Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein

Steve S L Chen, Chun Nan Lee, Woan Ruoh Lee, Kenneth Mcintosh, Tun Hou Lee

Research output: Contribution to journalArticle

108 Citations (Scopus)

Abstract

The N-terminal region of the envelope (env) transmembrane protein of human immunodeficiency virus type 1 (HIV-1) has a leucine zipper-like motif. This highly conserved zipper motif, which consists of a heptad repeat of leucine or isoleucine residues, has been suggested to play a role in HIV-1 env glycoprotein oligomerization. This hypothesis was tested by replacing the highly conserved leucine or isoleucine residues in the zipper motif with a strong α-helix breaker, proline. We report here that such substitutions did not abolish the ability of env protein to form oligomers, indicating that this highly conserved zipper motif does not have a crucial role in env protein oligomerization. However, the mutant viruses all showed impaired infectivity, suggesting that this conserved zipper motif can have an important role in the virus life cycle.

Original languageEnglish
Pages (from-to)3615-3619
Number of pages5
JournalJournal of Virology
Volume67
Issue number6
Publication statusPublished - Jun 1993
Externally publishedYes

ASJC Scopus subject areas

  • Immunology

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