Egress of HSV-1 capsid requires the interaction of VP26 and a cellular tetraspanin membrane protein

Virol J. 2010 Jul 14:7:156. doi: 10.1186/1743-422X-7-156.

Abstract

HSV-1 viral capsid maturation and egress from the nucleus constitutes a self-controlled process of interactions between host cytoplasmic membrane proteins and viral capsid proteins. In this study, a member of the tetraspanin superfamily, CTMP-7, was shown to physically interact with HSV-1 protein VP26, and the VP26-CTMP-7 complex was detected both in vivo and in vitro. The interaction of VP26 with CTMP-7 plays an essential role in normal HSV-1 replication. Additionally, analysis of a recombinant virus HSV-1-UG showed that mutating VP26 resulted in a decreased viral replication rate and in aggregation of viral mutant capsids in the nucleus. Together, our data support the notion that biological events mediated by a VP26 - CTMP-7 interaction aid in viral capsid enveloping and egress from the cell during the HSV-1 infectious process.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Capsid Proteins / genetics
  • Capsid Proteins / metabolism*
  • Cell Line
  • Cricetinae
  • Herpes Simplex / genetics
  • Herpes Simplex / metabolism*
  • Herpes Simplex / virology
  • Herpesvirus 1, Human / genetics
  • Herpesvirus 1, Human / physiology*
  • Humans
  • Membrane Proteins
  • Molecular Sequence Data
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism*
  • Protein Binding
  • Tetraspanins
  • Virus Release*
  • Virus Replication

Substances

  • Capsid Proteins
  • Membrane Proteins
  • Nerve Tissue Proteins
  • TSPAN7 protein, human
  • Tetraspanins
  • capsid protein VP26, herpes simplex virus type 1