Overall signal sequence hydrophobicity determines the in vivo translocation efficiency of a herpesvirus glycoprotein

Patrick Ryan, Alan Robbins, Mary Whealy, L. W. Enquist

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

We have described three mutant strains of Pseudorabies virus that contain mutations in the signal sequence coding region of a nonessential envelope glycoprotein, gIII. The alterations disrupt, truncate, or eliminate the hydrophobic core domain of the signal sequence. Each mutant was assayed for its ability to promote the translocation of gIII across the endoplasmic reticulum membrane and the subsequent localization of the mature form of the glycoprotein to the infected cell surface or the virus envelope. Our results confirm and extend findings in other systems that the overall hydrophobicity of the signal sequence core region is a major determinant of translocation efficiency. We were unable to correlate simply the length of the core or the average hydrophobicity of core residues with export efficiency. Because our work involved the use of infectious virus mutants, we were able to identify a virus defect associated with a complete block in gIII export. This defect will facilitate a pseudoreversion analysis of gIII signal sequence function.

Original languageEnglish (US)
Pages (from-to)5-21
Number of pages17
JournalVirus Genes
Volume7
Issue number1
DOIs
StatePublished - Feb 1 1993
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics
  • Virology

Keywords

  • Pseudorabies virus
  • glycoprotein gIII
  • herpesvirus
  • hydrophobicity
  • protein export
  • signal sequence

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