Identification of structural protein-protein interactions of herpes simplex virus type 1

Jin H. Lee, Valerio Vittone, Eve Diefenbach, Anthony L. Cunningham, Russell J. Diefenbach*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

87 Citations (Scopus)


In this study we have defined protein-protein interactions between the structural proteins of herpes simplex virus type 1 (HSV-1) using a LexA yeast two-hybrid system. The majority of the capsid, tegument and envelope proteins of HSV-1 were screened in a matrix approach. A total of 40 binary interactions were detected including 9 out of 10 previously identified tegument-tegument interactions (Vittone, V., Diefenbach, E., Triffett, D., Douglas, M.W., Cunningham, A.L., and Diefenbach, R.J., 2005. Determination of interactions between tegument proteins of herpes simplex virus type 1. J. Virol. 79, 9566-9571). A total of 12 interactions involving the capsid protein pUL35 (VP26) and 11 interactions involving the tegument protein pUL46 (VP11/12) were identified. The most significant novel interactions detected in this study, which are likely to play a role in viral assembly, include pUL35-pUL37 (capsid-tegument), pUL46-pUL37 (tegument-tegument) and pUL49 (VP22)-pUS9 (tegument-envelope). This information will provide further insights into the pathways of HSV-1 assembly and the identified interactions are potential targets for new antiviral drugs.

Original languageEnglish
Pages (from-to)347-54
Number of pages8
Issue number2
Publication statusPublished - 1 Sep 2008
Externally publishedYes

Bibliographical note

Corrigendum can be found in Virology, Volume 385(1), 282-283,


  • herpes simplex virus
  • virus assembly
  • yeast two-hybrid assay
  • protein–protein interactions


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