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

Journal Article (Journal Article)

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 alpha-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.

Full Text

Duke Authors

Cited Authors

  • Chen, SS; Lee, CN; Lee, WR; McIntosh, K; Lee, TH

Published Date

  • June 1993

Published In

Volume / Issue

  • 67 / 6

Start / End Page

  • 3615 - 3619

PubMed ID

  • 8497069

Pubmed Central ID

  • PMC237711

International Standard Serial Number (ISSN)

  • 0022-538X

Digital Object Identifier (DOI)

  • 10.1128/JVI.67.6.3615-3619.1993


  • eng

Conference Location

  • United States