Residues F593 and E596 of HSV-1 tegument protein pUL36 (VP1/2) mediate binding of tegument protein pUL37

Branka Mijatov, Anthony L. Cunningham, Russell J Diefenbach

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

The herpes simplex virus type 1 (HSV-1) structural tegument proteins pUL36 (VP1/2) and pUL37 are essential for secondary envelopment during the egress of viral particles. Our laboratory has previously shown that HSV-1 pUL36(512-767) fragment interacts with full-length pUL37. A number of single and double amino acid changes of conserved residues in the pUL36(512-767) fragment were generated using alanine-scanning site-directed mutagenesis. The interaction of pUL36(512-767) and pUL37 was then assessed using a combination of yeast two-hybrid and coimmunoprecipitation assays. Single changes to alanine of pUL36 residues F593 and E596 impaired binding of pUL37 with the greatest effect observed for the substitution E596A. Double mutations involving either of these residues in combination with the substitution E580A essentially blocked binding of pUL37. This information will provide the basis for generation of viral mutants to further define the importance of the pUL36/pUL37 interaction in assembly of HSV-1.

Original languageEnglish
Pages (from-to)26-31
Number of pages6
JournalVirology
Volume368
Issue number1
DOIs
Publication statusPublished - 10 Nov 2007
Externally publishedYes

Keywords

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Herpesvirus 1, Human
  • Immunoprecipitation
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Protein Binding
  • Protein Interaction Mapping
  • Two-Hybrid System Techniques
  • Viral Structural Proteins
  • Journal Article
  • Research Support, Non-U.S. Gov't

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