Directed evolution of retrovirus envelope protein cytoplasmic tails guided by functional incorporation into lentivirus particles

Christoph A. Merten, Jörn Stitz, Gundula Braun, Eric M. Poeschla, Klaus Cichutek, Christian J. Buchholz

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

In contrast to most gammaretrovirus envelope proteins (Env), the Gibbon ape leukemia virus (GaLV) Env protein does not mediate the infectivity of human immunodeficiency virus type 1 (HIV-1) particles. We made use of this observation to set up a directed evolution system by creating a library of GaLV Env variants diversified at three critical amino acids, all located around the R-peptide cleavage site within the cytoplasmic tail. This library was screened for variants that were able to functionally pseudotype HIV-1 vector particles. All selected Env variants mediated the infectivity of HIV-1 vector particles and encoded novel cytoplasmic tail motifs. They were efficiently incorporated into HIV particles, and the R peptide was processed by the HIV protease. Interestingly, in some of the selected variants, the R-peptide cleavage site had shifted closer to the C terminus. These data demonstrate a valuable approach for the engineering of chimeric viruses and vector particles.

Original languageEnglish (US)
Pages (from-to)834-840
Number of pages7
JournalJournal of virology
Volume79
Issue number2
DOIs
StatePublished - Jan 1 2005

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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