Identification of binding domains in the herpes simplex virus type 1 small capsid protein pUL35 (VP26)

Arin Apcarian, Anthony L. Cunningham, Russell J Diefenbach

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

In this study, fragments of the small capsid protein pUL35 (VP26) from herpes simplex virus type 1 (HSV-1) were generated to identify binding domains for a number of known ligands. Analysis of the binding of dynein light chain subunits, DYNLT1 and DYNLT3, as well the HSV-1 structural proteins pUL19 (VP5) and pUL37 was then undertaken using the LexA yeast two-hybrid assay. The N-terminal half of pUL35, in particular residues 30-43, was identified as a common region for the binding of DYNLT1 and DYNLT3. Additional distinct regions in the C terminus of pUL35 also contribute to the binding of DYNLT1 and DYNLT3. In contrast, only the C-terminal half of pUL35 was found to mediate the binding of pUL19 and pUL37 through distinct regions. The relevance of this information to the role of pUL35 in viral transport and assembly is discussed.

Original languageEnglish
Pages (from-to)2659-2663
Number of pages5
JournalJournal of General Virology
Volume91
Issue number11
DOIs
Publication statusPublished - Nov 2010
Externally publishedYes

Keywords

  • Binding Sites
  • Capsid Proteins
  • Dyneins
  • Herpesvirus 1, Human
  • Protein Binding
  • Protein Interaction Mapping
  • Two-Hybrid System Techniques
  • Viral Structural Proteins
  • Virus Assembly
  • Virus Replication
  • Journal Article
  • Research Support, Non-U.S. Gov't

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