and these studies indicate that UL35 is expressed as a gamma 2 (true late) gene [2].
  • We have investigated the protein product of the UL35 ORF by using a trpE-UL35 gene fusion to produce a corresponding fusion protein in Escherichia coli [2].


  1. Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: structural authenticity and localization of VP26. Trus, B.L., Homa, F.L., Booy, F.P., Newcomb, W.W., Thomsen, D.R., Cheng, N., Brown, J.C., Steven, A.C. J. Virol. (1995) [Pubmed]
  2. Identification and characterization of the herpes simplex virus type 1 virion protein encoded by the UL35 open reading frame. McNabb, D.S., Courtney, R.J. J. Virol. (1992) [Pubmed]
  3. Herpes simplex virus type 1 capsid protein VP26 interacts with dynein light chains RP3 and Tctex1 and plays a role in retrograde cellular transport. Douglas, M.W., Diefenbach, R.J., Homa, F.L., Miranda-Saksena, M., Rixon, F.J., Vittone, V., Byth, K., Cunningham, A.L. J. Biol. Chem. (2004) [Pubmed]
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